ID S39AE_HUMAN Reviewed; 492 AA. AC Q15043; A6NH98; B4DIW3; B6EU88; D3DSR4; Q6ZME8; Q96BB3; DT 04-DEC-2007, integrated into UniProtKB/Swiss-Prot. DT 30-NOV-2010, sequence version 3. DT 12-SEP-2018, entry version 136. DE RecName: Full=Zinc transporter ZIP14; DE AltName: Full=LIV-1 subfamily of ZIP zinc transporter 4; DE Short=LZT-Hs4; DE AltName: Full=Solute carrier family 39 member 14; DE AltName: Full=Zrt- and Irt-like protein 14; DE Short=ZIP-14; DE Flags: Precursor; GN Name=SLC39A14; Synonyms=KIAA0062, ZIP14; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE RP SPECIFICITY. RC TISSUE=Bone marrow; RX PubMed=7584044; DOI=10.1093/dnares/1.5.223; RA Nomura N., Nagase T., Miyajima N., Sazuka T., Tanaka A., Sato S., RA Seki N., Kawarabayasi Y., Ishikawa K., Tabata S.; RT "Prediction of the coding sequences of unidentified human genes. II. RT The coding sequences of 40 new genes (KIAA0041-KIAA0080) deduced by RT analysis of cDNA clones from human cell line KG-1."; RL DNA Res. 1:223-229(1994). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3). RC TISSUE=Hippocampus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., RA Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., RA Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., RA Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T., RA Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K., RA DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G., RA Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B., RA Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., RA O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K., RA Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., RA Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K., RA Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q., RA Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N., RA Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP PRO-33. RC TISSUE=Colon; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP SUBUNIT, AND SUBCELLULAR LOCATION. RX PubMed=12659941; DOI=10.1016/S0005-2736(03)00048-8; RA Taylor K.M., Nicholson R.I.; RT "The LZT proteins; the LIV-1 subfamily of zinc transporters."; RL Biochim. Biophys. Acta 1611:16-30(2003). RN [7] RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND FUNCTION. RX PubMed=15642354; DOI=10.1016/j.febslet.2004.12.006; RA Taylor K.M., Morgan H.E., Johnson A., Nicholson R.I.; RT "Structure-function analysis of a novel member of the LIV-1 subfamily RT of zinc transporters, ZIP14."; RL FEBS Lett. 579:427-432(2005). RN [8] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-77. RC TISSUE=Liver; RX PubMed=19159218; DOI=10.1021/pr8008012; RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.; RT "Glycoproteomics analysis of human liver tissue by combination of RT multiple enzyme digestion and hydrazide chemistry."; RL J. Proteome Res. 8:651-661(2009). RN [9] RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-77 AND ASN-102. RC TISSUE=Leukemic T-cell; RX PubMed=19349973; DOI=10.1038/nbt.1532; RA Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M., RA Schiess R., Aebersold R., Watts J.D.; RT "Mass-spectrometric identification and relative quantification of N- RT linked cell surface glycoproteins."; RL Nat. Biotechnol. 27:378-386(2009). RN [10] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., RA Wang L., Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human RT liver phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [12] RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INVOLVEMENT IN RP HMNDYT2, VARIANTS HMNDYT2 VAL-98; ARG-383 AND LYS-469, AND RP CHARACTERIZATION OF VARIANTS HMNDYT2 VAL-98; ARG-383 AND LYS-469. RX PubMed=27231142; DOI=10.1038/ncomms11601; RA Tuschl K., Meyer E., Valdivia L.E., Zhao N., Dadswell C., RA Abdul-Sada A., Hung C.Y., Simpson M.A., Chong W.K., Jacques T.S., RA Woltjer R.L., Eaton S., Gregory A., Sanford L., Kara E., Houlden H., RA Cuno S.M., Prokisch H., Valletta L., Tiranti V., Younis R., RA Maher E.R., Spencer J., Straatman-Iwanowska A., Gissen P., Selim L.A., RA Pintos-Morell G., Coroleu-Lletget W., Mohammad S.S., Yoganathan S., RA Dale R.C., Thomas M., Rihel J., Bodamer O.A., Enns C.A., RA Hayflick S.J., Clayton P.T., Mills P.B., Kurian M.A., Wilson S.W.; RT "Mutations in SLC39A14 disrupt manganese homeostasis and cause RT childhood-onset parkinsonism-dystonia."; RL Nat. Commun. 7:11601-11601(2016). CC -!- FUNCTION: Broad-scope metal ion transporter with a preference for CC zinc uptake. Also mediates cellular uptake of nontransferrin-bound CC iron. {ECO:0000269|PubMed:15642354, ECO:0000269|PubMed:27231142}. CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12659941}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:27231142}; CC Multi-pass membrane protein {ECO:0000255}. Cytoplasm CC {ECO:0000269|PubMed:27231142}. Cell projection, lamellipodium CC {ECO:0000269|PubMed:12659941, ECO:0000269|PubMed:15642354}. CC Note=Localized to the plasma membrane and also found colocalized CC with F-actin concentrated on lamellipodiae. CC {ECO:0000269|PubMed:12659941, ECO:0000269|PubMed:15642354, CC ECO:0000269|PubMed:27231142}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q15043-1; Sequence=Displayed; CC Name=2; CC IsoId=Q15043-2; Sequence=VSP_029728; CC Note=No experimental confirmation available.; CC Name=3; CC IsoId=Q15043-3; Sequence=VSP_040139; CC -!- TISSUE SPECIFICITY: Expressed in liver and in brain by large CC neurons in the globus pallidus, the insular cortex and the dentate CC nucleus and to a lower extent in the putamen and the caudate CC nucleus (at protein level) (PubMed:27231142). Isoform 1 is CC ubiquitously expressed, with increased expression in liver, CC pancreas, fetal liver, thyroid gland, left and right ventricle, CC right atrium and fetal heart. Weakly expressed in spleen, thymus, CC and peripheral blood leukocytes (PubMed:15642354, PubMed:7584044, CC PubMed:27231142). Isoform 3 is widely expressed but not detected CC in brain, heart, skeletal muscle and fetal skin (PubMed:27231142). CC {ECO:0000269|PubMed:15642354, ECO:0000269|PubMed:27231142, CC ECO:0000269|PubMed:7584044}. CC -!- DISEASE: Hypermanganesemia with dystonia 2 (HMNDYT2) [MIM:617013]: CC A metabolic autosomal recessive disorder characterized by CC increased blood manganese levels, neurodegeneration, and rapidly CC progressive parkinsonism and dystonia. Affected individuals CC present with loss of developmental milestones, progressive CC dystonia and bulbar dysfunction in infancy or early childhood. CC Towards the end of the first decade, they manifest severe CC generalized pharmacoresistant dystonia, spasticity, limb CC contractures and scoliosis, and loss of independent ambulation. CC Cognition may be impaired, but is better preserved than motor CC function. {ECO:0000269|PubMed:27231142}. Note=The disease is CC caused by mutations affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the ZIP transporter (TC 2.A.5) family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA06685.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC ----------------------------------------------------------------------- DR EMBL; D31887; BAA06685.1; ALT_INIT; mRNA. DR EMBL; AK172810; BAD18780.1; -; mRNA. DR EMBL; AK295807; BAG58625.1; -; mRNA. DR EMBL; AC087854; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC105910; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471080; EAW63681.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63682.1; -; Genomic_DNA. DR EMBL; CH471080; EAW63683.1; -; Genomic_DNA. DR EMBL; BC015770; AAH15770.1; -; mRNA. DR CCDS; CCDS47822.1; -. [Q15043-2] DR CCDS; CCDS47823.1; -. [Q15043-1] DR CCDS; CCDS6030.1; -. [Q15043-3] DR RefSeq; NP_001121903.1; NM_001128431.2. [Q15043-1] DR RefSeq; NP_001128625.1; NM_001135153.1. [Q15043-1] DR RefSeq; NP_056174.2; NM_015359.4. [Q15043-3] DR RefSeq; XP_005273522.1; XM_005273465.2. [Q15043-1] DR RefSeq; XP_005273523.1; XM_005273466.4. [Q15043-1] DR RefSeq; XP_006716387.1; XM_006716324.2. [Q15043-1] DR RefSeq; XP_011542780.1; XM_011544478.2. [Q15043-1] DR RefSeq; XP_016868783.1; XM_017013294.1. [Q15043-1] DR RefSeq; XP_016868784.1; XM_017013295.1. [Q15043-1] DR UniGene; Hs.491232; -. DR ProteinModelPortal; Q15043; -. DR SMR; Q15043; -. DR BioGrid; 117063; 5. DR IntAct; Q15043; 10. DR STRING; 9606.ENSP00000289952; -. DR TCDB; 2.A.5.4.5; the zinc (zn(2+))-iron (fe(2+)) permease (zip) family. DR iPTMnet; Q15043; -. DR PhosphoSitePlus; Q15043; -. DR BioMuta; SLC39A14; -. DR DMDM; 313104191; -. DR EPD; Q15043; -. DR MaxQB; Q15043; -. DR PaxDb; Q15043; -. DR PeptideAtlas; Q15043; -. DR PRIDE; Q15043; -. DR ProteomicsDB; 60392; -. DR ProteomicsDB; 60393; -. [Q15043-2] DR ProteomicsDB; 60394; -. [Q15043-3] DR DNASU; 23516; -. DR Ensembl; ENST00000240095; ENSP00000240095; ENSG00000104635. [Q15043-2] DR Ensembl; ENST00000289952; ENSP00000289952; ENSG00000104635. [Q15043-1] DR Ensembl; ENST00000359741; ENSP00000352779; ENSG00000104635. [Q15043-3] DR Ensembl; ENST00000381237; ENSP00000370635; ENSG00000104635. [Q15043-1] DR GeneID; 23516; -. DR KEGG; hsa:23516; -. DR UCSC; uc003xbp.5; human. [Q15043-1] DR CTD; 23516; -. DR DisGeNET; 23516; -. DR EuPathDB; HostDB:ENSG00000104635.13; -. DR GeneCards; SLC39A14; -. DR HGNC; HGNC:20858; SLC39A14. DR HPA; HPA016508; -. DR MalaCards; SLC39A14; -. DR MIM; 608736; gene. DR MIM; 617013; phenotype. DR neXtProt; NX_Q15043; -. DR OpenTargets; ENSG00000104635; -. DR PharmGKB; PA134863701; -. DR eggNOG; KOG2693; Eukaryota. DR eggNOG; COG0428; LUCA. DR GeneTree; ENSGT00760000119115; -. DR HOGENOM; HOG000070225; -. DR HOVERGEN; HBG108450; -. DR InParanoid; Q15043; -. DR KO; K14720; -. DR OMA; CCCYLGM; -. DR OrthoDB; EOG091G064Y; -. DR PhylomeDB; Q15043; -. DR TreeFam; TF318470; -. DR Reactome; R-HSA-442380; Zinc influx into cells by the SLC39 gene family. DR ChiTaRS; SLC39A14; human. DR GenomeRNAi; 23516; -. DR PRO; PR:Q15043; -. DR Proteomes; UP000005640; Chromosome 8. DR Bgee; ENSG00000104635; Expressed in 227 organ(s), highest expression level in right lobe of liver. DR CleanEx; HS_SLC39A14; -. DR ExpressionAtlas; Q15043; baseline and differential. DR Genevisible; Q15043; HS. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0016021; C:integral component of membrane; IDA:BHF-UCL. DR GO; GO:0005887; C:integral component of plasma membrane; IDA:BHF-UCL. DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell. DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB. DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IEA:Ensembl. DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IDA:UniProtKB. DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IDA:BHF-UCL. DR GO; GO:0006882; P:cellular zinc ion homeostasis; IDA:BHF-UCL. DR GO; GO:0071578; P:zinc ion import across plasma membrane; IDA:BHF-UCL. DR GO; GO:0071577; P:zinc ion transmembrane transport; IDA:BHF-UCL. DR InterPro; IPR003689; ZIP. DR Pfam; PF02535; Zip; 1. PE 1: Evidence at protein level; KW Alternative splicing; Cell membrane; Cell projection; KW Complete proteome; Cytoplasm; Disease mutation; Dystonia; KW Glycoprotein; Ion transport; Membrane; Neurodegeneration; KW Parkinsonism; Polymorphism; Reference proteome; Signal; Transmembrane; KW Transmembrane helix; Transport; Zinc; Zinc transport. FT SIGNAL 1 30 {ECO:0000255}. FT CHAIN 31 492 Zinc transporter ZIP14. FT /FTId=PRO_0000312194. FT TOPO_DOM 31 157 Extracellular. {ECO:0000255}. FT TRANSMEM 158 178 Helical. {ECO:0000255}. FT TOPO_DOM 179 186 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 187 207 Helical. {ECO:0000255}. FT TOPO_DOM 208 224 Extracellular. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TOPO_DOM 246 397 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 398 418 Helical. {ECO:0000255}. FT TOPO_DOM 419 424 Extracellular. {ECO:0000255}. FT TRANSMEM 425 445 Helical. {ECO:0000255}. FT TOPO_DOM 446 460 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 461 481 Helical. {ECO:0000255}. FT TOPO_DOM 482 492 Extracellular. {ECO:0000255}. FT MOTIF 251 258 HHHGHXHX-motif. FT MOTIF 376 381 XEXPHE-motif. FT CARBOHYD 77 77 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19159218, FT ECO:0000269|PubMed:19349973}. FT CARBOHYD 102 102 N-linked (GlcNAc...) asparagine. FT {ECO:0000269|PubMed:19349973}. FT VAR_SEQ 156 199 YGLLCVTVISLCSLLGASVVPFMKKTFYKRLLLYFIALAIG FT TLY -> FGFLSVSLINLASLLGVLVLPCTEKAFFSRVLTY FT FIALSIGTLL (in isoform 3). FT {ECO:0000303|PubMed:14702039}. FT /FTId=VSP_040139. FT VAR_SEQ 445 492 FPEMNEVCQEDERKGSILIPFIIQNLGLLTGFTIMVVLTMY FT SGQIQIG -> MEFCSVAQAGVQWCHLSSLQPLPLGLKRLS FT CLSLPSN (in isoform 2). FT {ECO:0000303|PubMed:15489334}. FT /FTId=VSP_029728. FT VARIANT 33 33 L -> P (in dbSNP:rs896378). FT {ECO:0000269|PubMed:15489334}. FT /FTId=VAR_037450. FT VARIANT 98 98 F -> V (in HMNDYT2; no effect on protein FT abundance; no effect on subcellular FT localization at the plasma membrane and FT within the cytoplasm; decreased manganese FT ion transmembrane transporter activity; FT dbSNP:rs879253763). FT {ECO:0000269|PubMed:27231142}. FT /FTId=VAR_077004. FT VARIANT 383 383 G -> R (in HMNDYT2; no effect on protein FT abundance; no effect on subcellular FT localization at the plasma membrane and FT within the cytoplasm; decreased manganese FT ion transmembrane transporter activity; FT dbSNP:rs879253766). FT {ECO:0000269|PubMed:27231142}. FT /FTId=VAR_077005. FT VARIANT 469 469 N -> K (in HMNDYT2; no effect on protein FT abundance; no effect on subcellular FT localization at the plasma membrane and FT within the cytoplasm; decreased manganese FT ion transmembrane transporter activity; FT dbSNP:rs750281602). FT {ECO:0000269|PubMed:27231142}. FT /FTId=VAR_077006. FT CONFLICT 57 57 L -> P (in Ref. 2; BAD18780). FT {ECO:0000305}. FT CONFLICT 314 314 D -> G (in Ref. 2; BAG58625). FT {ECO:0000305}. FT CONFLICT 380 380 H -> R (in Ref. 2; BAD18780). FT {ECO:0000305}. SQ SEQUENCE 492 AA; 54212 MW; F2ACE1DA4656A5F0 CRC64; MKLLLLHPAF QSCLLLTLLG LWRTTPEAHA SSLGAPAISA ASFLQDLIHR YGEGDSLTLQ QLKALLNHLD VGVGRGNVTQ HVQGHRNLST CFSSGDLFTA HNFSEQSRIG SSELQEFCPT ILQQLDSRAC TSENQENEEN EQTEEGRPSA VEVWGYGLLC VTVISLCSLL GASVVPFMKK TFYKRLLLYF IALAIGTLYS NALFQLIPEA FGFNPLEDYY VSKSAVVFGG FYLFFFTEKI LKILLKQKNE HHHGHSHYAS ESLPSKKDQE EGVMEKLQNG DLDHMIPQHC SSELDGKAPM VDEKVIVGSL SVQDLQASQS ACYWLKGVRY SDIGTLAWMI TLSDGLHNFI DGLAIGASFT VSVFQGISTS VAILCEEFPH ELGDFVILLN AGMSIQQALF FNFLSACCCY LGLAFGILAG SHFSANWIFA LAGGMFLYIS LADMFPEMNE VCQEDERKGS ILIPFIIQNL GLLTGFTIMV VLTMYSGQIQ IG //