ID TIDC1_HUMAN Reviewed; 285 AA. AC Q9NPL8; D3DN81; Q6IAJ7; Q6UWU6; Q9NPR3; Q9NPS5; Q9P0Y6; DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 2. DT 28-JAN-2026, entry version 160. DE RecName: Full=Complex I assembly factor TIMMDC1, mitochondrial {ECO:0000305}; DE AltName: Full=Protein M5-14; DE AltName: Full=Translocase of inner mitochondrial membrane domain-containing protein 1; DE Short=TIMM domain containing-protein 1; GN Name=TIMMDC1 {ECO:0000312|HGNC:HGNC:1321}; Synonyms=C3orf1; GN ORFNames=UNQ247/PRO284; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], VARIANTS ASP-76 AND ILE-217, AND TISSUE RP SPECIFICITY. RX PubMed=11092749; DOI=10.3109/10425170009033252; RA Escarceller M., Pluvinet R., Sumoy L., Estivill X.; RT "Identification and expression analysis of C3orf1, a novel human gene RT homologous to the Drosophila RP140-upstream gene."; RL DNA Seq. 11:335-338(2000). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Li D.X., Roberts R.; RT "Identification of a novel transcript, M5-14, preferentially expressed in RT cardiac and skeletal muscle."; RL Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX PubMed=12975309; DOI=10.1101/gr.1293003; RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J., RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P., RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A., RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D., RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L., RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C., RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J., RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.; RT "The secreted protein discovery initiative (SPDI), a large-scale effort to RT identify novel human secreted and transmembrane proteins: a bioinformatics RT assessment."; RL Genome Res. 13:2265-2270(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-217. RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=B-cell; 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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] 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., Buerckstuemmer T., RA 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 [9] RP FUNCTION, SUBCELLULAR LOCATION, AND SUBUNIT. RX PubMed=24191001; DOI=10.1073/pnas.1319247110; RA Andrews B., Carroll J., Ding S., Fearnley I.M., Walker J.E.; RT "Assembly factors for the membrane arm of human complex I."; RL Proc. Natl. Acad. Sci. U.S.A. 110:18934-18939(2013). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-277, AND IDENTIFICATION BY RP 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., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [11] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). RN [12] RP INTERACTION WITH TMEM70. RX PubMed=33753518; DOI=10.1073/pnas.2100558118; RA Carroll J., He J., Ding S., Fearnley I.M., Walker J.E.; RT "TMEM70 and TMEM242 help to assemble the rotor ring of human ATP synthase RT and interact with assembly factors for complex I."; RL Proc. Natl. Acad. Sci. U.S.A. 118:0-0(2021). RN [13] RP INVOLVEMENT IN MC1DN31. RX PubMed=28604674; DOI=10.1038/ncomms15824; RA Kremer L.S., Bader D.M., Mertes C., Kopajtich R., Pichler G., Iuso A., RA Haack T.B., Graf E., Schwarzmayr T., Terrile C., Konarikova E., Repp B., RA Kastenmueller G., Adamski J., Lichtner P., Leonhardt C., Funalot B., RA Donati A., Tiranti V., Lombes A., Jardel C., Glaeser D., Taylor R.W., RA Ghezzi D., Mayr J.A., Roetig A., Freisinger P., Distelmaier F., Strom T.M., RA Meitinger T., Gagneur J., Prokisch H.; RT "Genetic diagnosis of Mendelian disorders via RNA sequencing."; RL Nat. Commun. 8:15824-15824(2017). CC -!- FUNCTION: Chaperone protein involved in the assembly of the CC mitochondrial NADH:ubiquinone oxidoreductase complex (complex I). CC Participates in constructing the membrane arm of complex I. CC {ECO:0000269|PubMed:24191001}. CC -!- SUBUNIT: Associates with the intermediate 315 kDa subcomplex of CC incompletely assembled complex I. Interacts with TMEM70 CC (PubMed:33753518). {ECO:0000269|PubMed:24191001, CC ECO:0000269|PubMed:33753518}. CC -!- INTERACTION: CC Q9NPL8; Q8TD06: AGR3; NbExp=3; IntAct=EBI-6268651, EBI-3925742; CC Q9NPL8; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-6268651, EBI-12109402; CC Q9NPL8; P55056: APOC4; NbExp=3; IntAct=EBI-6268651, EBI-18302142; CC Q9NPL8; O95236-2: APOL3; NbExp=3; IntAct=EBI-6268651, EBI-11976321; CC Q9NPL8; Q8N6S5: ARL6IP6; NbExp=3; IntAct=EBI-6268651, EBI-2808844; CC Q9NPL8; Q8WVX3-2: ARLN; NbExp=3; IntAct=EBI-6268651, EBI-12003442; CC Q9NPL8; O75787: ATP6AP2; NbExp=3; IntAct=EBI-6268651, EBI-2512037; CC Q9NPL8; P51572: BCAP31; NbExp=3; IntAct=EBI-6268651, EBI-77683; CC Q9NPL8; Q6UWT4: C5orf46; NbExp=3; IntAct=EBI-6268651, EBI-11986083; CC Q9NPL8; P13236: CCL4; NbExp=3; IntAct=EBI-6268651, EBI-2873970; CC Q9NPL8; O95674: CDS2; NbExp=3; IntAct=EBI-6268651, EBI-3913685; CC Q9NPL8; Q8TAZ6: CMTM2; NbExp=3; IntAct=EBI-6268651, EBI-2339374; CC Q9NPL8; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-6268651, EBI-6942903; CC Q9NPL8; Q9HCS2: CYP4F12; NbExp=3; IntAct=EBI-6268651, EBI-3918831; CC Q9NPL8; Q96PD2-2: DCBLD2; NbExp=3; IntAct=EBI-6268651, EBI-12135455; CC Q9NPL8; Q9NR28: DIABLO; NbExp=3; IntAct=EBI-6268651, EBI-517508; CC Q9NPL8; Q8N682: DRAM1; NbExp=3; IntAct=EBI-6268651, EBI-10305400; CC Q9NPL8; Q6UW88-2: EPGN; NbExp=3; IntAct=EBI-6268651, EBI-17468158; CC Q9NPL8; O75063: FAM20B; NbExp=3; IntAct=EBI-6268651, EBI-11090967; CC Q9NPL8; Q96KR6: FAM210B; NbExp=3; IntAct=EBI-6268651, EBI-18938272; CC Q9NPL8; Q969F0: FATE1; NbExp=4; IntAct=EBI-6268651, EBI-743099; CC Q9NPL8; Q14802-3: FXYD3; NbExp=3; IntAct=EBI-6268651, EBI-12175685; CC Q9NPL8; P29033: GJB2; NbExp=3; IntAct=EBI-6268651, EBI-3905204; CC Q9NPL8; Q8TDV0: GPR151; NbExp=3; IntAct=EBI-6268651, EBI-11955647; CC Q9NPL8; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-6268651, EBI-13345167; CC Q9NPL8; Q8TED1: GPX8; NbExp=3; IntAct=EBI-6268651, EBI-11721746; CC Q9NPL8; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-6268651, EBI-18053395; CC Q9NPL8; P01563: IFNA2; NbExp=3; IntAct=EBI-6268651, EBI-4394394; CC Q9NPL8; Q99706: KIR2DL4; NbExp=3; IntAct=EBI-6268651, EBI-10294579; CC Q9NPL8; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-6268651, EBI-2820517; CC Q9NPL8; Q9NX47: MARCHF5; NbExp=3; IntAct=EBI-6268651, EBI-2341610; CC Q9NPL8; Q5SR56: MFSD14B; NbExp=3; IntAct=EBI-6268651, EBI-373355; CC Q9NPL8; Q6N075: MFSD5; NbExp=3; IntAct=EBI-6268651, EBI-3920969; CC Q9NPL8; Q9NX14: NDUFB11; NbExp=4; IntAct=EBI-6268651, EBI-1246182; CC Q9NPL8; Q92982: NINJ1; NbExp=3; IntAct=EBI-6268651, EBI-2802124; CC Q9NPL8; Q8N912: NRAC; NbExp=3; IntAct=EBI-6268651, EBI-12051377; CC Q9NPL8; P50542-3: PEX5; NbExp=3; IntAct=EBI-6268651, EBI-12181987; CC Q9NPL8; Q07326: PIGF; NbExp=3; IntAct=EBI-6268651, EBI-17180304; CC Q9NPL8; P18031: PTPN1; NbExp=3; IntAct=EBI-6268651, EBI-968788; CC Q9NPL8; Q16849-3: PTPRN; NbExp=3; IntAct=EBI-6268651, EBI-10200782; CC Q9NPL8; Q9Y225-2: RNF24; NbExp=3; IntAct=EBI-6268651, EBI-13044680; CC Q9NPL8; Q8TAC9: SCAMP5; NbExp=3; IntAct=EBI-6268651, EBI-2695784; CC Q9NPL8; O00767: SCD; NbExp=3; IntAct=EBI-6268651, EBI-2684237; CC Q9NPL8; O75920: SERF1B; NbExp=3; IntAct=EBI-6268651, EBI-2115181; CC Q9NPL8; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-6268651, EBI-749270; CC Q9NPL8; Q6ICL7: SLC35E4; NbExp=3; IntAct=EBI-6268651, EBI-12867720; CC Q9NPL8; Q8N357: SLC35F6; NbExp=3; IntAct=EBI-6268651, EBI-713484; CC Q9NPL8; Q96JF0-2: ST6GAL2; NbExp=3; IntAct=EBI-6268651, EBI-12908338; CC Q9NPL8; Q86Y82: STX12; NbExp=3; IntAct=EBI-6268651, EBI-2691717; CC Q9NPL8; O43752: STX6; NbExp=3; IntAct=EBI-6268651, EBI-2695795; CC Q9NPL8; Q7Z5S9: TMEM144; NbExp=3; IntAct=EBI-6268651, EBI-12876358; CC Q9NPL8; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-6268651, EBI-8638294; CC Q9NPL8; Q96HP8: TMEM176A; NbExp=3; IntAct=EBI-6268651, EBI-2800645; CC Q9NPL8; Q969S6: TMEM203; NbExp=3; IntAct=EBI-6268651, EBI-12274070; CC Q9NPL8; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-6268651, EBI-11528917; CC Q9NPL8; Q969K7: TMEM54; NbExp=3; IntAct=EBI-6268651, EBI-3922833; CC Q9NPL8; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-6268651, EBI-6656213; CC Q9NPL8; Q8N2M4: TMEM86A; NbExp=3; IntAct=EBI-6268651, EBI-12015604; CC Q9NPL8; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-6268651, EBI-10243654; CC Q9NPL8; Q9NYZ1: TVP23B; NbExp=3; IntAct=EBI-6268651, EBI-11343401; CC Q9NPL8; Q86WB7-2: UNC93A; NbExp=3; IntAct=EBI-6268651, EBI-13356252; CC Q9NPL8; Q8N511: VMA12; NbExp=3; IntAct=EBI-6268651, EBI-10265825; CC Q9NPL8; O95070: YIF1A; NbExp=3; IntAct=EBI-6268651, EBI-2799703; CC Q9NPL8; Q9Y548: YIPF1; NbExp=3; IntAct=EBI-6268651, EBI-7850136; CC -!- SUBCELLULAR LOCATION: Mitochondrion membrane CC {ECO:0000269|PubMed:24191001}; Multi-pass membrane protein CC {ECO:0000269|PubMed:24191001}. CC -!- TISSUE SPECIFICITY: Generalized expression enhanced in heart and CC skeletal muscle. {ECO:0000269|PubMed:11092749}. CC -!- DISEASE: Mitochondrial complex I deficiency, nuclear type 31 (MC1DN31) CC [MIM:618251]: A form of mitochondrial complex I deficiency, the most CC common biochemical signature of mitochondrial disorders, a group of CC highly heterogeneous conditions characterized by defective oxidative CC phosphorylation, which collectively affects 1 in 5-10000 live births. CC Clinical disorders have variable severity, ranging from lethal neonatal CC disease to adult-onset neurodegenerative disorders. Phenotypes include CC macrocephaly with progressive leukodystrophy, non-specific CC encephalopathy, cardiomyopathy, myopathy, liver disease, Leigh CC syndrome, Leber hereditary optic neuropathy, and some forms of CC Parkinson disease. MC1DN31 transmission pattern is consistent with CC autosomal recessive inheritance. {ECO:0000269|PubMed:28604674}. CC Note=The disease is caused by variants affecting the gene represented CC in this entry. CC -!- SIMILARITY: Belongs to the Tim17/Tim22/Tim23 family. {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; AF210057; AAG43510.1; -; mRNA. DR EMBL; AL390077; CAB98201.1; -; mRNA. DR EMBL; AL390090; CAB98212.1; -; mRNA. DR EMBL; AL390094; CAB98251.1; -; mRNA. DR EMBL; AF139077; AAF62372.1; -; mRNA. DR EMBL; AL136622; CAB66557.1; -; mRNA. DR EMBL; AY358633; AAQ88996.1; -; mRNA. DR EMBL; CR457158; CAG33439.1; -; mRNA. DR EMBL; CR533524; CAG38555.1; -; mRNA. DR EMBL; CH471052; EAW79566.1; -; Genomic_DNA. DR EMBL; CH471052; EAW79568.1; -; Genomic_DNA. DR EMBL; BC012341; AAH12341.1; -; mRNA. DR CCDS; CCDS33831.1; -. DR RefSeq; NP_057673.2; NM_016589.4. DR AlphaFoldDB; Q9NPL8; -. DR BioGRID; 119451; 266. DR FunCoup; Q9NPL8; 2200. DR IntAct; Q9NPL8; 181. DR MINT; Q9NPL8; -. DR STRING; 9606.ENSP00000418803; -. DR iPTMnet; Q9NPL8; -. DR PhosphoSitePlus; Q9NPL8; -. DR SwissPalm; Q9NPL8; -. DR BioMuta; TIMMDC1; -. DR DMDM; 116243026; -. DR jPOST; Q9NPL8; -. DR MassIVE; Q9NPL8; -. DR PaxDb; 9606-ENSP00000418803; -. DR PeptideAtlas; Q9NPL8; -. DR ProteomicsDB; 82035; -. DR Pumba; Q9NPL8; -. DR Antibodypedia; 53806; 35 antibodies from 16 providers. DR DNASU; 51300; -. DR Ensembl; ENST00000494664.6; ENSP00000418803.1; ENSG00000113845.11. DR GeneID; 51300; -. DR KEGG; hsa:51300; -. DR MANE-Select; ENST00000494664.6; ENSP00000418803.1; NM_016589.4; NP_057673.2. DR UCSC; uc003ecn.4; human. DR AGR; HGNC:1321; -. DR ClinPGx; PA25900; -. DR CTD; 51300; -. DR DisGeNET; 51300; -. DR GeneCards; TIMMDC1; -. DR HGNC; HGNC:1321; TIMMDC1. DR HPA; ENSG00000113845; Low tissue specificity. DR MalaCards; TIMMDC1; -. DR MIM; 615534; gene. DR MIM; 618251; phenotype. DR OpenTargets; ENSG00000113845; -. DR Orphanet; 2609; Isolated complex I deficiency. DR VEuPathDB; HostDB:ENSG00000113845; -. DR eggNOG; KOG4608; Eukaryota. DR GeneTree; ENSGT00390000013817; -. DR HOGENOM; CLU_068982_0_0_1; -. DR InParanoid; Q9NPL8; -. DR OMA; SYMNFME; -. DR OrthoDB; 5826189at2759; -. DR PAN-GO; Q9NPL8; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q9NPL8; -. DR PathwayCommons; Q9NPL8; -. DR Reactome; R-HSA-6799198; Complex I biogenesis. DR SignaLink; Q9NPL8; -. DR Agora; ENSG00000113845; -. DR BioGRID-ORCS; 51300; 186 hits in 1168 CRISPR screens. DR ChiTaRS; TIMMDC1; human. DR GeneWiki; C3orf1; -. DR GenomeRNAi; 51300; -. DR Pharos; Q9NPL8; Tbio. DR PRO; PR:Q9NPL8; -. DR Proteomes; UP000005640; Chromosome 3. DR RNAct; Q9NPL8; protein. DR Bgee; ENSG00000113845; Expressed in left ventricle myocardium and 187 other cell types or tissues. DR ExpressionAtlas; Q9NPL8; baseline and differential. DR GO; GO:0005743; C:mitochondrial inner membrane; TAS:Reactome. DR GO; GO:0005739; C:mitochondrion; IDA:LIFEdb. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IEA:InterPro. DR InterPro; IPR055299; TIMMDC1. DR PANTHER; PTHR13002; C3ORF1 PROTEIN-RELATED; 1. DR PANTHER; PTHR13002:SF1; COMPLEX I ASSEMBLY FACTOR TIMMDC1, MITOCHONDRIAL; 1. DR Pfam; PF02466; Tim17; 1. PE 1: Evidence at protein level; KW Chaperone; Membrane; Mitochondrion; Phosphoprotein; KW Primary mitochondrial disease; Proteomics identification; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1..285 FT /note="Complex I assembly factor TIMMDC1, mitochondrial" FT /id="PRO_0000252478" FT TRANSMEM 80..100 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 137..159 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 165..185 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 189..209 FT /note="Helical" FT /evidence="ECO:0000255" FT MOD_RES 277 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT VARIANT 76 FT /note="N -> D (in dbSNP:rs11539377)" FT /evidence="ECO:0000269|PubMed:11092749" FT /id="VAR_027885" FT VARIANT 217 FT /note="V -> I (in dbSNP:rs57168946)" FT /evidence="ECO:0000269|PubMed:11092749, ECO:0000269|Ref.5" FT /id="VAR_061572" FT CONFLICT 156 FT /note="L -> P (in Ref. 5; CAG33439)" FT /evidence="ECO:0000305" FT CONFLICT 213 FT /note="S -> A (in Ref. 4; AAQ88996)" FT /evidence="ECO:0000305" FT CONFLICT 255 FT /note="Q -> R (in Ref. 4; AAQ88996)" FT /evidence="ECO:0000305" SQ SEQUENCE 285 AA; 32178 MW; 5AA6474C3ABCCFA2 CRC64; MEVPPPAPRS FLCRALCLFP RVFAAEAVTA DSEVLEERQK RLPYVPEPYY PESGWDRLRE LFGKDEQQRI SKDLANICKT AATAGIIGWV YGGIPAFIHA KQQYIEQSQA EIYHNRFDAV QSAHRAATRG FIRYGWRWGW RTAVFVTIFN TVNTSLNVYR NKDALSHFVI AGAVTGSLFR INVGLRGLVA GGIIGALLGT PVGGLLMAFQ KYSGETVQER KQKDRKALHE LKLEEWKGRL QVTEHLPEKI ESSLQEDEPE NDAKKIEALL NLPRNPSVID KQDKD //