ID MSMB_HUMAN Reviewed; 114 AA. AC P08118; B1API6; P11999; Q13125; Q6IAY9; Q9UC59; DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot. DT 01-AUG-1988, sequence version 1. DT 28-JAN-2026, entry version 207. DE RecName: Full=Beta-microseminoprotein; DE AltName: Full=Immunoglobulin-binding factor; DE Short=IGBF; DE AltName: Full=PN44; DE AltName: Full=Prostate secreted seminal plasma protein; DE AltName: Full=Prostate secretory protein of 94 amino acids; DE Short=PSP-94; DE Short=PSP94; DE AltName: Full=Seminal plasma beta-inhibin; DE Flags: Precursor; GN Name=MSMB; Synonyms=PRSP; 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] (ISOFORM PSP94). RX PubMed=3829888; DOI=10.1089/dna.1987.6.23; RA Mbikay M., Nolet S., Fournier S., Benjannet S., Chapdelaine P., Paradis G., RA Dube J.Y., Tremblay R., Lazure C., Seidah N.G., Chretien M.; RT "Molecular cloning and sequence of the cDNA for a 94-amino-acid seminal RT plasma protein secreted by the human prostate."; RL DNA 6:23-29(1987). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSP94). RX PubMed=2590204; DOI=10.1016/0006-291x(89)91812-3; RA Ulvsbaeck M., Lindstroem C., Weiber H., Abrahamsson P.-A., Lilja H., RA Lundwall A.; RT "Molecular cloning of a small prostate protein, known as beta- RT microseminoprotein, PSP94 or beta-inhibin, and demonstration of transcripts RT in non-genital tissues."; RL Biochem. Biophys. Res. Commun. 164:1310-1315(1989). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2322265; DOI=10.1016/0006-291x(90)90648-7; RA Green C.B., Liu W.Y., Kwok S.C.M.; RT "Cloning and nucleotide sequence analysis of the human beta- RT microseminoprotein gene."; RL Biochem. Biophys. Res. Commun. 167:1184-1190(1990). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=2054385; DOI=10.1016/0167-4781(91)90016-f; RA Nolet S., Mbikay M., Chretien M.; RT "Prostatic secretory protein PSP94: gene organization and promoter sequence RT in rhesus monkey and human."; RL Biochim. Biophys. Acta 1089:247-249(1991). RN [5] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSP94). RC TISSUE=Prostate; RX PubMed=7506990; DOI=10.1016/0304-3835(93)90049-f; RA Liu A.Y., Bradner R.C., Vessella R.L.; RT "Decreased expression of prostatic secretory protein PSP94 in prostate RT cancer."; RL Cancer Lett. 74:91-99(1993). RN [6] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSP57), AND TISSUE SPECIFICITY. RC TISSUE=Prostate; RX PubMed=7566962; RA Xuan J.W., Chin J.L., Guo Y., Chambers A.F., Finkelman M.A., Clarke M.W.; RT "Alternative splicing of PSP94 (prostatic secretory protein of 94 amino RT acids) mRNA in prostate tissue."; RL Oncogene 11:1041-1047(1995). RN [7] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM PSP94). RA Baijal-Gupta M., Clarke M.W.; RT "Prostate specific protein (PSP94) expression in a human endometrial cell RT line (KLE)."; RL Submitted (DEC-1996) to the EMBL/GenBank/DDBJ databases. RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PSP94). RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., RA Phelan M., Farmer A.; RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PSP94). 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 [10] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15164054; DOI=10.1038/nature02462; RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P., RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.; RT "The DNA sequence and comparative analysis of human chromosome 10."; RL Nature 429:375-381(2004). RN [11] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM PSP94). RC TISSUE=Prostate; 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 [12] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 2-72. RX PubMed=10491085; DOI=10.1046/j.1432-1327.1999.00614.x; RA Maekinen M., Valtonen-Andre C., Lundwall A.; RT "New world, but not old world, monkeys carry several genes encoding beta- RT microseminoprotein."; RL Eur. J. Biochem. 264:407-414(1999). RN [13] RP PROTEIN SEQUENCE OF 21-113. RX PubMed=3995056; DOI=10.1016/0167-4838(85)90200-6; RA Akiyama K., Yoshioka Y., Schmid K., Offner G.D., Troxler R.F., Tsuda R., RA Hara M.; RT "The amino acid sequence of human beta-microseminoprotein."; RL Biochim. Biophys. Acta 829:288-294(1985). RN [14] RP PROTEIN SEQUENCE OF 21-114. RX PubMed=6434350; DOI=10.1016/0014-5793(84)80766-8; RA Seidah N.G., Arbatti N.J., Rochemont J., Sheth A.R., Chretien M.; RT "Complete amino acid sequence of human seminal plasma beta-inhibin. RT Prediction of post Gln-Arg cleavage as a maturation site."; RL FEBS Lett. 175:349-355(1984). RN [15] RP PROTEIN SEQUENCE OF 21-50 AND 113-114. RX PubMed=1930232; DOI=10.1016/s0006-291x(05)81300-2; RA Liang Z.G., Kamada M., Koide S.S.; RT "Structural identity of immunoglobulin binding factor and prostatic RT secretory protein of human seminal plasma."; RL Biochem. Biophys. Res. Commun. 180:356-359(1991). RN [16] RP PROTEIN SEQUENCE OF 21-41, AND TISSUE SPECIFICITY. RC TISSUE=Semen; RX PubMed=7671139; DOI=10.1016/1357-2725(95)00021-g; RA Ohkubo I., Tada T., Ochiai Y., Ueyama H., Eimoto T., Sasaki M.; RT "Human seminal plasma beta-microseminoprotein: its purification, RT characterization, and immunohistochemical localization."; RL Int. J. Biochem. Cell Biol. 27:603-611(1995). RN [17] RP PROTEIN SEQUENCE OF 21-32. RX PubMed=11788998; RX DOI=10.1002/1615-9861(200201)2:1<112::aid-prot112>3.3.co;2-e; RA Ghafouri B., Stahlbom B., Tagesson C., Lindahl M.; RT "Newly identified proteins in human nasal lavage fluid from non-smokers and RT smokers using two-dimensional gel electrophoresis and peptide mass RT fingerprinting."; RL Proteomics 2:112-120(2002). RN [18] RP INTERACTION WITH PI16. RX PubMed=15344909; DOI=10.1042/bj20040290; RA Reeves J.R., Xuan J.W., Arfanis K., Morin C., Garde S.V., Ruiz M.T., RA Wisniewski J., Panchal C., Tanner J.E.; RT "Identification, purification and characterization of a novel human blood RT protein with binding affinity for prostate secretory protein of 94 amino RT acids."; RL Biochem. J. 385:105-114(2005). RN [19] RP INVOLVEMENT IN SUSCEPTIBILITY TO HEREDITARY PROSTATE CANCER. RX PubMed=18264096; DOI=10.1038/ng.91; RA Thomas G., Jacobs K.B., Yeager M., Kraft P., Wacholder S., Orr N., Yu K., RA Chatterjee N., Welch R., Hutchinson A., Crenshaw A., Cancel-Tassin G., RA Staats B.J., Wang Z., Gonzalez-Bosquet J., Fang J., Deng X., Berndt S.I., RA Calle E.E., Feigelson H.S., Thun M.J., Rodriguez C., Albanes D., RA Virtamo J., Weinstein S., Schumacher F.R., Giovannucci E., Willett W.C., RA Cussenot O., Valeri A., Andriole G.L., Crawford E.D., Tucker M., RA Gerhard D.S., Fraumeni J.F. Jr., Hoover R., Hayes R.B., Hunter D.J., RA Chanock S.J.; RT "Multiple loci identified in a genome-wide association study of prostate RT cancer."; RL Nat. Genet. 40:310-315(2008). RN [20] RP INVOLVEMENT IN SUSCEPTIBILITY TO HEREDITARY PROSTATE CANCER. RX PubMed=22887727; DOI=10.1002/humu.22176; RA Fitzgerald L.M., Zhang X., Kolb S., Kwon E.M., Liew Y.C., Hurtado-Coll A., RA Knudsen B.S., Ostrander E.A., Stanford J.L.; RT "Investigation of the relationship between prostate cancer and MSMB and RT NCOA4 genetic variants and protein expression."; RL Hum. Mutat. 34:149-156(2013). RN [21] RP STRUCTURE BY NMR OF 21-114, AND DISULFIDE BONDS. RX PubMed=16930619; DOI=10.1016/j.jmb.2006.07.029; RA Ghasriani H., Teilum K., Johnsson Y., Fernlund P., Drakenberg T.; RT "Solution structures of human and porcine beta-microseminoprotein."; RL J. Mol. Biol. 362:502-515(2006). RN [22] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 21-114, SUBUNIT, AND DISULFIDE RP BONDS. RX PubMed=20184897; DOI=10.1016/j.jmb.2010.02.035; RA Kumar A., Jagtap D.D., Mahale S.D., Kumar M.; RT "Crystal structure of prostate secretory protein PSP94 shows an edge-to- RT edge association of two monomers to form a homodimer."; RL J. Mol. Biol. 397:947-956(2010). CC -!- SUBUNIT: Homodimer; Interacts with PI16. {ECO:0000269|PubMed:15344909, CC ECO:0000269|PubMed:20184897}. CC -!- INTERACTION: CC P08118; O43765: SGTA; NbExp=3; IntAct=EBI-10195681, EBI-347996; CC -!- SUBCELLULAR LOCATION: Secreted. Note=Sperm surface. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=PSP94; CC IsoId=P08118-1; Sequence=Displayed; CC Name=PSP57; CC IsoId=P08118-2; Sequence=VSP_003275, VSP_003276; CC -!- TISSUE SPECIFICITY: Strongly expressed in prostate, liver, kidney, CC breast and penis. Also expressed in pancreas, esophagus, stomach, CC deodenum, colon, trachea, lung, salivary glands and fallopian tube. CC PSP94 is expressed in lung and breast, whereas PSP57 is found in kidney CC and bladder. {ECO:0000269|PubMed:7566962, ECO:0000269|PubMed:7671139}. CC -!- DISEASE: Prostate cancer, hereditary, 13 (HPC13) [MIM:611928]: A CC condition associated with familial predisposition to cancer of the CC prostate. Most prostate cancers are adenocarcinomas that develop in the CC acini of the prostatic ducts. Other rare histopathologic types of CC prostate cancer that occur in approximately 5% of patients include CC small cell carcinoma, mucinous carcinoma, prostatic ductal carcinoma, CC transitional cell carcinoma, squamous cell carcinoma, basal cell CC carcinoma, adenoid cystic carcinoma (basaloid), signet-ring cell CC carcinoma and neuroendocrine carcinoma. Note=Disease susceptibility is CC associated with variants affecting the gene represented in this entry. CC -!- MISCELLANEOUS: Specific receptors for this protein are found on CC spermatozoa and in the prostate. CC -!- SIMILARITY: Belongs to the beta-microseminoprotein family. CC {ECO:0000305}. CC -!- CAUTION: Was originally thought to inhibit the secretion of FSH by CC pituitary cells. {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; M15885; AAA36635.1; -; mRNA. DR EMBL; M34376; AAA59871.1; -; Genomic_DNA. DR EMBL; M34373; AAA59871.1; JOINED; Genomic_DNA. DR EMBL; M34374; AAA59871.1; JOINED; Genomic_DNA. DR EMBL; M34375; AAA59871.1; JOINED; Genomic_DNA. DR EMBL; X57928; CAA41002.1; -; Genomic_DNA. DR EMBL; X57929; CAA41002.1; JOINED; Genomic_DNA. DR EMBL; X57930; CAA41002.1; JOINED; Genomic_DNA. DR EMBL; X57931; CAA41002.1; JOINED; Genomic_DNA. DR EMBL; S67815; AAB29732.1; -; mRNA. DR EMBL; U22178; AAA83556.1; -; mRNA. DR EMBL; U78976; AAB37355.1; -; mRNA. DR EMBL; BT006816; AAP35462.1; -; mRNA. DR EMBL; CR457015; CAG33296.1; -; mRNA. DR EMBL; AL450342; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005257; AAH05257.1; -; mRNA. DR EMBL; AJ133356; CAB39325.1; -; Genomic_DNA. DR CCDS; CCDS73095.1; -. [P08118-2] DR CCDS; CCDS73096.1; -. [P08118-1] DR PIR; A34567; A34567. DR PIR; G01730; G01730. DR RefSeq; NP_002434.1; NM_002443.4. [P08118-1] DR RefSeq; NP_619540.1; NM_138634.3. [P08118-2] DR PDB; 2IZ3; NMR; -; A=21-114. DR PDB; 3IX0; X-ray; 2.30 A; A/B/C/D=21-114. DR PDBsum; 2IZ3; -. DR PDBsum; 3IX0; -. DR AlphaFoldDB; P08118; -. DR BMRB; P08118; -. DR SMR; P08118; -. DR BioGRID; 110583; 65. DR FunCoup; P08118; 65. DR IntAct; P08118; 36. DR MINT; P08118; -. DR STRING; 9606.ENSP00000463092; -. DR iPTMnet; P08118; -. DR PhosphoSitePlus; P08118; -. DR BioMuta; MSMB; -. DR DMDM; 131436; -. DR MassIVE; P08118; -. DR PaxDb; 9606-ENSP00000463092; -. DR PeptideAtlas; P08118; -. DR ProteomicsDB; 52068; -. [P08118-1] DR ProteomicsDB; 52069; -. [P08118-2] DR Antibodypedia; 72459; 774 antibodies from 31 providers. DR DNASU; 4477; -. DR Ensembl; ENST00000581478.5; ENSP00000462641.1; ENSG00000263639.7. [P08118-2] DR Ensembl; ENST00000582163.3; ENSP00000463092.1; ENSG00000263639.7. [P08118-1] DR GeneID; 4477; -. DR KEGG; hsa:4477; -. DR MANE-Select; ENST00000582163.3; ENSP00000463092.1; NM_002443.4; NP_002434.1. DR UCSC; uc001jiq.5; human. [P08118-1] DR AGR; HGNC:7372; -. DR ClinPGx; PA31177; -. DR CTD; 4477; -. DR DisGeNET; 4477; -. DR GeneCards; MSMB; -. DR HGNC; HGNC:7372; MSMB. DR HPA; ENSG00000263639; Tissue enriched (prostate). DR MalaCards; MSMB; -. DR MIM; 157145; gene. DR MIM; 611928; phenotype. DR OpenTargets; ENSG00000263639; -. DR Orphanet; 1331; Familial prostate cancer. DR VEuPathDB; HostDB:ENSG00000263639; -. DR eggNOG; ENOG502SF48; Eukaryota. DR GeneTree; ENSGT00940000154371; -. DR HOGENOM; CLU_2637379_0_0_1; -. DR InParanoid; P08118; -. DR OMA; ETEIICC; -. DR OrthoDB; 6076852at2759; -. DR PAN-GO; P08118; 0 GO annotations based on evolutionary models. DR PhylomeDB; P08118; -. DR PathwayCommons; P08118; -. DR SignaLink; P08118; -. DR Agora; ENSG00000263639; -. DR BioGRID-ORCS; 4477; 20 hits in 1133 CRISPR screens. DR ChiTaRS; MSMB; human. DR EvolutionaryTrace; P08118; -. DR GeneWiki; MSMB; -. DR GenomeRNAi; 4477; -. DR Pharos; P08118; Tbio. DR PRO; PR:P08118; -. DR Proteomes; UP000005640; Chromosome 10. DR RNAct; P08118; protein. DR Bgee; ENSG00000263639; Expressed in trachea and 123 other cell types or tissues. DR ExpressionAtlas; P08118; baseline and differential. DR GO; GO:0005615; C:extracellular space; TAS:ProtInc. DR GO; GO:0005634; C:nucleus; TAS:ProtInc. DR FunFam; 2.10.70.10:FF:000137; Beta-microseminoprotein; 1. DR FunFam; 2.20.25.590:FF:000001; Beta-microseminoprotein; 1. DR Gene3D; 2.20.25.590; -; 1. DR Gene3D; 2.10.70.10; Complement Module, domain 1; 1. DR InterPro; IPR008735; PSP94. DR PANTHER; PTHR10500; BETA-MICROSEMINOPROTEIN; 1. DR PANTHER; PTHR10500:SF8; BETA-MICROSEMINOPROTEIN; 1. DR Pfam; PF05825; PSP94; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Direct protein sequencing; KW Disulfide bond; Proteomics identification; Reference proteome; Secreted; KW Signal. FT SIGNAL 1..20 FT /evidence="ECO:0000269|PubMed:11788998, FT ECO:0000269|PubMed:1930232, ECO:0000269|PubMed:3995056, FT ECO:0000269|PubMed:6434350, ECO:0000269|PubMed:7671139" FT CHAIN 21..114 FT /note="Beta-microseminoprotein" FT /id="PRO_0000019268" FT DISULFID 22..70 FT /evidence="ECO:0000269|PubMed:20184897" FT DISULFID 38..62 FT /evidence="ECO:0000269|PubMed:20184897" FT DISULFID 57..93 FT /evidence="ECO:0000269|PubMed:20184897" FT DISULFID 60..69 FT /evidence="ECO:0000269|PubMed:20184897" FT DISULFID 84..107 FT VAR_SEQ 37..77 FT /note="KCMDLKGNKHPINSEWQTDNCETCTCYETEISCCTLVSTPV -> MFLHLWV FT MTKTTAKESSRRRTASISWWRRRTQKRPVLSVNG (in isoform PSP57)" FT /evidence="ECO:0000303|PubMed:7566962" FT /id="VSP_003275" FT VAR_SEQ 78..114 FT /note="Missing (in isoform PSP57)" FT /evidence="ECO:0000303|PubMed:7566962" FT /id="VSP_003276" FT VARIANT 17 FT /note="L -> S (in dbSNP:rs1804776)" FT /id="VAR_011935" FT VARIANT 25 FT /note="I -> M (in dbSNP:rs1804778)" FT /id="VAR_011936" FT VARIANT 52 FT /note="W -> R (in dbSNP:rs1804780)" FT /id="VAR_011937" FT VARIANT 53 FT /note="Q -> R (in dbSNP:rs1804468)" FT /id="VAR_011938" FT VARIANT 80 FT /note="D -> A (in dbSNP:rs1802774)" FT /id="VAR_011939" FT VARIANT 87 FT /note="I -> T (in dbSNP:rs1802771)" FT /id="VAR_011940" FT VARIANT 91 FT /note="E -> G (in dbSNP:rs1804469)" FT /id="VAR_011941" FT VARIANT 92 FT /note="D -> G (in dbSNP:rs1804461)" FT /id="VAR_011942" FT VARIANT 98 FT /note="V -> L (in dbSNP:rs1804464)" FT /id="VAR_011943" FT CONFLICT 113 FT /note="I -> G (in Ref. 14; AA sequence)" FT /evidence="ECO:0000305" FT STRAND 22..26 FT /evidence="ECO:0007829|PDB:3IX0" FT STRAND 33..35 FT /evidence="ECO:0007829|PDB:3IX0" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:3IX0" FT STRAND 57..62 FT /evidence="ECO:0007829|PDB:3IX0" FT STRAND 64..71 FT /evidence="ECO:0007829|PDB:3IX0" FT STRAND 75..79 FT /evidence="ECO:0007829|PDB:3IX0" FT TURN 81..83 FT /evidence="ECO:0007829|PDB:3IX0" FT STRAND 84..89 FT /evidence="ECO:0007829|PDB:3IX0" FT HELIX 90..92 FT /evidence="ECO:0007829|PDB:3IX0" FT STRAND 94..101 FT /evidence="ECO:0007829|PDB:3IX0" FT STRAND 110..113 FT /evidence="ECO:0007829|PDB:3IX0" SQ SEQUENCE 114 AA; 12865 MW; D0B13E436D70BB1D CRC64; MNVLLGSVVI FATFVTLCNA SCYFIPNEGV PGDSTRKCMD LKGNKHPINS EWQTDNCETC TCYETEISCC TLVSTPVGYD KDNCQRIFKK EDCKYIVVEK KDPKKTCSVS EWII //