MSMB_HUMAN
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 03-AUG-2022, entry version 191.
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>3.0.co;2-n;
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}.
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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_002443.3. [P08118-1]
DR RefSeq; NP_619540.1; NM_138634.2. [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; 61.
DR IntAct; P08118; 2.
DR MINT; P08118; -.
DR STRING; 9606.ENSP00000463092; -.
DR iPTMnet; P08118; -.
DR PhosphoSitePlus; P08118; -.
DR BioMuta; MSMB; -.
DR DMDM; 131436; -.
DR jPOST; P08118; -.
DR MassIVE; P08118; -.
DR PaxDb; P08118; -.
DR PeptideAtlas; P08118; -.
DR PRIDE; P08118; -.
DR ProteomicsDB; 52068; -. [P08118-1]
DR Antibodypedia; 72459; 751 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 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 neXtProt; NX_P08118; -.
DR OpenTargets; ENSG00000263639; -.
DR Orphanet; 1331; Familial prostate cancer.
DR PharmGKB; PA31177; -.
DR VEuPathDB; HostDB:ENSG00000263639; -.
DR eggNOG; ENOG502SF48; Eukaryota.
DR GeneTree; ENSGT00940000154371; -.
DR HOGENOM; CLU_2637379_0_0_1; -.
DR InParanoid; P08118; -.
DR OMA; CPIFAAV; -.
DR OrthoDB; 1519822at2759; -.
DR PhylomeDB; P08118; -.
DR TreeFam; TF338336; -.
DR PathwayCommons; P08118; -.
DR SignaLink; P08118; -.
DR BioGRID-ORCS; 4477; 14 hits in 1057 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 121 other tissues.
DR ExpressionAtlas; P08118; baseline and differential.
DR Genevisible; P08118; HS.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; TAS:ProtInc.
DR InterPro; IPR008735; PSP94.
DR PANTHER; PTHR10500; PTHR10500; 1.
DR Pfam; PF05825; PSP94; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Direct protein sequencing;
KW Disulfide bond; Reference proteome; Secreted; 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
