MSMB_PIG
ID MSMB_PIG Reviewed; 111 AA.
AC O02826;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Beta-microseminoprotein;
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=TS507;
DE Flags: Precursor;
GN Name=MSMB; Synonyms=PSP94;
OS Sus scrofa (Pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX NCBI_TaxID=9823;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=8562060; DOI=10.1002/mrd.1080420204;
RA Tanaka T., Itahana K., Andoh N., Takeya T., Sato E.;
RT "Expression of prostatic secretory protein (PSP)-like protein in porcine
RT corpus luteum: isolation and characterization of a new gene encoding PSP94-
RT like protein.";
RL Mol. Reprod. Dev. 42:149-156(1995).
RN [2]
RP PROTEIN SEQUENCE OF 21-111, AND PYROGLUTAMATE FORMATION AT GLN-21.
RC TISSUE=Seminal plasma;
RX PubMed=8117114; DOI=10.1006/abbi.1994.1086;
RA Fernlund P., Granberg L.B., Roepstorff P.;
RT "Amino acid sequence of beta-microseminoprotein from porcine seminal
RT plasma.";
RL Arch. Biochem. Biophys. 309:70-76(1994).
RN [3]
RP STRUCTURE BY NMR OF 21-111, AND DISULFIDE BONDS.
RX PubMed=15701518; DOI=10.1016/j.jmb.2004.12.029;
RA Wang I., Lou Y.C., Wu K.P., Wu S.H., Chang W.C., Chen C.;
RT "Novel solution structure of porcine beta-microseminoprotein.";
RL J. Mol. Biol. 346:1071-1082(2005).
RN [4]
RP STRUCTURE BY NMR OF 21-111.
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).
CC -!- SUBUNIT: Homodimer; Interacts with PI16. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Sperm surface. {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Corpora lutea, mostly in the luteal cells
CC surrounding blood vessels.
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; S80724; AAB50711.1; -; mRNA.
DR PIR; S41663; S41663.
DR RefSeq; NP_999017.1; NM_213852.1.
DR PDB; 1XHH; NMR; -; A=21-111.
DR PDB; 2IZ4; NMR; -; A=21-111.
DR PDBsum; 1XHH; -.
DR PDBsum; 2IZ4; -.
DR AlphaFoldDB; O02826; -.
DR BMRB; O02826; -.
DR SMR; O02826; -.
DR STRING; 9823.ENSSSCP00000028823; -.
DR PaxDb; O02826; -.
DR PRIDE; O02826; -.
DR Ensembl; ENSSSCT00005020266; ENSSSCP00005012201; ENSSSCG00005012967.
DR Ensembl; ENSSSCT00015085900; ENSSSCP00015034931; ENSSSCG00015064131.
DR Ensembl; ENSSSCT00030037521; ENSSSCP00030017182; ENSSSCG00030026852.
DR Ensembl; ENSSSCT00050024263; ENSSSCP00050010184; ENSSSCG00050017855.
DR Ensembl; ENSSSCT00060108450; ENSSSCP00060048325; ENSSSCG00060078504.
DR Ensembl; ENSSSCT00060108455; ENSSSCP00060048328; ENSSSCG00060078504.
DR Ensembl; ENSSSCT00065032023; ENSSSCP00065013112; ENSSSCG00065024053.
DR GeneID; 396852; -.
DR KEGG; ssc:396852; -.
DR CTD; 4477; -.
DR eggNOG; ENOG502SF48; Eukaryota.
DR HOGENOM; CLU_144891_0_0_1; -.
DR InParanoid; O02826; -.
DR OrthoDB; 1519822at2759; -.
DR TreeFam; TF338336; -.
DR EvolutionaryTrace; O02826; -.
DR Proteomes; UP000008227; Unplaced.
DR Proteomes; UP000314985; Unplaced.
DR Genevisible; O02826; SS.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR InterPro; IPR008735; PSP94.
DR PANTHER; PTHR10500; PTHR10500; 1.
DR Pfam; PF05825; PSP94; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Disulfide bond;
KW Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT SIGNAL 1..20
FT /evidence="ECO:0000269|PubMed:8117114"
FT CHAIN 21..111
FT /note="Beta-microseminoprotein"
FT /id="PRO_0000019272"
FT MOD_RES 21
FT /note="Pyrrolidone carboxylic acid"
FT /evidence="ECO:0000269|PubMed:8117114"
FT DISULFID 22..67
FT /evidence="ECO:0000269|PubMed:15701518"
FT DISULFID 35..59
FT /evidence="ECO:0000269|PubMed:15701518"
FT DISULFID 54..90
FT /evidence="ECO:0000269|PubMed:15701518"
FT DISULFID 57..66
FT /evidence="ECO:0000269|PubMed:15701518"
FT DISULFID 81..104
FT /evidence="ECO:0000269|PubMed:15701518"
FT STRAND 23..26
FT /evidence="ECO:0007829|PDB:1XHH"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:1XHH"
FT TURN 38..40
FT /evidence="ECO:0007829|PDB:1XHH"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1XHH"
FT STRAND 48..50
FT /evidence="ECO:0007829|PDB:2IZ4"
FT STRAND 52..59
FT /evidence="ECO:0007829|PDB:1XHH"
FT STRAND 61..68
FT /evidence="ECO:0007829|PDB:1XHH"
FT STRAND 72..75
FT /evidence="ECO:0007829|PDB:1XHH"
FT STRAND 79..86
FT /evidence="ECO:0007829|PDB:1XHH"
FT TURN 87..90
FT /evidence="ECO:0007829|PDB:1XHH"
FT STRAND 91..96
FT /evidence="ECO:0007829|PDB:1XHH"
FT STRAND 99..103
FT /evidence="ECO:0007829|PDB:1XHH"
FT STRAND 108..110
FT /evidence="ECO:0007829|PDB:1XHH"
SQ SEQUENCE 111 AA; 12246 MW; ABF33A067A23765E CRC64;
MKFLLGTLVV LATFVTLCNS QCYFIPNQSL KPNECQDLKG VSHPLNSVWK TKDCEECTCG
QNAISCCNTA AIPTGYDTNK CQKILNKKTC TYTVVEKKDP GKTCDVTGWV L
