SEMG2_HUMAN
ID SEMG2_HUMAN Reviewed; 582 AA.
AC Q02383; Q53ZU2; Q6X2M5; Q6X2M6;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1993, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Semenogelin-2;
DE AltName: Full=Semenogelin II;
DE Short=SGII;
DE Flags: Precursor;
GN Name=SEMG2;
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].
RC TISSUE=Seminal vesicle;
RX PubMed=1584792; DOI=10.1073/pnas.89.10.4559;
RA Lundwall A., Lilja H.;
RT "Molecular cloning of epididymal and seminal vesicular transcripts encoding
RT a semenogelin-related protein.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4559-4563(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1517240; DOI=10.1016/s0021-9258(19)37155-8;
RA Ulvsbaeck M., Lazure C., Lilja H., Spurr N.K., Rao V.V., Loeffler C.,
RA Hansmann I., Lundwall A.;
RT "Gene structure of semenogelin I and II. The predominant proteins in human
RT semen are encoded by two homologous genes on chromosome 20.";
RL J. Biol. Chem. 267:18080-18084(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND VARIANTS ASN-274 AND ARG-368.
RX PubMed=14629036; DOI=10.1007/s00239-003-2474-x;
RA Jensen-Seaman M.I., Li W.-H.;
RT "Evolution of the hominoid semenogelin genes, the major proteins of
RT ejaculated semen.";
RL J. Mol. Evol. 57:261-270(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
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 [6]
RP PARTIAL PROTEIN SEQUENCE.
RX PubMed=2757795;
RA Schneider K., Kausler W., Tripier D., Jouvenal K., Spiteller G.;
RT "Isolation and structure determination of two peptides occurring in human
RT seminal plasma.";
RL Biol. Chem. Hoppe-Seyler 370:353-356(1989).
RN [7]
RP CHARACTERIZATION.
RX PubMed=8665951; DOI=10.1111/j.1432-1033.1996.0048q.x;
RA Malm J., Hellman J., Magnusson H., Laurell C.B., Lilja H.;
RT "Isolation and characterization of the major gel proteins in human semen,
RT semenogelin I and semenogelin II.";
RL Eur. J. Biochem. 238:48-53(1996).
RN [8]
RP GLYCOSYLATION, AND INTERACTION WITH SERPINA5.
RX PubMed=8665956; DOI=10.1111/j.1432-1033.1996.0088q.x;
RA Kise H., Nishioka J., Kawamura J., Suzuki K.;
RT "Characterization of semenogelin II and its molecular interaction with
RT prostate-specific antigen and protein C inhibitor.";
RL Eur. J. Biochem. 238:88-96(1996).
CC -!- FUNCTION: Participates in the formation of a gel matrix (sperm
CC coagulum) entrapping the accessory gland secretions and ejaculated
CC spermatozoa.
CC -!- SUBUNIT: Interacts with SERPINA5. {ECO:0000269|PubMed:8665956}.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Seminal vesicles, and to a much lesser extent,
CC epididymis.
CC -!- PTM: Semenogelin-2 is thought to form both the 71 kDa polypeptide and,
CC in its glycosylated form, the 76 kDa polypeptide.
CC {ECO:0000269|PubMed:8665956}.
CC -!- SIMILARITY: Belongs to the semenogelin family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Shackled sperm - Issue 62 of
CC September 2005;
CC URL="https://web.expasy.org/spotlight/back_issues/062";
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DR EMBL; M81652; AAA60562.1; -; mRNA.
DR EMBL; M81651; AAA60313.1; -; Genomic_DNA.
DR EMBL; Z47556; CAA87637.1; -; Genomic_DNA.
DR EMBL; AY259284; AAP86625.1; -; Genomic_DNA.
DR EMBL; AY259285; AAP86626.1; -; Genomic_DNA.
DR EMBL; AY259286; AAP86627.1; -; Genomic_DNA.
DR EMBL; AL049767; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75870.1; -; Genomic_DNA.
DR CCDS; CCDS13346.1; -.
DR PIR; A43412; A43412.
DR RefSeq; NP_002999.1; NM_003008.2.
DR AlphaFoldDB; Q02383; -.
DR BioGRID; 112307; 78.
DR IntAct; Q02383; 27.
DR MINT; Q02383; -.
DR STRING; 9606.ENSP00000361855; -.
DR DrugBank; DB14533; Zinc chloride.
DR DrugBank; DB14548; Zinc sulfate, unspecified form.
DR GlyConnect; 2012; 2 O-Linked glycans (1 site).
DR GlyGen; Q02383; 3 sites, 11 N-linked glycans (1 site), 3 O-linked glycans (2 sites).
DR iPTMnet; Q02383; -.
DR PhosphoSitePlus; Q02383; -.
DR BioMuta; SEMG2; -.
DR DMDM; 401079; -.
DR jPOST; Q02383; -.
DR MassIVE; Q02383; -.
DR PaxDb; Q02383; -.
DR PeptideAtlas; Q02383; -.
DR PRIDE; Q02383; -.
DR ProteomicsDB; 58084; -.
DR Antibodypedia; 27534; 89 antibodies from 17 providers.
DR DNASU; 6407; -.
DR Ensembl; ENST00000372769.4; ENSP00000361855.3; ENSG00000124157.7.
DR GeneID; 6407; -.
DR KEGG; hsa:6407; -.
DR MANE-Select; ENST00000372769.4; ENSP00000361855.3; NM_003008.3; NP_002999.1.
DR UCSC; uc002xnk.4; human.
DR CTD; 6407; -.
DR DisGeNET; 6407; -.
DR GeneCards; SEMG2; -.
DR HGNC; HGNC:10743; SEMG2.
DR HPA; ENSG00000124157; Tissue enriched (seminal).
DR MIM; 182141; gene.
DR neXtProt; NX_Q02383; -.
DR OpenTargets; ENSG00000124157; -.
DR PharmGKB; PA35665; -.
DR VEuPathDB; HostDB:ENSG00000124157; -.
DR eggNOG; ENOG502T80H; Eukaryota.
DR GeneTree; ENSGT00940000162560; -.
DR HOGENOM; CLU_034710_0_0_1; -.
DR InParanoid; Q02383; -.
DR OMA; TEEKIHG; -.
DR OrthoDB; 305064at2759; -.
DR PhylomeDB; Q02383; -.
DR TreeFam; TF342360; -.
DR PathwayCommons; Q02383; -.
DR SignaLink; Q02383; -.
DR BioGRID-ORCS; 6407; 8 hits in 1027 CRISPR screens.
DR ChiTaRS; SEMG2; human.
DR GeneWiki; SEMG2; -.
DR GenomeRNAi; 6407; -.
DR Pharos; Q02383; Tbio.
DR PRO; PR:Q02383; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q02383; protein.
DR Bgee; ENSG00000124157; Expressed in seminal vesicle and 44 other tissues.
DR Genevisible; Q02383; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0002020; F:protease binding; IPI:UniProtKB.
DR GO; GO:0008270; F:zinc ion binding; IMP:UniProtKB.
DR GO; GO:0019731; P:antibacterial humoral response; IMP:UniProtKB.
DR GO; GO:0050817; P:coagulation; IDA:UniProtKB.
DR GO; GO:1901318; P:negative regulation of flagellated sperm motility; IEA:InterPro.
DR GO; GO:1900005; P:positive regulation of serine-type endopeptidase activity; IDA:UniProtKB.
DR GO; GO:0048240; P:sperm capacitation; IBA:GO_Central.
DR InterPro; IPR008836; Semenogelin.
DR Pfam; PF05474; Semenogelin; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Glycoprotein; Reference proteome; Repeat;
KW Secreted; Signal.
FT SIGNAL 1..23
FT CHAIN 24..582
FT /note="Semenogelin-2"
FT /id="PRO_0000032359"
FT REPEAT 70..129
FT /note="3-1"
FT REPEAT 141..200
FT /note="2-1"
FT REPEAT 201..260
FT /note="2-2"
FT REPEAT 501..559
FT /note="3-2"
FT REGION 24..59
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 70..559
FT /note="Repeat-rich region"
FT REGION 132..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 173..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 228..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 261..500
FT /note="4 X 60 AA tandem repeats, type I"
FT REGION 269..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..194
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..307
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..334
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..362
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 370..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..535
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 272
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000305|PubMed:8665956"
FT VARIANT 43
FT /note="Q -> K (in dbSNP:rs2233896)"
FT /id="VAR_034489"
FT VARIANT 57
FT /note="T -> A (in dbSNP:rs2233897)"
FT /id="VAR_034490"
FT VARIANT 274
FT /note="S -> N (in dbSNP:rs2233901)"
FT /evidence="ECO:0000269|PubMed:14629036"
FT /id="VAR_024630"
FT VARIANT 279
FT /note="H -> Y (in dbSNP:rs2233903)"
FT /id="VAR_034491"
FT VARIANT 368
FT /note="G -> R (in dbSNP:rs2071650)"
FT /evidence="ECO:0000269|PubMed:14629036"
FT /id="VAR_024631"
SQ SEQUENCE 582 AA; 65444 MW; EBF63FBF3A8EC45B CRC64;
MKSIILFVLS LLLILEKQAA VMGQKGGSKG QLPSGSSQFP HGQKGQHYFG QKDQQHTKSK
GSFSIQHTYH VDINDHDWTR KSQQYDLNAL HKATKSKQHL GGSQQLLNYK QEGRDHDKSK
GHFHMIVIHH KGGQAHHGTQ NPSQDQGNSP SGKGLSSQCS NTEKRLWVHG LSKEQASASG
AQKGRTQGGS QSSYVLQTEE LVVNKQQRET KNSHQNKGHY QNVVDVREEH SSKLQTSLHP
AHQDRLQHGP KDIFTTQDEL LVYNKNQHQT KNLSQDQEHG RKAHKISYPS SRTEERQLHH
GEKSVQKDVS KGSISIQTEE KIHGKSQNQV TIHSQDQEHG HKENKISYQS SSTEERHLNC
GEKGIQKGVS KGSISIQTEE QIHGKSQNQV RIPSQAQEYG HKENKISYQS SSTEERRLNS
GEKDVQKGVS KGSISIQTEE KIHGKSQNQV TIPSQDQEHG HKENKMSYQS SSTEERRLNY
GGKSTQKDVS QSSISFQIEK LVEGKSQIQT PNPNQDQWSG QNAKGKSGQS ADSKQDLLSH
EQKGRYKQES SESHNIVITE HEVAQDDHLT QQYNEDRNPI ST
