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   24-JAN-2024, entry version 172.
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   SMR; Q02383; -.
DR   BioGRID; 112307; 82.
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   GlyCosmos; Q02383; 2 sites, 13 glycans.
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; 9606-ENSP00000361855; -.
DR   PeptideAtlas; Q02383; -.
DR   ProteomicsDB; 58084; -.
DR   Pumba; Q02383; -.
DR   Antibodypedia; 27534; 109 antibodies from 18 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   AGR; HGNC:10743; -.
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; HGKSQNQ; -.
DR   OrthoDB; 4729048at2759; -.
DR   PhylomeDB; Q02383; -.
DR   TreeFam; TF342360; -.
DR   PathwayCommons; Q02383; -.
DR   SignaLink; Q02383; -.
DR   BioGRID-ORCS; 6407; 8 hits in 1104 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 45 other cell types or tissues.
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   PANTHER; PTHR10547:SF6; SEMENOGELIN-2; 1.
DR   PANTHER; PTHR10547; SEMENOGELIN/SEMINAL VESICLE SECRETORY PROTEIN; 1.
DR   Pfam; PF05474; Semenogelin; 1.
DR   Genevisible; Q02383; HS.
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
//