Full text data of SEMG1
SEMG1
(SEMG)
[Confidence: low (only semi-automatic identification from reviews)]
Semenogelin-1 (Semenogelin I; SGI; Alpha-inhibin-92; Alpha-inhibin-31; Seminal basic protein; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Semenogelin-1 (Semenogelin I; SGI; Alpha-inhibin-92; Alpha-inhibin-31; Seminal basic protein; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P04279
ID SEMG1_HUMAN Reviewed; 462 AA.
AC P04279; Q53ZV0; Q53ZV1; Q53ZV2; Q6X4I9; Q6Y809; Q6Y822; Q6Y823;
read moreAC Q86U64; Q96QM3;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Semenogelin-1;
DE AltName: Full=Semenogelin I;
DE Short=SGI;
DE Contains:
DE RecName: Full=Alpha-inhibin-92;
DE Contains:
DE RecName: Full=Alpha-inhibin-31;
DE Contains:
DE RecName: Full=Seminal basic protein;
DE Flags: Precursor;
GN Name=SEMG1; Synonyms=SEMG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2912989;
RA Lilja H., Abrahamsson P.-A., Lundwall A.;
RT "Semenogelin, the predominant protein in human semen. Primary
RT structure and identification of closely related proteins in the male
RT accessory sex glands and on the spermatozoa.";
RL J. Biol. Chem. 264:1894-1900(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=1517240;
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
RT human 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 THR-79 AND LEU-372.
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 MRNA] (ISOFORM 2).
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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-237 AND 241-449, AND VARIANT
RP THR-79.
RX PubMed=14562960; DOI=10.1007/s00239-002-2463-0;
RA Kingan S.B., Tatar M., Rand D.M.;
RT "Reduced polymorphism in the chimpanzee semen coagulating protein,
RT semenogelin I.";
RL J. Mol. Evol. 57:159-169(2003).
RN [9]
RP PROTEIN SEQUENCE OF 108-159.
RX PubMed=3972122; DOI=10.1016/0014-5793(85)81179-0;
RA Lilja H., Jeppsson J.-O.;
RT "Amino acid sequence of the predominant basic protein in human seminal
RT plasma.";
RL FEBS Lett. 182:181-184(1985).
RN [10]
RP PROTEIN SEQUENCE OF 108-138.
RX PubMed=6698208; DOI=10.1016/0014-5793(84)80840-6;
RA Seidah N.G., Ramasharma K., Sairam M.R., Chretien M.;
RT "Partial amino acid sequence of a human seminal plasma peptide with
RT inhibin-like activity.";
RL FEBS Lett. 167:98-102(1984).
RN [11]
RP PROTEIN SEQUENCE OF 108-138.
RX PubMed=6422553; DOI=10.1126/science.6422553;
RA Ramasharma K., Sairam M.R., Seidah N.G., Chretien M., Manjunath P.,
RA Schiller P.W., Yamashiro D., Li C.H.;
RT "Isolation, structure, and synthesis of a human seminal plasma peptide
RT with inhibin-like activity.";
RL Science 223:1199-1202(1984).
RN [12]
RP PROTEIN SEQUENCE OF 316-344.
RX PubMed=2757795;
RA Schneider K., Kausler W., Tripier D., Jouvenal K., Spiteller G.;
RT "Isolation and structure determination of two peptides occurring in
RT human seminal plasma.";
RL Biol. Chem. Hoppe-Seyler 370:353-356(1989).
RN [13]
RP PROTEIN SEQUENCE OF 373-397.
RX PubMed=8444163; DOI=10.1111/j.1432-1033.1993.tb17629.x;
RA Khan Z., Smyth D.G.;
RT "Isolation and identification of N-terminally extended forms of 5-
RT oxoprolylglutamylprolinamide (Glp-Glu-Pro-NH2), a thyrotropin-
RT releasing-hormone (TRH)-like peptide present in human semen.";
RL Eur. J. Biochem. 212:35-40(1993).
RN [14]
RP PROTEIN SEQUENCE OF 68-159.
RX PubMed=3889920; DOI=10.1073/pnas.82.12.4041;
RA Li C.H., Hammonds R.G., Ramasharma K., Chung D.;
RT "Human seminal alpha inhibins: isolation, characterization, and
RT structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4041-4044(1985).
RN [15]
RP REVIEW.
RX PubMed=10412373; DOI=10.1007/s000180050346;
RA Robert M., Gagnon C.;
RT "Semenogelin I: a coagulum forming, multifunctional seminal vesicle
RT protein.";
RL Cell. Mol. Life Sci. 55:944-960(1999).
RN [16]
RP INTERACTION WITH EPPIN.
RX PubMed=15590901; DOI=10.1095/biolreprod.104.036483;
RA Wang Z., Widgren E.E., Sivashanmugam P., O'Rand M.G., Richardson R.T.;
RT "Association of eppin with semenogelin on human spermatozoa.";
RL Biol. Reprod. 72:1064-1070(2005).
RN [17]
RP IDENTIFICATION IN A COMPLEX WITH LTF; CLU AND EPPIN.
RX PubMed=17567961; DOI=10.1095/biolreprod.107.060194;
RA Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.;
RT "Characterization of an eppin protein complex from human semen and
RT spermatozoa.";
RL Biol. Reprod. 77:476-484(2007).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF CYS-239.
RX PubMed=19889947; DOI=10.1095/biolreprod.109.081331;
RA Mitra A., Richardson R.T., O'Rand M.G.;
RT "Analysis of recombinant human semenogelin as an inhibitor of human
RT sperm motility.";
RL Biol. Reprod. 82:489-496(2010).
CC -!- FUNCTION: Predominant protein in semen. It participates in the
CC formation of a gel matrix entrapping the accessory gland
CC secretions and ejaculated spermatozoa. Fragments of semenogelin
CC and/or fragments of the related proteins may contribute to the
CC activation of progressive sperm movements as the gel-forming
CC proteins are fragmented by KLK3/PSA.
CC -!- FUNCTION: Alpha-inhibin-92 and alpha-inhibin-31, derived from the
CC proteolytic degradation of semenogelin, inhibit the secretion of
CC pituitary follicle-stimulating hormone.
CC -!- SUBUNIT: Occurs in disulfide-linked complexes which may also
CC contain two less abundant 71- and 76-kDa semenogelin-related
CC polypeptides. Interacts with EPPIN (via C-terminus); Cys-239 is a
CC critical amino acid for both binding to EPPIN.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04279-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04279-2; Sequence=VSP_004385;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Seminal vesicle.
CC -!- PTM: Transglutaminase substrate.
CC -!- PTM: Rapidly cleaved after ejaculation by KLK3/PSA, resulting in
CC liquefaction of the semen coagulum and the progressive release of
CC motile spermatozoa.
CC -!- SIMILARITY: Belongs to the semenogelin family.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Shackled sperm - Issue
CC 62 of September 2005;
CC URL="http://web.expasy.org/spotlight/back_issues/sptlt062.shtml";
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DR EMBL; J04440; AAB59506.1; -; mRNA.
DR EMBL; Z47556; CAA87636.1; -; Genomic_DNA.
DR EMBL; M81650; AAA18168.1; -; Genomic_DNA.
DR EMBL; AY256465; AAP82462.1; -; Genomic_DNA.
DR EMBL; AY256466; AAP82463.1; -; Genomic_DNA.
DR EMBL; AY256467; AAP82464.1; -; Genomic_DNA.
DR EMBL; AY256468; AAP82465.1; -; Genomic_DNA.
DR EMBL; AY256469; AAP82466.1; -; Genomic_DNA.
DR EMBL; BT007177; AAP35841.1; -; mRNA.
DR EMBL; AL049767; CAB53523.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75871.1; -; Genomic_DNA.
DR EMBL; BC007096; AAH07096.1; -; mRNA.
DR EMBL; BC055416; AAH55416.1; -; mRNA.
DR EMBL; AY174423; AAO20112.1; -; Genomic_DNA.
DR EMBL; AY174424; AAO20113.1; -; Genomic_DNA.
DR EMBL; AY174437; AAO20126.1; -; Genomic_DNA.
DR PIR; B43412; WTHUB.
DR RefSeq; NP_002998.1; NM_003007.3.
DR UniGene; Hs.1968; -.
DR ProteinModelPortal; P04279; -.
DR IntAct; P04279; 2.
DR MINT; MINT-2862979; -.
DR PhosphoSite; P04279; -.
DR DMDM; 134426; -.
DR PaxDb; P04279; -.
DR PRIDE; P04279; -.
DR DNASU; 6406; -.
DR Ensembl; ENST00000244069; ENSP00000244069; ENSG00000124233.
DR Ensembl; ENST00000372781; ENSP00000361867; ENSG00000124233.
DR GeneID; 6406; -.
DR KEGG; hsa:6406; -.
DR UCSC; uc002xni.2; human.
DR CTD; 6406; -.
DR GeneCards; GC20P043835; -.
DR HGNC; HGNC:10742; SEMG1.
DR HPA; HPA042476; -.
DR MIM; 182140; gene.
DR neXtProt; NX_P04279; -.
DR PharmGKB; PA35664; -.
DR eggNOG; NOG74001; -.
DR HOVERGEN; HBG054194; -.
DR InParanoid; P04279; -.
DR OMA; QNPNQDQ; -.
DR OrthoDB; EOG7J4469; -.
DR PhylomeDB; P04279; -.
DR Reactome; REACT_116125; Disease.
DR GeneWiki; Semenogelin_I; -.
DR GenomeRNAi; 6406; -.
DR NextBio; 24890; -.
DR PMAP-CutDB; P04279; -.
DR PRO; PR:P04279; -.
DR ArrayExpress; P04279; -.
DR Bgee; P04279; -.
DR CleanEx; HS_SEMG1; -.
DR Genevestigator; P04279; -.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0030141; C:secretory granule; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007320; P:insemination; TAS:ProtInc.
DR GO; GO:0019953; P:sexual reproduction; IEA:InterPro.
DR InterPro; IPR008836; Semenogelin.
DR PANTHER; PTHR10547; PTHR10547; 1.
DR Pfam; PF05474; Semenogelin; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Polymorphism; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 23
FT CHAIN 24 462 Semenogelin-1.
FT /FTId=PRO_0000032351.
FT PEPTIDE 68 159 Alpha-inhibin-92.
FT /FTId=PRO_0000032352.
FT PEPTIDE 108 159 Seminal basic protein.
FT /FTId=PRO_0000032353.
FT PEPTIDE 108 138 Alpha-inhibin-31.
FT /FTId=PRO_0000032354.
FT REPEAT 70 129 3-1.
FT REPEAT 141 200 2-1.
FT REPEAT 201 260 2-2.
FT REPEAT 381 439 3-2.
FT REGION 70 439 Repeat-rich region (By similarity).
FT REGION 164 283 Interaction with EPPIN.
FT REGION 261 380 2 X 60 AA tandem repeats, type 1.
FT MOD_RES 24 24 Pyrrolidone carboxylic acid (Probable).
FT DISULFID 239 239 Interchain.
FT VAR_SEQ 312 371 Missing (in isoform 2).
FT /FTId=VSP_004385.
FT VARIANT 58 58 E -> G (in dbSNP:rs11559137).
FT /FTId=VAR_053650.
FT VARIANT 79 79 S -> T (less common genetic variant;
FT dbSNP:rs2301366).
FT /FTId=VAR_005610.
FT VARIANT 108 108 H -> R (in dbSNP:rs2233884).
FT /FTId=VAR_053651.
FT VARIANT 372 372 R -> L (in dbSNP:rs2233887).
FT /FTId=VAR_022679.
FT MUTAGEN 239 239 C->G: Abrogates binding to EPPIN and do
FT not inhibit spem motility.
FT CONFLICT 100 100 L -> Q (in Ref. 3; AAP82463).
FT CONFLICT 235 237 QTS -> LRT (in Ref. 8; AAO20112/
FT AAO20113).
FT CONFLICT 321 321 K -> L (in Ref. 12; AA sequence).
FT CONFLICT 423 423 K -> N (in Ref. 2; CAA87636/AAA18168).
FT CONFLICT 457 457 R -> Q (in Ref. 4 and 7).
SQ SEQUENCE 462 AA; 52131 MW; 760F48EFCF2FA702 CRC64;
MKPNIIFVLS LLLILEKQAA VMGQKGGSKG RLPSEFSQFP HGQKGQHYSG QKGKQQTESK
GSFSIQYTYH VDANDHDQSR KSQQYDLNAL HKTTKSQRHL GGSQQLLHNK QEGRDHDKSK
GHFHRVVIHH KGGKAHRGTQ NPSQDQGNSP SGKGISSQYS NTEERLWVHG LSKEQTSVSG
AQKGRKQGGS QSSYVLQTEE LVANKQQRET KNSHQNKGHY QNVVEVREEH SSKVQTSLCP
AHQDKLQHGS KDIFSTQDEL LVYNKNQHQT KNLNQDQQHG RKANKISYQS SSTEERRLHY
GENGVQKDVS QSSIYSQTEE KAQGKSQKQI TIPSQEQEHS QKANKISYQS SSTEERRLHY
GENGVQKDVS QRSIYSQTEK LVAGKSQIQA PNPKQEPWHG ENAKGESGQS TNREQDLLSH
EQKGRHQHGS HGGLDIVIIE QEDDSDRHLA QHLNNDRNPL FT
//
ID SEMG1_HUMAN Reviewed; 462 AA.
AC P04279; Q53ZV0; Q53ZV1; Q53ZV2; Q6X4I9; Q6Y809; Q6Y822; Q6Y823;
read moreAC Q86U64; Q96QM3;
DT 20-MAR-1987, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1990, sequence version 2.
DT 22-JAN-2014, entry version 146.
DE RecName: Full=Semenogelin-1;
DE AltName: Full=Semenogelin I;
DE Short=SGI;
DE Contains:
DE RecName: Full=Alpha-inhibin-92;
DE Contains:
DE RecName: Full=Alpha-inhibin-31;
DE Contains:
DE RecName: Full=Seminal basic protein;
DE Flags: Precursor;
GN Name=SEMG1; Synonyms=SEMG;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=2912989;
RA Lilja H., Abrahamsson P.-A., Lundwall A.;
RT "Semenogelin, the predominant protein in human semen. Primary
RT structure and identification of closely related proteins in the male
RT accessory sex glands and on the spermatozoa.";
RL J. Biol. Chem. 264:1894-1900(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=1517240;
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
RT human 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 THR-79 AND LEU-372.
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 MRNA] (ISOFORM 2).
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
RT vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [5]
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.,
RA Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J.,
RA Buck D., Burrill W.D., Butler A.P., Carder C., Carter N.P.,
RA Chapman J.C., Clamp M., Clark G., Clark L.N., Clark S.Y., Clee C.M.,
RA Clegg S., Cobley V.E., Collier R.E., Connor R.E., Corby N.R.,
RA Coulson A., Coville G.J., Deadman R., Dhami P.D., Dunn M.,
RA 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.,
RA Rice C.M., Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S.,
RA Skuce C.D., Smith M.L., Soderlund C., Steward C.A., Sulston J.E.,
RA Swann R.M., Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A.,
RA Tracey A., Tromans A.C., Vaudin M., Wall M., Wallis J.M.,
RA Whitehead S.L., Whittaker P., Willey D.L., Williams L., Williams S.A.,
RA Wilming L., Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S.,
RA Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 62-237 AND 241-449, AND VARIANT
RP THR-79.
RX PubMed=14562960; DOI=10.1007/s00239-002-2463-0;
RA Kingan S.B., Tatar M., Rand D.M.;
RT "Reduced polymorphism in the chimpanzee semen coagulating protein,
RT semenogelin I.";
RL J. Mol. Evol. 57:159-169(2003).
RN [9]
RP PROTEIN SEQUENCE OF 108-159.
RX PubMed=3972122; DOI=10.1016/0014-5793(85)81179-0;
RA Lilja H., Jeppsson J.-O.;
RT "Amino acid sequence of the predominant basic protein in human seminal
RT plasma.";
RL FEBS Lett. 182:181-184(1985).
RN [10]
RP PROTEIN SEQUENCE OF 108-138.
RX PubMed=6698208; DOI=10.1016/0014-5793(84)80840-6;
RA Seidah N.G., Ramasharma K., Sairam M.R., Chretien M.;
RT "Partial amino acid sequence of a human seminal plasma peptide with
RT inhibin-like activity.";
RL FEBS Lett. 167:98-102(1984).
RN [11]
RP PROTEIN SEQUENCE OF 108-138.
RX PubMed=6422553; DOI=10.1126/science.6422553;
RA Ramasharma K., Sairam M.R., Seidah N.G., Chretien M., Manjunath P.,
RA Schiller P.W., Yamashiro D., Li C.H.;
RT "Isolation, structure, and synthesis of a human seminal plasma peptide
RT with inhibin-like activity.";
RL Science 223:1199-1202(1984).
RN [12]
RP PROTEIN SEQUENCE OF 316-344.
RX PubMed=2757795;
RA Schneider K., Kausler W., Tripier D., Jouvenal K., Spiteller G.;
RT "Isolation and structure determination of two peptides occurring in
RT human seminal plasma.";
RL Biol. Chem. Hoppe-Seyler 370:353-356(1989).
RN [13]
RP PROTEIN SEQUENCE OF 373-397.
RX PubMed=8444163; DOI=10.1111/j.1432-1033.1993.tb17629.x;
RA Khan Z., Smyth D.G.;
RT "Isolation and identification of N-terminally extended forms of 5-
RT oxoprolylglutamylprolinamide (Glp-Glu-Pro-NH2), a thyrotropin-
RT releasing-hormone (TRH)-like peptide present in human semen.";
RL Eur. J. Biochem. 212:35-40(1993).
RN [14]
RP PROTEIN SEQUENCE OF 68-159.
RX PubMed=3889920; DOI=10.1073/pnas.82.12.4041;
RA Li C.H., Hammonds R.G., Ramasharma K., Chung D.;
RT "Human seminal alpha inhibins: isolation, characterization, and
RT structure.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:4041-4044(1985).
RN [15]
RP REVIEW.
RX PubMed=10412373; DOI=10.1007/s000180050346;
RA Robert M., Gagnon C.;
RT "Semenogelin I: a coagulum forming, multifunctional seminal vesicle
RT protein.";
RL Cell. Mol. Life Sci. 55:944-960(1999).
RN [16]
RP INTERACTION WITH EPPIN.
RX PubMed=15590901; DOI=10.1095/biolreprod.104.036483;
RA Wang Z., Widgren E.E., Sivashanmugam P., O'Rand M.G., Richardson R.T.;
RT "Association of eppin with semenogelin on human spermatozoa.";
RL Biol. Reprod. 72:1064-1070(2005).
RN [17]
RP IDENTIFICATION IN A COMPLEX WITH LTF; CLU AND EPPIN.
RX PubMed=17567961; DOI=10.1095/biolreprod.107.060194;
RA Wang Z., Widgren E.E., Richardson R.T., O'Rand M.G.;
RT "Characterization of an eppin protein complex from human semen and
RT spermatozoa.";
RL Biol. Reprod. 77:476-484(2007).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF CYS-239.
RX PubMed=19889947; DOI=10.1095/biolreprod.109.081331;
RA Mitra A., Richardson R.T., O'Rand M.G.;
RT "Analysis of recombinant human semenogelin as an inhibitor of human
RT sperm motility.";
RL Biol. Reprod. 82:489-496(2010).
CC -!- FUNCTION: Predominant protein in semen. It participates in the
CC formation of a gel matrix entrapping the accessory gland
CC secretions and ejaculated spermatozoa. Fragments of semenogelin
CC and/or fragments of the related proteins may contribute to the
CC activation of progressive sperm movements as the gel-forming
CC proteins are fragmented by KLK3/PSA.
CC -!- FUNCTION: Alpha-inhibin-92 and alpha-inhibin-31, derived from the
CC proteolytic degradation of semenogelin, inhibit the secretion of
CC pituitary follicle-stimulating hormone.
CC -!- SUBUNIT: Occurs in disulfide-linked complexes which may also
CC contain two less abundant 71- and 76-kDa semenogelin-related
CC polypeptides. Interacts with EPPIN (via C-terminus); Cys-239 is a
CC critical amino acid for both binding to EPPIN.
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P04279-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P04279-2; Sequence=VSP_004385;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Seminal vesicle.
CC -!- PTM: Transglutaminase substrate.
CC -!- PTM: Rapidly cleaved after ejaculation by KLK3/PSA, resulting in
CC liquefaction of the semen coagulum and the progressive release of
CC motile spermatozoa.
CC -!- SIMILARITY: Belongs to the semenogelin family.
CC -!- WEB RESOURCE: Name=Protein Spotlight; Note=Shackled sperm - Issue
CC 62 of September 2005;
CC URL="http://web.expasy.org/spotlight/back_issues/sptlt062.shtml";
CC -----------------------------------------------------------------------
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DR EMBL; J04440; AAB59506.1; -; mRNA.
DR EMBL; Z47556; CAA87636.1; -; Genomic_DNA.
DR EMBL; M81650; AAA18168.1; -; Genomic_DNA.
DR EMBL; AY256465; AAP82462.1; -; Genomic_DNA.
DR EMBL; AY256466; AAP82463.1; -; Genomic_DNA.
DR EMBL; AY256467; AAP82464.1; -; Genomic_DNA.
DR EMBL; AY256468; AAP82465.1; -; Genomic_DNA.
DR EMBL; AY256469; AAP82466.1; -; Genomic_DNA.
DR EMBL; BT007177; AAP35841.1; -; mRNA.
DR EMBL; AL049767; CAB53523.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75871.1; -; Genomic_DNA.
DR EMBL; BC007096; AAH07096.1; -; mRNA.
DR EMBL; BC055416; AAH55416.1; -; mRNA.
DR EMBL; AY174423; AAO20112.1; -; Genomic_DNA.
DR EMBL; AY174424; AAO20113.1; -; Genomic_DNA.
DR EMBL; AY174437; AAO20126.1; -; Genomic_DNA.
DR PIR; B43412; WTHUB.
DR RefSeq; NP_002998.1; NM_003007.3.
DR UniGene; Hs.1968; -.
DR ProteinModelPortal; P04279; -.
DR IntAct; P04279; 2.
DR MINT; MINT-2862979; -.
DR PhosphoSite; P04279; -.
DR DMDM; 134426; -.
DR PaxDb; P04279; -.
DR PRIDE; P04279; -.
DR DNASU; 6406; -.
DR Ensembl; ENST00000244069; ENSP00000244069; ENSG00000124233.
DR Ensembl; ENST00000372781; ENSP00000361867; ENSG00000124233.
DR GeneID; 6406; -.
DR KEGG; hsa:6406; -.
DR UCSC; uc002xni.2; human.
DR CTD; 6406; -.
DR GeneCards; GC20P043835; -.
DR HGNC; HGNC:10742; SEMG1.
DR HPA; HPA042476; -.
DR MIM; 182140; gene.
DR neXtProt; NX_P04279; -.
DR PharmGKB; PA35664; -.
DR eggNOG; NOG74001; -.
DR HOVERGEN; HBG054194; -.
DR InParanoid; P04279; -.
DR OMA; QNPNQDQ; -.
DR OrthoDB; EOG7J4469; -.
DR PhylomeDB; P04279; -.
DR Reactome; REACT_116125; Disease.
DR GeneWiki; Semenogelin_I; -.
DR GenomeRNAi; 6406; -.
DR NextBio; 24890; -.
DR PMAP-CutDB; P04279; -.
DR PRO; PR:P04279; -.
DR ArrayExpress; P04279; -.
DR Bgee; P04279; -.
DR CleanEx; HS_SEMG1; -.
DR Genevestigator; P04279; -.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0030141; C:secretory granule; IEA:InterPro.
DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro.
DR GO; GO:0007320; P:insemination; TAS:ProtInc.
DR GO; GO:0019953; P:sexual reproduction; IEA:InterPro.
DR InterPro; IPR008836; Semenogelin.
DR PANTHER; PTHR10547; PTHR10547; 1.
DR Pfam; PF05474; Semenogelin; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Direct protein sequencing;
KW Disulfide bond; Polymorphism; Pyrrolidone carboxylic acid;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1 23
FT CHAIN 24 462 Semenogelin-1.
FT /FTId=PRO_0000032351.
FT PEPTIDE 68 159 Alpha-inhibin-92.
FT /FTId=PRO_0000032352.
FT PEPTIDE 108 159 Seminal basic protein.
FT /FTId=PRO_0000032353.
FT PEPTIDE 108 138 Alpha-inhibin-31.
FT /FTId=PRO_0000032354.
FT REPEAT 70 129 3-1.
FT REPEAT 141 200 2-1.
FT REPEAT 201 260 2-2.
FT REPEAT 381 439 3-2.
FT REGION 70 439 Repeat-rich region (By similarity).
FT REGION 164 283 Interaction with EPPIN.
FT REGION 261 380 2 X 60 AA tandem repeats, type 1.
FT MOD_RES 24 24 Pyrrolidone carboxylic acid (Probable).
FT DISULFID 239 239 Interchain.
FT VAR_SEQ 312 371 Missing (in isoform 2).
FT /FTId=VSP_004385.
FT VARIANT 58 58 E -> G (in dbSNP:rs11559137).
FT /FTId=VAR_053650.
FT VARIANT 79 79 S -> T (less common genetic variant;
FT dbSNP:rs2301366).
FT /FTId=VAR_005610.
FT VARIANT 108 108 H -> R (in dbSNP:rs2233884).
FT /FTId=VAR_053651.
FT VARIANT 372 372 R -> L (in dbSNP:rs2233887).
FT /FTId=VAR_022679.
FT MUTAGEN 239 239 C->G: Abrogates binding to EPPIN and do
FT not inhibit spem motility.
FT CONFLICT 100 100 L -> Q (in Ref. 3; AAP82463).
FT CONFLICT 235 237 QTS -> LRT (in Ref. 8; AAO20112/
FT AAO20113).
FT CONFLICT 321 321 K -> L (in Ref. 12; AA sequence).
FT CONFLICT 423 423 K -> N (in Ref. 2; CAA87636/AAA18168).
FT CONFLICT 457 457 R -> Q (in Ref. 4 and 7).
SQ SEQUENCE 462 AA; 52131 MW; 760F48EFCF2FA702 CRC64;
MKPNIIFVLS LLLILEKQAA VMGQKGGSKG RLPSEFSQFP HGQKGQHYSG QKGKQQTESK
GSFSIQYTYH VDANDHDQSR KSQQYDLNAL HKTTKSQRHL GGSQQLLHNK QEGRDHDKSK
GHFHRVVIHH KGGKAHRGTQ NPSQDQGNSP SGKGISSQYS NTEERLWVHG LSKEQTSVSG
AQKGRKQGGS QSSYVLQTEE LVANKQQRET KNSHQNKGHY QNVVEVREEH SSKVQTSLCP
AHQDKLQHGS KDIFSTQDEL LVYNKNQHQT KNLNQDQQHG RKANKISYQS SSTEERRLHY
GENGVQKDVS QSSIYSQTEE KAQGKSQKQI TIPSQEQEHS QKANKISYQS SSTEERRLHY
GENGVQKDVS QRSIYSQTEK LVAGKSQIQA PNPKQEPWHG ENAKGESGQS TNREQDLLSH
EQKGRHQHGS HGGLDIVIIE QEDDSDRHLA QHLNNDRNPL FT
//
MIM
182140
*RECORD*
*FIELD* NO
182140
*FIELD* TI
*182140 SEMENOGELIN; SEMG
;;SEMENOGELIN I; SEMG1
*FIELD* TX
CLONING
Lilja et al. (1989) isolated from a seminal vesicular cDNA library
read morelambda-gt11 clones for semenogelin, the predominant protein in human
semen. One clone carrying a cDNA insert of 1,606 nucleotides and a
polyadenylated tail coded for the entire semenogelin precursor. An open
reading frame of 1,386 nucleotides encoded a signal peptide and a mature
protein of 439 amino acid residues, in which residues 85 to 136 were
identical with a previously characterized semenogelin fragment. An
abundant seminal vesicular mRNA transcript of 1.8 kb codes for
semenogelin. Two additional transcripts, 1 a seminal vesicular 2.2-kb
species and 1 an epididymal 2.0-kb species, code for related proteins
that have both structural and antigenic features in common with
semenogelin. Semenogelin and the semenogelin-related proteins are the
major proteins involved in the gelatinous entrapment of ejaculated
spermatozoa. The spermatozoa become progressively motile as these
gel-forming proteins are fragmented by the kallikrein-like protease,
prostate-specific antigen (176820), and the gel dissolves.
MAPPING
By in situ hybridization, Loeffler et al. (1991) mapped the SEMG gene to
20q12-q13.2.
Ulvsback et al. (1992) cloned the 2 semenogelin genes, SEMG1 and SEMG2
(182141), and demonstrated that they are located 11.5 kb apart in the
region 20q12-q13.1.
*FIELD* RF
1. Lilja, H.; Abrahamsson, P.-A.; Lundwall, A.: Semenogelin, the
predominant protein in human semen: primary structure and identification
of closely related proteins in the male accessory sex glands and on
the spermatozoa. J. Biol. Chem. 264: 1894-1900, 1989.
2. Loeffler, C.; Rao, V. V. N. G.; Schnittger, S.; Pfau, H. P.; Lundwall,
A.; Schaefer, R.; Stolz, F. M.; Hansmann, I.: Personal Communication.
8/18/1991.
3. Ulvsback, M.; Lazure, C.; Lilja, H.; Spurr, N. K.; Rao, V. V.;
Loffler, C.; Hansmann, I.; Lundwall, A.: Gene structure of semenogelin
I and II: the predominant proteins in human semen are encoded by two
homologous genes on chromosome 20. J. Biol. Chem. 267: 18080-18084,
1992.
*FIELD* CD
Victor A. McKusick: 3/20/1989
*FIELD* ED
alopez: 06/04/2010
carol: 5/27/1993
supermim: 3/16/1992
carol: 1/10/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 3/28/1989
*RECORD*
*FIELD* NO
182140
*FIELD* TI
*182140 SEMENOGELIN; SEMG
;;SEMENOGELIN I; SEMG1
*FIELD* TX
CLONING
Lilja et al. (1989) isolated from a seminal vesicular cDNA library
read morelambda-gt11 clones for semenogelin, the predominant protein in human
semen. One clone carrying a cDNA insert of 1,606 nucleotides and a
polyadenylated tail coded for the entire semenogelin precursor. An open
reading frame of 1,386 nucleotides encoded a signal peptide and a mature
protein of 439 amino acid residues, in which residues 85 to 136 were
identical with a previously characterized semenogelin fragment. An
abundant seminal vesicular mRNA transcript of 1.8 kb codes for
semenogelin. Two additional transcripts, 1 a seminal vesicular 2.2-kb
species and 1 an epididymal 2.0-kb species, code for related proteins
that have both structural and antigenic features in common with
semenogelin. Semenogelin and the semenogelin-related proteins are the
major proteins involved in the gelatinous entrapment of ejaculated
spermatozoa. The spermatozoa become progressively motile as these
gel-forming proteins are fragmented by the kallikrein-like protease,
prostate-specific antigen (176820), and the gel dissolves.
MAPPING
By in situ hybridization, Loeffler et al. (1991) mapped the SEMG gene to
20q12-q13.2.
Ulvsback et al. (1992) cloned the 2 semenogelin genes, SEMG1 and SEMG2
(182141), and demonstrated that they are located 11.5 kb apart in the
region 20q12-q13.1.
*FIELD* RF
1. Lilja, H.; Abrahamsson, P.-A.; Lundwall, A.: Semenogelin, the
predominant protein in human semen: primary structure and identification
of closely related proteins in the male accessory sex glands and on
the spermatozoa. J. Biol. Chem. 264: 1894-1900, 1989.
2. Loeffler, C.; Rao, V. V. N. G.; Schnittger, S.; Pfau, H. P.; Lundwall,
A.; Schaefer, R.; Stolz, F. M.; Hansmann, I.: Personal Communication.
8/18/1991.
3. Ulvsback, M.; Lazure, C.; Lilja, H.; Spurr, N. K.; Rao, V. V.;
Loffler, C.; Hansmann, I.; Lundwall, A.: Gene structure of semenogelin
I and II: the predominant proteins in human semen are encoded by two
homologous genes on chromosome 20. J. Biol. Chem. 267: 18080-18084,
1992.
*FIELD* CD
Victor A. McKusick: 3/20/1989
*FIELD* ED
alopez: 06/04/2010
carol: 5/27/1993
supermim: 3/16/1992
carol: 1/10/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 3/28/1989