SEMG2_PANTR
ID SEMG2_PANTR Reviewed; 407 AA.
AC Q5U7N4; A4K2P3;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 67.
DE RecName: Full=Semenogelin-2;
DE AltName: Full=Semenogelin II;
DE Short=SGII;
DE Flags: Precursor;
GN Name=SEMG2;
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=15531881; DOI=10.1038/ng1471;
RA Dorus S., Evans P.D., Wyckoff G.J., Choi S.S., Lahn B.T.;
RT "Rate of molecular evolution of the seminal protein gene SEMG2 correlates
RT with levels of female promiscuity.";
RL Nat. Genet. 36:1326-1329(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=17267810; DOI=10.1101/gr.6004607;
RG NISC comparative sequencing program;
RA Hurle B., Swanson W., Green E.D.;
RT "Comparative sequence analyses reveal rapid and divergent evolutionary
RT changes of the WFDC locus in the primate lineage.";
RL Genome Res. 17:276-286(2007).
CC -!- FUNCTION: Participates in the formation of a gel matrix (sperm
CC coagulum) entrapping the accessory gland secretions and ejaculated
CC spermatozoa. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with SERPINA5. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the semenogelin family. {ECO:0000305}.
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DR EMBL; AY781386; AAV51944.1; -; mRNA.
DR EMBL; DP000037; ABO52928.1; -; Genomic_DNA.
DR RefSeq; NP_001009138.1; NM_001009138.1.
DR STRING; 9598.ENSPTRP00000054529; -.
DR GeneID; 493189; -.
DR KEGG; ptr:493189; -.
DR CTD; 6407; -.
DR InParanoid; Q5U7N4; -.
DR OrthoDB; 305064at2759; -.
DR Proteomes; UP000002277; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0050817; P:coagulation; IEA:InterPro.
DR GO; GO:1901318; P:negative regulation of flagellated sperm motility; IEA:InterPro.
DR GO; GO:0048240; P:sperm capacitation; IBA:GO_Central.
DR InterPro; IPR008836; Semenogelin.
DR Pfam; PF05474; Semenogelin; 1.
PE 2: Evidence at transcript level;
KW Reference proteome; Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..407
FT /note="Semenogelin-2"
FT /id="PRO_0000032365"
FT REGION 25..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..193
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..407
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..60
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 110..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..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..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 12
FT /note="V -> L (in Ref. 2; ABO52928)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 407 AA; 45812 MW; EB0BCBA06D74D529 CRC64;
MKSIILFVLS LVLILEKQAA VMGQKDGSKG QLPSGSSQFP HGQKGQHYFG QKDQQHTKSK
GSFSIQHTYH VDINDHDQTR KSQQYDLNAL HKVTKSKQHL DGSQQLLNYK QEGRDHDKSE
GHFHMIVIHH KGGQAHCGTQ NPSQDQGNSP SGKGLSSQYS NTEKRLWVHG LSKEQASASG
AQKGRTQGGS QSSYVLQTEE LVVNKQQLET KNSHQNKGHY QNVVDVREEH SGKLQTSLHP
AHQDRLQHGP KDIFTTQDEL LVYNKNQHQT KNLNQDQEHG QKAHKISYQS SRTEERQLNH
GEKSVQKDVS KGSISIQTEE KIHGKSQNQV TIHSQDQEHG HKENKMSYQS SSTEERHLNC
GEKGIQKGVS KGSISIQTEE QIHGKSQNXV RIPSQAQEYG RKENKIS