SEMG2_GORGO
ID SEMG2_GORGO Reviewed; 474 AA.
AC Q5U7N3;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Semenogelin-2;
DE AltName: Full=Semenogelin II;
DE Short=SGII;
DE Flags: Precursor;
GN Name=SEMG2;
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595;
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).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY781387; AAV51945.1; -; mRNA.
DR AlphaFoldDB; Q5U7N3; -.
DR SMR; Q5U7N3; -.
DR eggNOG; ENOG502T80H; Eukaryota.
DR InParanoid; Q5U7N3; -.
DR Proteomes; UP000001519; 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..474
FT /note="Semenogelin-2"
FT /id="PRO_0000032358"
FT REGION 24..62
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..158
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 226..247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..474
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..62
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..158
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 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..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 402..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 430..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 474 AA; 53286 MW; BB2FB699F938F966 CRC64;
MKSIILFVLS LLLILEKQAA VMGQKGGSKG QLPSGSSQFP HGQKGQHYFG QKDQQHTKSK
GSFSIQHTYH VDINDHDRTR KSQQYDLNAL HKATKSKQHL GGSQQLLNYK QEGRDHDKSK
GHFHMIVIHH KGGQAHRGTQ NPSQDQGNSP SGKGLSSQYS NTEKRLWVHG LSKEQASASG
AQKGRTQGGS QSSYVLQTEE LVVNKQQRET KNSHQNKGHY QNAVDVREEH SSKLQTSLHP
AHQDRLQHGS KDIFTTQDEL LVYNKNQHQT KNLNQDQEHG QKAHKISYQS SRTEERQLNH
GEKSVQKDVS KGSISIQTEK KIHGKSQNQV TIHSQDQEHG HKENKMSHQS SSTEERHLNC
GEKGIQKGVS KGSISIQTEE QIHGKSQNQV RIPSQAQEYG HKENKISYRS SSTEERRLNS
GEKDVQKGVS KGSISIQTEE KIHGKSQNQV TIPSQDQEHG HKENKMSYQS SSTE