SEMG2_MACFA
ID SEMG2_MACFA Reviewed; 582 AA.
AC Q5U7N0;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 23-FEB-2022, entry version 42.
DE RecName: Full=Semenogelin-2;
DE AltName: Full=Semenogelin II;
DE Short=SGII;
DE Flags: Precursor;
GN Name=SEMG2;
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541;
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}.
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DR EMBL; AY781390; AAV51948.1; -; mRNA.
DR eggNOG; ENOG502T80H; Eukaryota.
DR Proteomes; UP000233100; 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 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..582
FT /note="Semenogelin-2"
FT /id="PRO_0000032362"
FT REGION 25..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 265..553
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..131
FT /note="Basic 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..209
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 319..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..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 410..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 470..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..543
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 65754 MW; 20E56C568FF69CBE CRC64;
MKSIILFVLS LLLILEKQAA VMGQKGGSKG QLSSGSSRFP HRHRSQHYSG QKDKQHTESK
GSFSIQHTYH VDANDHDRTR KSQQYYLNAQ HKTTKSKQHL RRHQRLLNYK QKGRGRVKPK
RHFHLIVIHR KGGQVHHGTQ NPSQDQGNSP SGKGISSQYS NTEERLRVRG LSKEQASASG
AQKGRTQGGS QTNYVLQTEE LVANKQQRET QNSHRNKGHY QNVVDVRXEH SSKLQTSLRP
AHQHKLQHGY KDIFTTQDEL LVYNKNQHQT KNLNQDQEHG RKAHKGSYQS SSTEERQPNH
EEKSVQKGVP KGSISIQTEE KIYGKSQNQV TIPSQDQEHG HKENKISYQS SSAEERRLNS
GEKGIQKGVS KGSISIQTEE KIHGKSQNQV AIPSQDQEHG HKENKISYQS SSAEERQLNS
GEKGIQKGVS KGSISIQTEE KIYGKSQNQV TIPSQDQEHG HKENKIAYQS SSTEERQLNY
GGKSIQKDVS QSSLSFQTEK LVEGKSQIQT PNPNQGQWSG QNAKGNSGKS ADRKQDLLSH
EQEGRYQQEF SGAHNTVNIE HKVAYDDLLT QQYNEDRNPI ST