SEMG2_COLGU
ID SEMG2_COLGU Reviewed; 582 AA.
AC Q5U7M8;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 36.
DE RecName: Full=Semenogelin-2;
DE AltName: Full=Semenogelin II;
DE Short=SGII;
DE Flags: Precursor;
GN Name=SEMG2;
OS Colobus guereza (Mantled guereza) (Eastern black-and-white colobus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Colobinae; Colobus.
OX NCBI_TaxID=33548;
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; AY781392; AAV51950.1; -; mRNA.
DR AlphaFoldDB; Q5U7M8; -.
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 Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..582
FT /note="Semenogelin-2"
FT /id="PRO_0000032357"
FT REGION 25..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 91..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 393..557
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 46..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..131
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..157
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..192
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..289
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..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 426..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; 65654 MW; 9F0B85D2610C0FA4 CRC64;
MKSIILFVLS LLLILEKQAA VMGQKGGSKG QLSSGSSRFP HRQRSQHYSG QKDKQHTESK
GSSSIQHTYH VDANDHDQTQ KSQQYDLNAQ HKTTKSEQHL GRSQRLLNYK QKGRDHVKPK
RHFRLIVIHR KGGQVHHGTQ NPSQNQGNSP SGKGISSQYS NTEERLRVCG LSKEQASASG
AQKGRTQGGS QSSYVLQTEE LVANKQQRET QNSHRNKGHY QNVVEVREGH SSKLQTSLHP
AHQHRLQHGS KDIFTTQDEL LVYNKNQHQT KNLNQDQEHG RKAHKVSYQS SSTEERQFNH
GEKSVQKDVP KGSISIQTEE KIYGKSQNQV SIPSQDQEHG HKENKISYQS SSTEERRLNC
GEKDIQKGVS KGGISIQTEE QIHGEFQNQV TISNQDQEHG HKENKISYQS SSTEERRLNG
GEKDIQKSVS KGSISIQTEE KIHGKSQNQV TIPSQDQEHG HKENKISYQS SSTEERQLNY
GGKSIQKDVS QSSLSFQTEK LVEGKSQIQT PNPNQDQWSG LNAKGNSGKS ADREQDLLSH
EQESRYQQKS SGAHNTVNIE HEVAYDDLLT QQYNEDRNPI ST