SEMG2_HYLLA
ID SEMG2_HYLLA Reviewed; 582 AA.
AC Q5U7N1;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 39.
DE RecName: Full=Semenogelin-2;
DE AltName: Full=Semenogelin II;
DE Short=SGII;
DE Flags: Precursor;
GN Name=SEMG2;
OS Hylobates lar (Common gibbon) (White-handed gibbon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Hylobates.
OX NCBI_TaxID=9580;
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; AY781389; AAV51947.1; -; mRNA.
DR AlphaFoldDB; Q5U7N1; -.
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_0000032361"
FT REGION 26..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 132..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..582
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..45
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 275..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..335
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 336..358
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 379..395
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..417
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 439..455
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..470
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 471..528
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 529..573
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 582 AA; 65665 MW; F8EA07771F9EB40B CRC64;
MKSIILFVLS LLLILEKQAA VMGQKCGSKG QLPSGSSQFP RGQKGQHYSG QKDEQHTKSK
GSFSIQHTYH VDVNDRDRTQ KSQQYDLNAQ HKMTKSKQHL GGSQELLNYK QEGRDHDKSK
DHFHMIVIHH KGGQAHRGTQ NPSQDQGNSP SGKGISSQYS NTNKRLWVHG LTKEQASASG
AQKGRTQGGS QSSYVLQTEE LVANKQQRET QNSPQNKGHY QNVVEMREEH SSKLQTSLHP
AYQDRLQHGP KDIFTTQDEL LVYNKNQHQT KNLNQDQEHG QKTHKISYQS SRTEERQLNC
GEKSVQKDVS KGGISIQTEE KIHGKSQNQV TIHSQGQEHG HKENKMSYQS SSTEERHLNC
GEKGIHKGVS KGSISIQTEE QIHGKSQNQV RIPSQAQEHG HKENKMSYQS SSTEERRLNC
GEKGIHKGVS KGSISIQTEE QIHGKSQNQV RIPSQAQEHG HKENKMSYQS SSTEERRLNY
GGKSMQKDVS QSSTSFHTEK LVEGKSQIQT PNPNQDQWSV QNAKGKSDQS AGREQDLLSH
EQKGRHQQES SEARNIVITE HEVAYDDHLT QQYNEDRNPV ST