SEMG2_HYLKL
ID SEMG2_HYLKL Reviewed; 522 AA.
AC Q6X2M3;
DT 29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 40.
DE RecName: Full=Semenogelin-2;
DE AltName: Full=Semenogelin II;
DE Short=SGII;
DE Flags: Precursor;
GN Name=SEMG2;
OS Hylobates klossii (Kloss's gibbon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hylobatidae;
OC Hylobates.
OX NCBI_TaxID=9587;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14629036; DOI=10.1007/s00239-003-2474-x;
RA Jensen-Seaman M.I., Li W.-H.;
RT "Evolution of the hominoid semenogelin genes, the major proteins of
RT ejaculated semen.";
RL J. Mol. Evol. 57:261-270(2003).
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; AY259291; AAP86629.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6X2M3; -.
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; 2.
PE 3: Inferred from homology;
KW Repeat; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..522
FT /note="Semenogelin-2"
FT /id="PRO_0000032360"
FT REGION 26..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 272..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..522
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..158
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 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..410
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..468
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 469..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 522 AA; 59027 MW; CEBDF15E3359E1D7 CRC64;
MKSIILFVLS LLLILEKQAA VMGQKCGSKG QLPSGSSQFP RGQKGQHYSG QKDEQHTKSK
GSFSIQHTYH VDINDHDRTQ KSQQYDLNAQ HKMTKSKQHL GGSQELLNYK QEGRDHDKSK
DHFHMIVIHH KGGQAHRGTQ NPSQDQGNSP SGKGISSQYS NTEKRLWVHG LTKEQASASG
AQKGRTQGGS QSSYVLQTEE LVANKQQRET QNSPQNKGHY QNVVEMREEH SSKLQTSLHP
AYQDRLQHGP KDIFTTQDEL LVYNKNQHQT KNLNQDQEHG QKTHKISYQS SRTEERQLNR
GEKSVQKDVS KGGISIQTEE KIHGKSQNQV TIHSQGQEHG HKENKMSYQS SSTEERHLNC
GEKGIHKGVS KGSISIQTEE QIHGKSQNQV RIPSQAQEHG HKENKMSYQS SSTEERRLNY
GGKSMQKDVS QSSTSFHTEK LVEGKSQIQT PNPNQDQWSV QNAKGKSDQS AGREQDLLSH
EQKGRHQQES SEARNIVITE HEVAYDDHLT QQYNEDRNPV ST