ID   SEMG2_ATEGE             Reviewed;         514 AA.
AC   Q5U7M7;
DT   29-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   07-DEC-2004, sequence version 1.
DT   02-JUN-2021, entry version 37.
DE   RecName: Full=Semenogelin-2;
DE   AltName: Full=Semenogelin II;
DE            Short=SGII;
DE   Flags: Precursor;
GN   Name=SEMG2;
OS   Ateles geoffroyi (Black-handed spider monkey) (Geoffroy's spider monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Atelidae;
OC   Atelinae; Ateles.
OX   NCBI_TaxID=9509;
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; AY781393; AAV51951.1; -; mRNA.
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   2: Evidence at transcript level;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..514
FT                   /note="Semenogelin-2"
FT                   /id="PRO_0000032356"
FT   REGION          24..514
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        47..61
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        69..83
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        98..129
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..164
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        177..244
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        323..346
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..406
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        453..482
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        491..514
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   514 AA;  56800 MW;  9C4180EE5DDFD70A CRC64;
     MKPIIFFVLS LLLILEKQAA VMGQKGGSKG RLPSESSQFP HGQKGQQYSA RKDKQHAESK
     GSASVEHTYP VDAHDHDQTR KSKQYDLNAQ NKTTKSEKHP AGSQESFNHK QKGREHGKSK
     GDFHVIVIHH KGGHAPHRTQ NPSQDQGNST SGKGIFNQDS NTKKRPLAPG LGKEQDSVSG
     AQRNRTQGGS QSSPVLQTKD LVPNKQPETQ NSQVPQNIGS SPNVNETKQK RSSKVQTPLC
     SAQEDRLQHG SKDVFSKNQN QTRGPNRDQE HGQKAPNRSC QCSSTEERPV NHREKGIQKD
     AFKGSTSNQT EDKIHDKSKK PVTTPGQDQQ DGHKANKTSS RSSGTEERQP NHGKKGIQKF
     AFKGSTSNQI EDKIHDTSQK PVTTPVQDQQ DGHKANKTSS RSSGTEERQP NHGEKGIQKD
     AFKGSTSNQT EDNIHDKPQK QITTSSQDQR SGQDAKGKSD QSADKEKDLL SHDQKGRHQE
     ESXGAHNIVI IEHEVSHDGH LAQHHDLDRN RLSI