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SEMG2_PONAB
ID   SEMG2_PONAB             Reviewed;         581 AA.
AC   P0C7A4; A4K2V6; Q5U7N2; Q6X2M4;
DT   08-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 54.
DE   RecName: Full=Semenogelin-2;
DE   AltName: Full=Semenogelin II;
DE            Short=SGII;
DE   Flags: Precursor;
GN   Name=SEMG2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=17267810; DOI=10.1101/gr.6004607;
RG   NISC comparative sequencing program;
RA   Hurle B., Swanson W., Green E.D.;
RT   "Comparative sequence analyses reveal rapid and divergent evolutionary
RT   changes of the WFDC locus in the primate lineage.";
RL   Genome Res. 17:276-286(2007).
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; DP000045; ABO52991.1; -; Genomic_DNA.
DR   RefSeq; NP_001162046.1; NM_001168574.1.
DR   AlphaFoldDB; P0C7A4; -.
DR   STRING; 9601.ENSPPYP00000012344; -.
DR   PRIDE; P0C7A4; -.
DR   Ensembl; ENSPPYT00000012826; ENSPPYP00000012344; ENSPPYG00000032101.
DR   GeneID; 100137039; -.
DR   KEGG; pon:100137039; -.
DR   CTD; 6407; -.
DR   eggNOG; ENOG502T80H; Eukaryota.
DR   GeneTree; ENSGT00940000162560; -.
DR   HOGENOM; CLU_034710_0_0_1; -.
DR   InParanoid; P0C7A4; -.
DR   OMA; TEEKIHG; -.
DR   OrthoDB; 305064at2759; -.
DR   TreeFam; TF342360; -.
DR   Proteomes; UP000001595; Chromosome 20.
DR   GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR   GO; GO:0002020; F:protease binding; IEA:Ensembl.
DR   GO; GO:0008270; F:zinc ion binding; IEA:Ensembl.
DR   GO; GO:0019731; P:antibacterial humoral response; IEA:Ensembl.
DR   GO; GO:0050817; P:coagulation; IEA:Ensembl.
DR   GO; GO:1901318; P:negative regulation of flagellated sperm motility; IEA:InterPro.
DR   GO; GO:1900005; P:positive regulation of serine-type endopeptidase activity; IEA:Ensembl.
DR   InterPro; IPR008836; Semenogelin.
DR   Pfam; PF05474; Semenogelin; 1.
PE   3: Inferred from homology;
KW   Reference proteome; Repeat; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..581
FT                   /note="Semenogelin-2"
FT                   /id="PRO_0000329296"
FT   REGION          24..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          132..157
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          173..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          271..581
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        25..62
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..157
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..194
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        271..319
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        334..361
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        365..414
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..469
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        470..527
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        528..542
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        558..572
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   581 AA;  65733 MW;  534B6E3465DF7C15 CRC64;
     MKSIILFVLS LLLILEKQAA VMGQKGGSKG QSPSGSSQFP HGQKGQHYFG QKDQQHTKSK
     GSFSIQHTYH VDVNDHDRTR ESQQYDLNAL HKTRKSKQHL GGSQELLNYK QEGRDHDKSK
     GHFHMIVIHH KGGKAHRGTQ NPSQDQGNSP SGRGISSQYS NTEKRLWVHG LSKEQASASG
     AQKGRTQGRS QSSYVLQTEE LVANKQRETQ NSHQNKGHYQ NVVEVREKHS SKLQTSLRPA
     YQDRLQHGPK DIFTTQGELL VYDKNQHQTK NLNQDQEHGR KAHKISYQSS HTEERQLNHG
     EKSVQKDISK GRISIQTEEK IHGKSQNQVT IHSQDQEHGH KENKMSYQSS STEERHLNCG
     EKGIQKSVSK GSISIQTEEQ IHGKSQNQVR IPSQAQEYGH KENKISYQSS STEERRLNSG
     EKDIQKGVSK GSISIQTEEK IHGKSQDQVT IPSQDQEHGH KENKMSYQSS STEERRLNYG
     GKNTQKDVSQ SSISFQTEKL VEGKSQIQTP NPNQDQWSGQ NAKGKSGQSA DREQDLLSHE
     QKGRYQQESS AARNIVITEH EVARDDHLTQ QYNEDRNPIS T
 
 
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