(data stored in ACNUC19913 zone)

SWISSPROT: A8CZ27_MACMU

ID   A8CZ27_MACMU            Unreviewed;       461 AA.
AC   A8CZ27;
DT   13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2007, sequence version 1.
DT   30-AUG-2017, entry version 87.
DE   SubName: Full=Coagulation factor IX protein {ECO:0000313|EMBL:ABV25020.1};
OS   Macaca mulatta (Rhesus macaque).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9544 {ECO:0000313|EMBL:ABV25020.1};
RN   [1] {ECO:0000313|EMBL:ABV25020.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Wang J., Ding Y., Cheng J.;
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|SAAS:SAAS00748227}.
CC   -!- SIMILARITY: Belongs to the peptidase S1 family.
CC       {ECO:0000256|SAAS:SAAS00559343}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation
CC       of feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR   EMBL; EU128170; ABV25020.1; -; mRNA.
DR   RefSeq; NP_001103153.1; NM_001109683.1.
DR   UniGene; Mmu.17306; -.
DR   ProteinModelPortal; A8CZ27; -.
DR   MEROPS; S01.214; -.
DR   GeneID; 695578; -.
DR   KEGG; mcc:695578; -.
DR   CTD; 2158; -.
DR   eggNOG; ENOG410IGPV; Eukaryota.
DR   eggNOG; COG5640; LUCA.
DR   HOGENOM; HOG000251821; -.
DR   HOVERGEN; HBG013304; -.
DR   KO; K01321; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR   CDD; cd00190; Tryp_SPc; 1.
DR   Gene3D; 4.10.740.10; -; 1.
DR   InterPro; IPR017857; Coagulation_fac_subgr_Gla_dom.
DR   InterPro; IPR035694; Coagulation_factor_IX.
DR   InterPro; IPR001881; EGF-like_Ca-bd_dom.
DR   InterPro; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
DR   InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
DR   InterPro; IPR018097; EGF_Ca-bd_CS.
DR   InterPro; IPR000294; GLA_domain.
DR   InterPro; IPR009003; Peptidase_S1_PA.
DR   InterPro; IPR001314; Peptidase_S1A.
DR   InterPro; IPR001254; Trypsin_dom.
DR   InterPro; IPR018114; TRYPSIN_HIS.
DR   InterPro; IPR033116; TRYPSIN_SER.
DR   PANTHER; PTHR24256:SF397; PTHR24256:SF397; 1.
DR   Pfam; PF00008; EGF; 1.
DR   Pfam; PF00594; Gla; 1.
DR   Pfam; PF00089; Trypsin; 1.
DR   PRINTS; PR00722; CHYMOTRYPSIN.
DR   PRINTS; PR00001; GLABLOOD.
DR   SMART; SM00181; EGF; 2.
DR   SMART; SM00179; EGF_CA; 1.
DR   SMART; SM00069; GLA; 1.
DR   SMART; SM00020; Tryp_SPc; 1.
DR   SUPFAM; SSF50494; SSF50494; 1.
DR   SUPFAM; SSF57630; SSF57630; 1.
DR   PROSITE; PS00010; ASX_HYDROXYL; 1.
DR   PROSITE; PS00022; EGF_1; 1.
DR   PROSITE; PS01186; EGF_2; 1.
DR   PROSITE; PS50026; EGF_3; 1.
DR   PROSITE; PS01187; EGF_CA; 1.
DR   PROSITE; PS00011; GLA_1; 1.
DR   PROSITE; PS50998; GLA_2; 1.
DR   PROSITE; PS50240; TRYPSIN_DOM; 1.
DR   PROSITE; PS00134; TRYPSIN_HIS; 1.
DR   PROSITE; PS00135; TRYPSIN_SER; 1.
PE   2: Evidence at transcript level;
DR   PRODOM; A8CZ27.
DR   SWISS-2DPAGE; A8CZ27.
KW   Calcium {ECO:0000256|SAAS:SAAS00738281};
KW   Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00076,
KW   ECO:0000256|SAAS:SAAS00037407};
KW   EGF-like domain {ECO:0000256|PROSITE-ProRule:PRU00076,
KW   ECO:0000256|SAAS:SAAS00032677};
KW   Hydrolase {ECO:0000256|RuleBase:RU363034,
KW   ECO:0000256|SAAS:SAAS00731231};
KW   Protease {ECO:0000256|RuleBase:RU363034,
KW   ECO:0000256|SAAS:SAAS00732737};
KW   Secreted {ECO:0000256|SAAS:SAAS00749664};
KW   Serine protease {ECO:0000256|RuleBase:RU363034};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL        1     28       {ECO:0000256|SAM:SignalP}.
FT   CHAIN        29    461       {ECO:0000256|SAM:SignalP}.
FT                                /FTId=PRO_5002720431.
FT   DOMAIN       47     93       Gla (gamma-carboxy-glutamate).
FT                                {ECO:0000259|PROSITE:PS50998}.
FT   DOMAIN       93    129       EGF-like. {ECO:0000259|PROSITE:PS50026}.
FT   DOMAIN      227    459       Peptidase S1. {ECO:0000259|PROSITE:
FT                                PS50240}.
FT   DISULFID    119    128       {ECO:0000256|PROSITE-ProRule:PRU00076}.
SQ   SEQUENCE   461 AA;  51802 MW;  51D9CF79072EEF8C CRC64;
     MQRVNMIMAE SPGLITICLL GYLLSAECTV FLDHENANKI LNRPKRYNSG KLEEFVQGNL
     ERECMEEKCN FEEAREVFEN TEKTTEFWKQ YVDGDQCESN PCLNGGSCKD DINSYECWCP
     FGFEGKNCEL DVTCNIKNGR CKQFCKNTAD NKVVCSCTEG YRLAENQRSC EPAVPFPCGR
     VSVSQTSTLT RAETVFPDVE YVNSTEAETI LDNITQSTQS FNDFTRVVGG EDAKPGQFPW
     QVVLNGKVDA FCGGSIVNEK WVVTAAHCVE TDAKITVVAG EHNIEETEHT EQKRNVIRII
     PHHNYNATIN KYNHDIALLE LDEPLVLNSY VTPICIADKE YTNIFLKFGS GYVSGWGRVF
     NKGRSASVLQ YLRVPLVDRA TCLRSTKFTI YNNMFCAGFH EGGRDSCQGD SGGPHVTEVE
     GTSFLTGIIS WGEECAMKGK YGIYTKVSRY VNWIKEKTKL T
//

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