ID E3TF85_ICTPU Unreviewed; 456 AA.
AC E3TF85;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Coagulation factor VII {ECO:0000313|EMBL:ADO28971.1, ECO:0000313|RefSeq:NP_001187676.1};
DE EC=3.4.21.21 {ECO:0000313|RefSeq:NP_001187676.1};
GN Name=FA7 {ECO:0000313|EMBL:ADO28971.1};
GN Synonyms=f7i {ECO:0000313|RefSeq:NP_001187676.1}, fa7
GN {ECO:0000313|RefSeq:NP_001187676.1};
OS Ictalurus punctatus (Channel catfish) (Silurus punctatus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Siluriformes;
OC Ictaluridae; Ictalurus.
OX NCBI_TaxID=7998 {ECO:0000313|EMBL:ADO28971.1};
RN [1] {ECO:0000313|EMBL:ADO28971.1, ECO:0000313|RefSeq:NP_001187676.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=20634964; DOI=10.1371/journal.pone.0011546;
RA Chen F., Lee Y., Jiang Y., Wang S., Peatman E., Abernathy J., Liu H.,
RA Liu S., Kucuktas H., Ke C., Liu Z.;
RT "Identification and characterization of full-length cDNAs in channel
RT catfish (Ictalurus punctatus) and blue catfish (Ictalurus furcatus).";
RL PLoS ONE 5:E11546-E11546(2010).
RN [2] {ECO:0000313|RefSeq:NP_001187676.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=23127152; DOI=10.1186/1471-2164-13-595;
RA Liu S., Zhang Y., Zhou Z., Waldbieser G., Sun F., Lu J., Zhang J.,
RA Jiang Y., Zhang H., Wang X., Rajendran K.V., Khoo L., Kucuktas H.,
RA Peatman E., Liu Z.;
RT "Efficient assembly and annotation of the transcriptome of catfish by RNA-
RT Seq analysis of a doubled haploid homozygote.";
RL BMC Genomics 13:595-595(2012).
RN [3] {ECO:0000313|RefSeq:NP_001187676.1}
RP IDENTIFICATION.
RG RefSeq;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the osteocalcin/matrix Gla protein family.
CC {ECO:0000256|ARBA:ARBA00008850}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}.
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DR EMBL; GU589019; ADO28971.1; -; mRNA.
DR RefSeq; NP_001187676.1; NM_001200747.1.
DR STRING; 7998.ENSIPUP00000016294; -.
DR GeneID; 100528477; -.
DR KEGG; ipu:100528477; -.
DR CTD; 282671; -.
DR OrthoDB; 4629979at2759; -.
DR Proteomes; UP000221080; Chromosome 26.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
DR GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR GO; GO:0007596; P:blood coagulation; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00054; EGF_CA; 1.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 4.10.740.10; Coagulation Factor IX; 1.
DR Gene3D; 2.10.25.10; Laminin; 2.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 2.
DR InterPro; IPR017857; Coagulation_fac-like_Gla_dom.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR035972; GLA-like_dom_SF.
DR InterPro; IPR000294; GLA_domain.
DR InterPro; IPR012224; Pept_S1A_FX.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001314; Peptidase_S1A.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR PANTHER; PTHR24278; COAGULATION FACTOR; 1.
DR PANTHER; PTHR24278:SF26; COAGULATION FACTOR VII; 1.
DR Pfam; PF00008; EGF; 1.
DR Pfam; PF14670; FXa_inhibition; 1.
DR Pfam; PF00594; Gla; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF001143; Factor_X; 1.
DR PRINTS; PR00722; CHYMOTRYPSIN.
DR PRINTS; PR00001; GLABLOOD.
DR SMART; SM00181; EGF; 2.
DR SMART; SM00069; GLA; 1.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF57196; EGF/Laminin; 1.
DR SUPFAM; SSF57630; GLA-domain; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 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.
PE 2: Evidence at transcript level;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE-
KW ProRule:PRU00076};
KW Signal {ECO:0000256|SAM:SignalP, ECO:0000313|RefSeq:NP_001187676.1}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 19..456
FT /evidence="ECO:0000256|SAM:SignalP,
FT ECO:0000313|RefSeq:NP_001187676.1"
FT /id="PRO_5011323948"
FT DOMAIN 37..83
FT /note="Gla"
FT /evidence="ECO:0000259|PROSITE:PS50998"
FT DOMAIN 83..119
FT /note="EGF-like"
FT /evidence="ECO:0000259|PROSITE:PS50026"
FT DOMAIN 186..428
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT DISULFID 109..118
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076"
SQ SEQUENCE 456 AA; 50475 MW; 089832B621EB8B40 CRC64;
MKSETFLVLC LFCHAVSGAV FLRRNDANSV LRRFRRANSG LLEELKKGNL ERECVEEICD
YEEAREVFED EAITKQFWIS YHAREPCLTN PCKNNGTCIY LGHSYICQCS EGFEGKYCQE
AFEDTLKCLY LNGGCEQFCD GSAWKRKCAC APGYALGEDK KSCIAQVQYP CGKAPLEITQ
TVLPRAVGGN QCPKGHYPWQ VLLKYDGQSL CGGVLLDTNW ILTAAHCVAK KDIKKLKVIA
GDHNIDQVEG TEQTFSVSHV IIHESYDPAS ADSDLALLRL SEPATLSNHT IPICLPTSEF
ARMELEAVRF HTVSGWGQHT VGGNVRTSQS VKSIAPVLRT LAVPFLPKPE CSIKSGVNIT
DNMLCTGYFE GSQESCRGDD GSPLTTQYKD THFLTGIVSW GKGCAHPGFY AIYTKVANFL
DWLQRGMATP IAHPDAFNTS RASVMTTPPA EQFTWN
//
