FA8_CANLF
ID FA8_CANLF Reviewed; 2343 AA.
AC O18806; O62730;
DT 24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Coagulation factor VIII;
DE AltName: Full=Procoagulant component;
DE Flags: Precursor;
GN Name=F8;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Liver;
RX PubMed=9493583;
RA Cameron C., Notley C., Hoyle S., McGlynn L., Hough C., Kamisue S.,
RA Giles A., Lillicrap D.;
RT "The canine factor VIII cDNA and 5' flanking sequence.";
RL Thromb. Haemost. 79:317-322(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Kidney;
RA Gordy P.W., Bowen R.A.;
RT "Characterization of the canine factor VIII cDNA.";
RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Factor VIII, along with calcium and phospholipid, acts as a
CC cofactor for factor IXa when it converts factor X to the activated
CC form, factor Xa. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with vWF. vWF binding is essential for the
CC stabilization of F8 in circulation (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space {ECO:0000250}.
CC -!- PTM: Proteolytically cleaved by cathepsin CTSG to produce a partially
CC activated form. {ECO:0000250|UniProtKB:P00451}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AF016234; AAB87412.1; -; mRNA.
DR EMBL; AF049489; AAC05384.1; -; mRNA.
DR RefSeq; NP_001003212.1; NM_001003212.1.
DR AlphaFoldDB; O18806; -.
DR SMR; O18806; -.
DR STRING; 9612.ENSCAFP00000029035; -.
DR PaxDb; O18806; -.
DR PRIDE; O18806; -.
DR GeneID; 403875; -.
DR KEGG; cfa:403875; -.
DR CTD; 2157; -.
DR eggNOG; ENOG502QSFZ; Eukaryota.
DR InParanoid; O18806; -.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000002254; Unplaced.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0006953; P:acute-phase response; IEA:UniProtKB-KW.
DR GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; -; 6.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR000421; FA58C.
DR InterPro; IPR024715; Factor_5/8-like.
DR InterPro; IPR008979; Galactose-bd-like_sf.
DR PANTHER; PTHR11709; PTHR11709; 3.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 2.
DR Pfam; PF00754; F5_F8_type_C; 2.
DR PIRSF; PIRSF000354; Factors_V_VIII; 1.
DR SMART; SM00231; FA58C; 2.
DR SUPFAM; SSF49503; SSF49503; 6.
DR SUPFAM; SSF49785; SSF49785; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 2.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
PE 2: Evidence at transcript level;
KW Acute phase; Blood coagulation; Calcium; Disulfide bond; Glycoprotein;
KW Hemostasis; Metal-binding; Reference proteome; Repeat; Secreted; Signal;
KW Sulfation.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..2343
FT /note="Coagulation factor VIII"
FT /id="PRO_0000002966"
FT DOMAIN 20..343
FT /note="F5/8 type A 1"
FT DOMAIN 20..199
FT /note="Plastocyanin-like 1"
FT DOMAIN 207..343
FT /note="Plastocyanin-like 2"
FT DOMAIN 393..724
FT /note="F5/8 type A 2"
FT DOMAIN 393..567
FT /note="Plastocyanin-like 3"
FT DOMAIN 577..724
FT /note="Plastocyanin-like 4"
FT DOMAIN 1705..2032
FT /note="F5/8 type A 3"
FT DOMAIN 1705..1869
FT /note="Plastocyanin-like 5"
FT DOMAIN 1879..2032
FT /note="Plastocyanin-like 6"
FT DOMAIN 2032..2180
FT /note="F5/8 type C 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DOMAIN 2185..2337
FT /note="F5/8 type C 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT REGION 752..774
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 754..1659
FT /note="B"
FT REGION 828..865
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1124..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1302..1326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1592..1632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 847..865
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1302..1323
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 385..386
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 753..754
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT SITE 1320..1321
FT /note="Cleavage (activation)"
FT /evidence="ECO:0000250"
FT SITE 1659..1660
FT /note="Cleavage (activation)"
FT /evidence="ECO:0000250"
FT SITE 1700..1701
FT /note="Cleavage; by thrombin"
FT /evidence="ECO:0000250"
FT MOD_RES 359
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 408
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 731
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 732
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 736
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 1675
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT MOD_RES 1691
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250"
FT CARBOHYD 233
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 253
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 877
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 921
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 937
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 938
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 956
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1007
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1037
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1062
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1069
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1080
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1179
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1193
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1275
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1341
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1391
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1419
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1429
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1453
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1547
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1618
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1821
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2129
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 2281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 2032..2180
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT DISULFID 2185..2337
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00081"
FT CONFLICT 293
FT /note="R -> G (in Ref. 2; AAC05384)"
FT /evidence="ECO:0000305"
FT CONFLICT 365
FT /note="D -> G (in Ref. 2; AAC05384)"
FT /evidence="ECO:0000305"
FT CONFLICT 480
FT /note="N -> K (in Ref. 2; AAC05384)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="F -> L (in Ref. 2; AAC05384)"
FT /evidence="ECO:0000305"
FT CONFLICT 603
FT /note="N -> D (in Ref. 2; AAC05384)"
FT /evidence="ECO:0000305"
FT CONFLICT 928
FT /note="S -> G (in Ref. 2; AAC05384)"
FT /evidence="ECO:0000305"
FT CONFLICT 1203
FT /note="P -> L (in Ref. 2; AAC05384)"
FT /evidence="ECO:0000305"
FT CONFLICT 1696
FT /note="N -> D (in Ref. 2; AAC05384)"
FT /evidence="ECO:0000305"
FT CONFLICT 2289
FT /note="G -> D (in Ref. 2; AAC05384)"
FT /evidence="ECO:0000305"
FT CONFLICT 2307
FT /note="R -> A (in Ref. 2; AAC05384)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2343 AA; 265831 MW; A854FAE571C3B399 CRC64;
MQVELYTCCF LCLLPFSLSA TRKYYLGAVE LSWDYMQSDL LSALHADTSF SSRVPGSLPL
TTSVTYRKTV FVEFTDDLFN IAKPRPPWMG LLGPTIQAEV YDTVVIVLKN MASHPVSLHA
VGVSYWKASE GAEYEDQTSQ KEKEDDNVIP GESHTYVWQV LKENGPMASD PPCLTYSYFS
HVDLVKDLNS GLIGALLVCK EGSLAKERTQ TLQEFVLLFA VFDEGKSWHS ETNASLTQAE
AQHELHTING YVNRSLPGLT VCHKRSVYWH VIGMGTTPEV HSIFLEGHTF LVRNHRQASL
EISPITFLTA QTFLMDLGQF LLFCHIPSHQ HDGMEAYVKV DSCPEEPQLR MKNNEDKDYD
DGLYDSDMDV VSFDDDSSSP FIQIRSVAKK HPKTWVHYIA AEEEDWDYAP SGPTPNDRSH
KNLYLNNGPQ RIGKKYKKVR FVAYTDETFK TREAIQYESG ILGPLLYGEV GDTLLIIFKN
QASRPYNIYP HGINYVTPLH TGRLPKGVKH LKDMPILPGE IFKYKWTVTV EDGPTKSDPR
CLTRYYSSFI NLERDLASGL IGPLLICYKE SVDQRGNQMM SDKRNVILFS VFDENRSWYL
TENMQRFLPN ADVVQPHDPE FQLSNIMHSI NGYVFDNLQL SVCLHEVAYW YILSVGAQTD
FLSVFFSGYT FKHKMVYEDT LTLFPFSGET VFMSMENPGL WVLGCHNSDF RNRGMTALLK
VSSCNRNIDD YYEDTYEDIP TPLLNENNVI KPRSFSQNSR HPSTKEKQLK ATTTPENDIE
KIDLQSGERT QLIKAQSVSS SDLLMLLGQN PTPRGLFLSD LREATDRADD HSRGAIERNK
GPPEVASLRP ELRHSEDREF TPEPELQLRL NENLGTNTTV ELKKLDLKIS SSSDSLMTSP
TIPSDKLAAA TEKTGSLGPP NMSVHFNSHL GTIVFGNNSS HLIQSGVPLE LSEEDNDSKL
LEAPLMNIQE SSLRENVLSM ESNRLFKEER IRGPASLIKD NALFKVNISS VKTNRAPVNL
TTNRKTRVAI PTLLIENSTS VWQDIMLERN TEFKEVTSLI HNETFMDRNT TALGLNHVSN
KTTLSKNVEM AHQKKEDPVP LRAENPDLSS SKIPFLPDWI KTHGKNSLSS EQRPSPKQLT
SLGSEKSVKD QNFLSEEKVV VGEDEFTKDT ELQEIFPNNK SIFFANLANV QENDTYNQEK
KSPEEIERKE KLTQENVALP QAHTMIGTKN FLKNLFLLST KQNVAGLEEQ PYTPILQDTR
SLNDSPHSEG IHMANFSKIR EEANLEGLGN QTNQMVERFP STTRMSSNAS QHVITQRGKR
SLKQPRLSQG EIKFERKVIA NDTSTQWSKN MNYLAQGTLT QIEYNEKEKR AITQSPLSDC
SMRNHVTIQM NDSALPVAKE SASPSVRHTD LTKIPSQHNS SHLPASACNY TFRERTSGVQ
EGSHFLQEAK RNNLSLAFVT LGITEGQGKF SSLGKSATNQ PMYKKLENTV LLQPGLSETS
DKVELLSQVH VDQEDSFPTK TSNDSPGHLD LMGKIFLQKT QGPVKMNKTN SPGKVPFLKW
ATESSEKIPS KLLGVLAWDN HYDTQIPSEE WKSQKKSQTN TAFKRKDTIL PLGPCENNDS
TAAINEGQDK PQREAMWAKQ GEPGRLCSQN PPVSKHHQRE ITVTTLQPEE DKFEYDDTFS
IEMKREDFDI YGDYENQGLR SFQKKTRHYF IAAVERLWDY GMSRSPHILR NRAQSGDVQQ
FKKVVFQEFT DGSFTQPLYR GELNEHLGLL GPYIRAEVED NIVVTFKNQA SRPYSFYSSL
ISYDEDEGQG AEPRRKFVNP NETKIYFWKV QHHMAPTKDE FDCKAWAYFS DVDLEKDVHS
GLIGPLLICR SNTLNPAHGR QVTVQEFALV FTIFDETKSW YFTENLERNC RAPCNVQKED
PTLKENFRFH AINGYVKDTL PGLVMAQDQK VRWYLLSMGS NENIHSIHFS GHVFTVRKKE
EYKMAVYNLY PGVFETVEML PSQVGIWRIE CLIGEHLQAG MSTLFLVYSK KCQTPLGMAS
GHIRDFQITA SGQYGQWAPK LARLHYSGSI NAWSTKDPFS WIKVDLLAPM IIHGIMTQGA
RQKFSSLYVS QFIIMYSLDG NKWHSYRGNS TGTLMVFFGN VDSSGIKHNI FNPPIIAQYI
RLHPTHYSIR STLRMELLGC DFNSCSMPLG MESKAISDAQ ITASSYLSSM LATWSPSQAR
LHLQGRTNAW RPQANNPKEW LQVDFRKTMK VTGITTQGVK SLLISMYVKE FLISSSQDGH
NWTLFLQNGK VKVFQGNRDS STPVRNRLEP PLVARYVRLH PQSWAHHIAL RLEVLGCDTQ
QPA
