ID H2R1R6_PANTR Unreviewed; 2351 AA.
AC H2R1R6; A0A2J8J4T5;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Coagulation factor VIII {ECO:0000313|Ensembl:ENSPTRP00000042755.4};
GN Name=F8 {ECO:0000313|Ensembl:ENSPTRP00000042755.4,
GN ECO:0000313|VGNC:VGNC:7458};
OS Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598 {ECO:0000313|Ensembl:ENSPTRP00000042755.4, ECO:0000313|Proteomes:UP000002277};
RN [1] {ECO:0000313|Ensembl:ENSPTRP00000042755.4, ECO:0000313|Proteomes:UP000002277}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16136131; DOI=10.1038/nature04072;
RG Chimpanzee sequencing and analysis consortium;
RT "Initial sequence of the chimpanzee genome and comparison with the human
RT genome.";
RL Nature 437:69-87(2005).
RN [2] {ECO:0000313|Ensembl:ENSPTRP00000042755.4}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC {ECO:0000256|ARBA:ARBA00010609}.
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DR EMBL; AACZ04059665; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC159217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC160653; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC163771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; XP_003317837.1; XM_003317789.3.
DR STRING; 9598.ENSPTRP00000042755; -.
DR PaxDb; 9598-ENSPTRP00000042755; -.
DR Ensembl; ENSPTRT00000049704.5; ENSPTRP00000042755.4; ENSPTRG00000022455.7.
DR GeneID; 473838; -.
DR KEGG; ptr:473838; -.
DR CTD; 2157; -.
DR VGNC; VGNC:7458; F8.
DR eggNOG; ENOG502QSFZ; Eukaryota.
DR GeneTree; ENSGT00940000160294; -.
DR HOGENOM; CLU_000948_1_0_1; -.
DR InParanoid; H2R1R6; -.
DR OrthoDB; 537265at2759; -.
DR TreeFam; TF329807; -.
DR Proteomes; UP000002277; Chromosome X.
DR Bgee; ENSPTRG00000022455; Expressed in heart and 22 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0007597; P:blood coagulation, intrinsic pathway; IBA:GO_Central.
DR CDD; cd14452; CuRO_1_FVIII_like; 1.
DR CDD; cd11015; CuRO_2_FVIII_like; 1.
DR CDD; cd04227; CuRO_3_FVIII_like; 1.
DR CDD; cd11016; CuRO_4_FVIII_like; 1.
DR CDD; cd04228; CuRO_5_FVIII_like; 1.
DR CDD; cd11018; CuRO_6_FVIII_like; 1.
DR CDD; cd00057; FA58C; 2.
DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 6.
DR Gene3D; 2.60.120.260; Galactose-binding domain-like; 2.
DR InterPro; IPR011707; Cu-oxidase-like_N.
DR InterPro; IPR011706; Cu-oxidase_C.
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; PTHR46806:SF7; COAGULATION FACTOR VIII; 1.
DR PANTHER; PTHR46806; F5/8 TYPE C DOMAIN-CONTAINING PROTEIN; 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; Cupredoxins; 6.
DR SUPFAM; SSF49785; Galactose-binding domain-like; 2.
DR PROSITE; PS01285; FA58C_1; 2.
DR PROSITE; PS01286; FA58C_2; 2.
DR PROSITE; PS50022; FA58C_3; 2.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR000354-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002277};
KW Signal {ECO:0000256|SAM:SignalP};
KW Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..2351
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015093263"
FT DOMAIN 2040..2188
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT DOMAIN 2193..2345
FT /note="F5/8 type C"
FT /evidence="ECO:0000259|PROSITE:PS50022"
FT REGION 906..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 941..961
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 172..198
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 267..348
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 547..573
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 649..730
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1851..1877
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 1918..1922
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT DISULFID 2040..2188
FT /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ SEQUENCE 2351 AA; 267012 MW; 50995F9C829B264F CRC64;
MQIELSTCFF LCLLRFCFSA TRRYYLGAVE LSWDYMQSDL GELPVDARFP PRVPKSFPFN
TSVVYKKTVF VEFTDHLFNI AKPRPPWMGL LGPTIQAEVY DTVVITLKNM ASHPVSLHAV
GVSYWKASEG AEYDDQTSQR EKEDDKVFPG GSHTYVWQVL KENGPMASDP LCLTYSYLSH
VDLVKDLNSG LIGALLVCRE GSLAKEKTQT LHKFILLFAV FDEGKSWHSE TKNSLMQDRD
AASARAWPKM HTVNGYVNRS LPGLIGCHRK SVYWHVIGMG TTPEVHSIFL EGHTFLVRNH
RQASLEISPI TFLTAQTLLM DLGQFLLFCH ISSHQHDGME AYVKVDSCPE EPQLRMKNNE
EAEDYDDDLT DSEMDVVRFD DDNSPSFIQI RSVAKKHPKT WVHYIAAEEE DWDYAPLVLA
PDDRSYKSQY LNNGPQRIGR KYKKVRFMAY TDETFKTREA IQHESGILGP LLYGEVGDTL
LIIFKNQASR PYNIYPHGIT DVRPLYSRRL PKGVKHLKDF PILPGEIFKY KWTVTVEDGP
TKSDPRCLTR YYSSFVNMER DLASGLIGPL LICYKESVDQ RGNQIMSDKR NVILFSVFDE
NRSWYLTENI QRFLPNPAGV QLEDPEFQAS NIMHSINGYV FDSLQLSVCL HEVAYWYILS
IGAQTDFLSV FFSGYTFKHK MVYEDTLTLF PFSGETVFMS MENPGLWILG CHNSDFRNRG
MTALLKVSSC DKNTGDYYED SYEDISAYLL SKNNAIEPRS FSQNSRHPST RQKQFNATTI
PENDIEKTDP WFAHRTPMPK VQNVSSSDLL MLLRQSPTPH GLSLSDLQEA KYETFSDDPS
PGAIDSNNSL SEMTHFRPQF HHSGDMVFTP ESGLQLRLNE KLGTTAATEL KKLDFKVSST
SNNLISTIPS DNLAAGTDNT SSLGPPSMPV HYDSQLDTTL FGKKSSPLTE SGRPLSLSEE
NNDSKLLESG LMNSQESSWG KNVSSTESGR LFKGKRAHGP ALLTKDNALF KVSISLLKTN
KTSNNSATNR KTHIDGPSLL IQSSPSVWQN ILESDTEFKK VTPLIHDRML MDKNATALRL
NHMSNKTTSS KNMEMVRQKK EGPIPPDAEN PDMSFFKMLF LPESASWIQR THGKNSLNSG
QGPSPKQLVS LGPEKSVEGQ NFLSEKNKVV VGKGEFTKDV GLKEMVFPSS RNLFLTNLDN
LHENNTHNQE KKIQEEIERK ETLIQENVVL PQIHTVTGTK NFMKNLFLLS TRQNVEGSYE
GAYAPVLQDF RSLNDSTNRT KKHTAHFSKK GEEENLAGLG NQTKQIVEKY ACTTRISPNT
SQQNFVTQRS KRALKQFRLP LEETELEKRI IVDDTSTQWS KNMKHLTPST LTQIDYNEKE
KGAITQSPLS DCLTRSHSIP QANRSPLPIA EVSSFPSIRP IYLTRVLFQD NSSHLPAASY
RKKDSGVQES SHFLQGAKKN NLSLAILTLE MTGDQREVGS LGTSATNSVT YKKVENTVLP
KPGLPKTSGK VELLPKVHIY QKDLFPTETS NGSPGHLDLV EGSLLQETEG AIKWNEANRP
GKIPFLRVAT ESSAKTPSKL LDPLAWDNHY GTQIPKEEWK SQEKSPEKTA FKKKDTILSL
NACESNHAIA AINEGQNKPE IEVTWAKQGR TERLCSQNPP GLKRHQREIT RTTLQSDQEE
IDYDDTISVE MKKEDFDIYD EDENQSPRSF QKKTRHYFIA AVERLWDYGM SSSPHVLRNR
AQSGSVPQFK KVVFQEFTDG SFTQPLYRGE LNEHLGLLGP YIRAEVEDNI MVTFKNQASR
PYSFYSSLIS YEEDQRQGAE PRKNFVKPNE TKTYFWKVQH HMAPTKDEFD CKAWAYFSDV
DLEKDVHSGL IGPLLVCHTN TLNPAHGRQV TVQEFALFFT IFDETKSWYF TENMERNCRA
PCNIQMEDPT FKENYRFHAI NGYIMDTLPG LVMAQDQRIR WYLLSMGSNE NIHSIHFSGH
VFTVRKKEEY KMALYNLYPG VFETVEMLPS KAGIWRVECL IGEHLHAGMS TLFLVYSNKC
QTPLGMASGH IRDFQITASG QYGQWAPKLA RLHYSGSINA WSTKEPFSWI KVDLLAPMII
HGIKTQGARQ KFSSLYISQF IIMYSLDGKK WQTYRGNSTG TLMVFFGNVD SSGIKHNIFN
PPIIARYIRL HPTHYSIRST LRMELMGCDL NSCSMPLGME SKAISDAQIT ASSYFTNMFA
TWSPSKARLH LQGRSNAWRP QVNNPKEWLQ VDFQKTMKVT GITTQGVKSL LTSMYVKEFL
ISSSQDGHHW TLFFQNGKVK VFQGNQDSFT PVVNSLDPPL LTRYLRIHPQ SWVHQIALRM
EVLGCEAQDL Y
//
