GenomeNet

Database: UniProt
Entry: G5B9E2_HETGA
LinkDB: G5B9E2_HETGA
Original site: G5B9E2_HETGA 
ID   G5B9E2_HETGA            Unreviewed;      2124 AA.
AC   G5B9E2;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 53.
DE   SubName: Full=Coagulation factor VIII {ECO:0000313|EMBL:EHB05903.1};
GN   ORFNames=GW7_15180 {ECO:0000313|EMBL:EHB05903.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB05903.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB05903.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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DR   EMBL; JH169117; EHB05903.1; -; Genomic_DNA.
DR   STRING; 10181.G5B9E2; -.
DR   eggNOG; ENOG502QSFZ; Eukaryota.
DR   InParanoid; G5B9E2; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   CDD; cd04227; CuRO_3_FVIII_like; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 7.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
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; 1.
DR   PIRSF; PIRSF000354; Factors_V_VIII; 3.
DR   SUPFAM; SSF49503; Cupredoxins; 7.
DR   SUPFAM; SSF49785; Galactose-binding domain-like; 1.
DR   PROSITE; PS01285; FA58C_1; 1.
DR   PROSITE; PS50022; FA58C_3; 1.
DR   PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1.
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:UP000006813};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..2124
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003474230"
FT   DOMAIN          2011..2124
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          802..835
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1310..1346
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        802..820
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        821..835
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1326..1341
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        214..240
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        309..390
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        590..616
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        692..773
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        1892..1918
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        1959..1963
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ   SEQUENCE   2124 AA;  240555 MW;  382788FDB98035AC CRC64;
     MQIELSICFF LCLLPFSFSA TRRYYLGAME LPWDYLQSDL LSELHVHTSF PPEMPRSFPF
     NSSVVYKKTV FVEFTDHLFN MAKPRPPWMG LLGPTIWAEV YDTVVITLKN MASHPVSLHA
     VGVSYWKASE GLLGPTIWAE VYDTVVITLK NMASHPVSLH AVGVSYWKAS EGAEYDDQTS
     QREKEDDKVF PGESHTYVWQ VSTENGPMTS DPQCLTYSYF SHVDLVKDLN SGLIGALLVC
     KEGSLTKERT QNLNQFVLLF AVFDEGKSWH SETKGLRTQA SDSASAGGWP KMHTVNGYVN
     RSLPGLIGCH RKSVYWHVIG MGTTPEVHSI FFEGHTFLVR NHRQASLEIS PITFLTAQTL
     LMDLGQFLLY CHISSHQHDG MEAYVKVDSC PEEPHLRMKE DEEEEDYDDD DDDLDSEMDV
     FRFDDDYSPF IQIRSAAKKH PKTWIHYIAA EEEDWDYAPS VHASDDRSYK SQYLNNGPQQ
     IGRKYKKIRF MAYTDETFKT RETIQYESGI LGPLLYGEVG DTLLIIFKNK ASRPYNIYPH
     GISDVSPLHS RRLPKGIKHL KDLPILPGKI FKYKWTVTIE DGPTKSDPRC LTRYYSSFLN
     PERDLASGLI GPLLICYKES VDQRGNQMMS DKRNVILFSV FDENRSWYLT ENMQRFLPNV
     AGVQAQDPEF QASNIKYSIN GYVFDSLQLS ACLHEVAYWY ILSVGAQTDF LSVFFSGYTF
     KHKMVYEDTL TLFPFSGETV FMAMENPGLW VLGCHNSDFR SRGMTALLKV SSCGRSTGDY
     YEDTYEDIPT YLLSENHIIE PRSFSQNSRH PTTRQKQFKA TTTAENDKEK TDPQFGERTG
     MVKVHNVFSS DLSMLLGQSP TPHGLSLSDI PKATYEALPD DYLPGAIDNN EGPSKVVHIR
     PELYQSGDTG FTPEPSLQLR VNENLGTTIA VELKKLDLEV SSSPNNLMVS PAILADNLAA
     GPEETSSLGS PNMPVSSQLS TSVLDKKPSP LIGAGVHLSL SERNNESKLL EGVLVNIQES
     SLGKNILSME SDMSLKEKTA HGPALLTKDN VLFKVNISLI KTNKTSNYST TNQKTHIDRP
     TLLIENSTSV WQGTILERDT EFQRVTSLIH DEVPMDKNTT ALRLNHMSNK TTSSKNLEIV
     DQKQADLVPS DEENPDVLFF KMLFLPEPAN WNNGTNGKNS LNSGQGPSPK QLLSLGSELS
     GEHQNFLTEE NKVVVENEFT KDAGPKELIP NNKSILLTNL ANVKDNDTHN QEKTIQEEIN
     QKKELTQENV VLPQVYTVTG TKNFLKKLFL LSTRQNISLD EGTYAPTLPD TKLLNNSTNR
     AKIHKPRFSQ RQEEEETNQD SSRNQTKQMV DKYLSTAGMF PNPSQKNITA QRGKRSLKQF
     RFPLEETEVE KGLIVDDPST QRSKNLKYLP QIDYKEKEGK AITQSPLSIS PMRNHSIDQI
     KSFALPIAKI SAPPFIRPTD LTQISSQDSS SHFLASTCNY SLKAKSPMAQ EDSHFLQVPK
     INNLSLAILP LEIIRKQGKV GSLGTSATNS VAYKKLENTV LLKPVLPETF GKVELLPKVP
     IRQEDLLLTE TIHESPVHLD HTEEILLQTT TKTIKWSKTN GPGKAPFLKG TTESSEKMNS
     KLLGPLVLGN QYATQMPKDK WRSQEKSPKN TVLKKKDSVL SLIPSESNCT IVAISDGQNR
     LQGEATGGKQ GGTGKLCPPN PLVLKRHQRE TTSITLQSEQ EDVYYDDAIS GETKRDFEIY
     GEDENQGPRS FQKRTRHYFI AAVERLWDYG MSRIPSVLRN RDQSGSAYQF KKVVFQEFTD
     GSFTQPLYRG ELNEHLGLLG PYLRAEVEDN IVVTFKNQAS RPYSFYSSLI SYKDDQKQEA
     EPRKNFVKPN ETKTYFWEVQ QHMAPTEDEF DCKAWAYFSD VDLEKDMHTG LIGPLLICHR
     NTLSPAHGRQ VTVQEFALLF TIFDETKSWY FTENMERNCK EPCSTQVEDP TFKENYRFHA
     INGYVMDTLP GLVMAQNQRI RWYLLSMGSN ENIHSIHFSG HVFTVRKKEE YKMAVYNLYP
     GQWAPKLARL HYSGLINAWS TKEPFSWIKV DLLTPMIIHG IKTQGARQKF SSLYISQFII
     MYSLDGKKWL TYRGNSTGTL MVCK
//
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