UniProt: A0A455ANQ7

Database: UniProt
Entry: A0A455ANQ7_PHYMC

LinkDB:  A0A455ANQ7_PHYMC 
Original site:  A0A455ANQ7_PHYMC

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Ontology (3)   
   GO (3)   
Protein sequence (1)   
   RefSeq(pep) (1)   
Protein domain (15)   
   InterPro (7)   
   Pfam (3)   
   PROSITE (4)   
   SMART (1)   
All databases (19)   

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ID   A0A455ANQ7_PHYMC        Unreviewed;      2217 AA.
AC   A0A455ANQ7;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Coagulation factor VIII isoform X4 {ECO:0000313|RefSeq:XP_028338217.1};
GN   Name=F8 {ECO:0000313|RefSeq:XP_028338217.1};
OS   Physeter macrocephalus (Sperm whale) (Physeter catodon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Whippomorpha; Cetacea; Odontoceti;
OC   Physeteridae; Physeter.
OX   NCBI_TaxID=9755 {ECO:0000313|Proteomes:UP000248484, ECO:0000313|RefSeq:XP_028338217.1};
RN   [1] {ECO:0000313|RefSeq:XP_028338217.1}
RP   IDENTIFICATION.
RC   TISSUE=Muscle {ECO:0000313|RefSeq:XP_028338217.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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DR   RefSeq; XP_028338217.1; XM_028482416.2.
DR   Proteomes; UP000248484; Chromosome 21.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProt.
DR   GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd04227; CuRO_3_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; 1.
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; 3.
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:UP000248484};
KW   Sulfation {ECO:0000256|ARBA:ARBA00022641}.
FT   DOMAIN          1906..2054
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   DOMAIN          2058..2211
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          1..23
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          629..651
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          771..790
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1001..1029
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1181..1200
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1001..1028
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        48..74
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        138..219
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        416..442
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        518..599
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        1717..1743
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        1784..1788
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        1906..2054
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ   SEQUENCE   2217 AA;  251695 MW;  AFCF09CAB6F627E2 CRC64;
     MKHKKGAEYE DKTSQREKED DKVIPGKSHT YVWQVLKENG PTASDPPCLT YSYLSHVDLV
     KDVNSGLIGA LLVCREGSLT KERTQTLHGF VLLFAVFDEG KSWHSGKNES LTQAMDPASA
     MHTINGYINR SLPGLIGCHK KSVYWHVIGM GTTPEVHSVF LEGHTFLVRN HRQASLEISP
     ITFLTAQTLL MDLGQFLLFC HISSHQHDGM EAYVTVHSCP EEPHIWMKSN EEEDYDDFDD
     SDMDVIRFDG DSAPPFIQIR SVAKKRPKTW VHHIAAEEED WDYAPSVPPS ADRSYKSLYL
     NNGPQRIGRK YKKVRFIAYT DETFKTREAI QYESGILGPL LYGEVGDTLL IIFKNKASRP
     YNIYPHGITD VSPLHSGRFP KGVKHLKDMP ILPGEIFKYK WTVTVEDGPT KSDPRCLTRY
     YSSFVNPERD LASGLIGPLL ICYKESVDQR GNQMMSDKRN VILFSVFDEN QSWYLTENIQ
     RFLPNADGVQ PQDPEFQVSN IMHSINGYVF DSLQLSVCLH EVAYWYILSI GAQTDFLSVF
     FSGYTFKHKM VYEDTLTLFP FSGETVFMSM ENPGLWVLGC HNSDFRNRGM TALLKVYSCD
     RNTGDYYEDT YEDIPTLLLN ENNVIEPRSF SQNSRHPSTR QMQFKATTTP ENDIEKTDLQ
     SGERMQLLKE QSVSSSDLLM LLGQNPTPHG LSLSDLQEAR NKANDHLPRA IERNKGPSEV
     AHLTPELHHS GERVSTPEPE LPLRLNENLG TTVTVELKKL DFKISSSSNN LMTPPTIPSD
     KLSAGTEKTG SLGPPNMPVN FSSQLGAIVF GKNSSHFIGF AVPLGLSKED NDSKSLEAVL
     TNSQESSLGE NVLSVESDRL FKEEGVRGPA SLTKDDALFQ VNISLVKTNK APVNSTTSTK
     THIDDPAFLI ENSTSVWQDI TLESNTEFQE VTSLIHGEMF MDKNTTALGL NHVSNKTTSS
     KNMETIHQNK EGSVPLDAEY PDTSFFKTLF LPDSTNWIKR THGKNSLSSG QRPNPKQLTS
     SGSEKSVKDQ NFLSEKNKVV VGEDELSKGT GFKEMIFPNS KNVFLTNLAN VQENDTHNQE
     KKSQEDIERK EKLIQENVVL PQVYTVTGTK NFLKNLFSLS TKQNVEGLDE ETYTPVLQDS
     RSLNGSAKRA GIHVAHFSKI REEANLEDLG NQTKQMLDKY PSTTKMSPIP SQQKAIPQRD
     KRDLKQFRLP LEELRLERGV ILNDTSTQWS KNMKYLTQGT FTQIEYNRKE KRAITQSFLS
     DCSMRSHDII QTNGSALPIA QVSVFPSIRP TDLTKTPSQD NSSRPPASIC SYSFVERSSG
     VQESSHFLQG GKRNNLSLAF LTLEVIGGQR KINALGKRAT NLLRYKKLEN TVLLKPGLPE
     ASGKVIHQED FFHTKTSNGS PAHLDLREEI FLQKTQGLVK LNKVNRPGKV PFLKWATESS
     ENTPPKLLGP LAWDNQYATL IPREEKSLEK SQKHTAFKTK DIILPLDPCE NNHSIAAINE
     VQDKTQREAT WVKQGGTGRL WSQNPPVLKR HQREITLTTF QPEEDKIDYD DTFSVDTKRE
     DFDIYDEDEN QDPRSFQKRT RHYFIAAVER LWDYGMNRSP HALRNRAENG DVPQFKKVVF
     EEFADGSFTQ PLYRGELNEH LGLLGPYIRA EVEDNIMVTF KNQASRPYSF YSSLISYEED
     QRQGAEPRKK FVRPNETKTY FWKVQHHMAP TKDEFDCKAW AYFSDVDLEK DVHSGLIGPL
     LICRTNTLSA AHGRQVTVQE FALFFTIFDE TKSWYFTENM ERNCRAPCNI QMEDPTFREK
     YRFHAINGYV MDTLPGLAMA QDQKIRWYLL SMGSNENIHS IHFSGHVFTV RKKEEYKMAV
     YNLYPGVFET VEMLPSKVGI WRIECLIGEH LQAGMSTLFL VYSKKCQTPL GMASGRIRDF
     QITASGQYGQ WAPKLARLHY SGSINAWSTK DPFSWIKVDL LAPMIIHSIM TQGARQKLSS
     LYISQFIIMY SLDGKQWRSY RGNSTGTLMV FFGNVDSSGI KHNIFNPPII ARYVRLHPTH
     YSIRSTLRME LMGCDLNSCN MALGMESKAI SDAQITASSH LSNVFATWSP SQARLHLQGR
     TNAWRPRANN RKEWLQVDFQ KTMRVTGITT QGVKSLLTSM YVKEFLISSS QDGHNWTLLL
     QNGKVKIFQG NQDSFTPVVN ALEPPLFTRF LRIHPQSWAH HIALRLELLG CEAQQQY
//

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