UniProt: A0A2K5YWE4

Database: UniProt
Entry: A0A2K5YWE4_MANLE

LinkDB:  A0A2K5YWE4_MANLE 
Original site:  A0A2K5YWE4_MANLE

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Ontology (3)   
   GO (3)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (16)   
   InterPro (8)   
   Pfam (4)   
   PROSITE (3)   
   SMART (1)   
All databases (22)   

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ID   A0A2K5YWE4_MANLE        Unreviewed;      2102 AA.
AC   A0A2K5YWE4;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Coagulation factor VIII {ECO:0000313|Ensembl:ENSMLEP00000019865.1};
GN   Name=F8 {ECO:0000313|Ensembl:ENSMLEP00000019865.1};
OS   Mandrillus leucophaeus (Drill) (Papio leucophaeus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Mandrillus.
OX   NCBI_TaxID=9568 {ECO:0000313|Ensembl:ENSMLEP00000019865.1, ECO:0000313|Proteomes:UP000233140};
RN   [1] {ECO:0000313|Ensembl:ENSMLEP00000019865.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the multicopper oxidase family.
CC       {ECO:0000256|ARBA:ARBA00010609}.
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DR   STRING; 9568.ENSMLEP00000019865; -.
DR   Ensembl; ENSMLET00000043357.1; ENSMLEP00000019865.1; ENSMLEG00000034152.1.
DR   GeneTree; ENSGT00940000160294; -.
DR   OMA; TWDYAPH; -.
DR   Proteomes; UP000233140; Unplaced.
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; cd14452; CuRO_1_FVIII_like; 1.
DR   CDD; cd11015; CuRO_2_FVIII_like; 1.
DR   CDD; cd04227; CuRO_3_FVIII_like; 1.
DR   CDD; cd04228; CuRO_5_FVIII_like; 1.
DR   CDD; cd11018; CuRO_6_FVIII_like; 1.
DR   CDD; cd00057; FA58C; 1.
DR   Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 6.
DR   Gene3D; 2.60.120.260; Galactose-binding domain-like; 1.
DR   InterPro; IPR011707; Cu-oxidase-like_N.
DR   InterPro; IPR001117; Cu-oxidase_2nd.
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; 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; 1.
DR   PIRSF; PIRSF000354; Factors_V_VIII; 2.
DR   SMART; SM00231; FA58C; 1.
DR   SUPFAM; SSF49503; Cupredoxins; 6.
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:UP000233140};
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..2102
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5014442268"
FT   DOMAIN          1999..2102
FT                   /note="F5/8 type C"
FT                   /evidence="ECO:0000259|PROSITE:PS50022"
FT   REGION          718..739
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          868..920
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..689
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        1810..1836
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
FT   DISULFID        1877..1881
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000354-1"
SQ   SEQUENCE   2102 AA;  238978 MW;  716A564DE139380F CRC64;
     MQIELSTYFF LCLLRFCFSA TRRYYLGAVE LSWDYMQSDL GELPVDTRFP PRVPRSFPFN
     TSVMYKKTVF VEFTDHLFNI AKPRPPWMGL LGPTIQAEVY DTVVITLKNM ASHPVSLHAV
     GVSYWKASEG AEYDDQTSQR EKEDDKVFPG GSHTYVWQVL KENGPMASDP LCLTYSYLSH
     VDLVKDLNSG LIGALLVCRE GSLAKEKTQT LHKFVLLFAV FDEGKSWHSE TKNSLMQDRD
     DASARAWPKM HTVNGYVNRS LPGLIGCHRK SVYWHVIGMG TTPEVHSIFL EGHTFLVRNH
     RQASLEISPI TFLTAQTLLM DLGQFLLFCH ISSHQHDGME AYVKVDSCPE EPQLRMKNNE
     EAEDYDDDLA DSEMDVVRFD DDNSPSFIQI RSVAKKHPKT WVHYIAAEEE VWDYAPSVLA
     PDDRSYKSQY LNNGSQRIGR KYKKVRFMAY TDETFKTREA IQYESGILGP LLYGEVGDTL
     LIIFKNQASR PYNIYPHGIT DVRPLYSRRL PKGVKHLKDF PILPGEIFKY KWTVTVEDGP
     TKSDPRCLTR YYSSFINMER DLASGLIGPL LICYKESVDQ RGNQIMSDKR NVILFSVFDE
     NQSWYLTENI QRFLPNPVGV QLEDPEFQAS NIMHSINGYV FDSLQLSVCL HEVAYWYILS
     IGAQLWILGC HNSDFRNRGM TALLKVSSCD KNTGDYYEDS YEDISTYLLS KNNAIEPRSF
     SQNSRHPSPR QKQFNATTIP KNDIEKTDPW FAHRTPMPKV QNVSSSDLLM LLRQSPTPHG
     LSLSDLQEAK YETFSDDPSP GAIDTNNNLS KMTHLRPQPH HSGDMVFTPE PDLQLRLNEK
     LGTTVATELK KLDFKVSSSS NNLISTIPSD NLAAGNDNTS SLGPPNMPVH YESQLDTTLS
     GKKSSPLIES GGPLSLSEEN NDSKLLESGL MNSQESSWGK NVWSTESGRL FKEKRAHGPA
     LLTKDNALFK VSISLLKINK TSNNSATDRK THIDGPSLLV ENSPSVWQNI LESDTEFQKV
     TPLIHDRMLT DKNTTALRLN HMSNKTTSSK NMEMVQQKIE GPILPDAENP DMSFFKMLFL
     PESANWIQRT HGKNSLNSGQ GPSAKLFISL GPENSVEGQN FLSEKNKVVV GKGELTKDIG
     LKEIVFPSSR NLFLTNLDNL HENNTHNQEK KIQEEIERKE TLIQDNIVLP QIHTVTGTKN
     FMKNLFLLST RQNVEGSYEG AYAPVRQDFR SLSDSTNRTK NHMAHFSEKG EEENLEGLEN
     QTKQIVEKYP HTTRISPNPS QQNFVTQRGK RALKQFRLPL EETELEKRLI VEDTSTQWSK
     NIKHLTPSTL TQIDYNEKEK GAITQSPLSD CLTRSHSITQ ANRSPLPIAK VSSFPSIRPM
     DLTGVLFQDN FSHLPAPSYR KKDSGVQESS HFLQGVKKNN LSLAILTLEM IGDQREVGSL
     VTSATNSVTY KKVENTVFLK PGLPETSGKV ELLPKVRIYQ KDLFPTETSS GSPGHLDLME
     GSLLQETEGA IKWKEANRPG KIPFLRGATE SSAKTPSKLL DPLAWDNHYG TQIPKEEWKS
     QEKSPENTAF KKKDTILPLN PCESNHTIAA INEEQNEPQI EVTWAKQGGT ERLCSQNPPV
     LKRHQREITL NTLQSDQEEI DYDDTISVEM KKEDFDIYGE DENQSPRSFQ KKTRHYFIAA
     VERLWDYGMS SSPHVLRNRA QSGSVPQFKK VVFQEFTDGS FTQPLYRGEL NEHLGLLGPY
     IRAEVEDNIM VTFKNQASRP YSFYSSLISY EEDQRQGAEP RKNFVKPNET KTYFWKVQHH
     MAPTKDEFDC KAWAYFSDVD LEKDVHSGLI GPLLVCHTNT LNPAHGRQVT VQEFALFFTI
     FDETKSWYFT ENTGRNCRAP CNIQMEDPTF KENYRFHAIN GYIMDTLPGL VMAQDQRIRW
     YLLSMGSNEN IHSIHFSGHV FTVRKKEEYK MAVYNLYPGV FETVEMLPSK AGIWRVECLI
     GEHLHAGMST LFLVYSNKCQ TPLGMASGRI RDFQITASGQ YGQWAPKLAR LHYSGSINAW
     STKEPFSWIK VDLLAPMIIH GIKTQGARQK FSSLYISQFI IMYSLDGKKW QTYRGNSTGT
     LM
//

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