ID A8KA37_HUMAN Unreviewed; 1090 AA. AC A8KA37; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 08-NOV-2023, entry version 73. DE SubName: Full=cDNA FLJ77213, highly similar to Homo sapiens coagulation factor VIII, procoagulant component (hemophilia A) (F8), transcript variant 1, mRNA {ECO:0000313|EMBL:BAF85591.1}; DE Flags: Fragment; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606 {ECO:0000313|EMBL:BAF85591.1}; RN [1] {ECO:0000313|EMBL:BAF85591.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Trachea {ECO:0000313|EMBL:BAF85591.1}; RA Wakamatsu A., Yamamoto J., Kimura K., Ishii S., Watanabe K., Sugiyama A., RA Murakawa K., Kaida T., Tsuchiya K., Fukuzumi Y., Kumagai A., Oishi Y., RA Yamamoto S., Ono Y., Komori Y., Yamazaki M., Kisu Y., Nishikawa T., RA Sugano S., Nomura N., Isogai T.; RT "NEDO human cDNA sequencing project."; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the multicopper oxidase family. CC {ECO:0000256|ARBA:ARBA00010609}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK292902; BAF85591.1; -; mRNA. DR AlphaFoldDB; A8KA37; -. DR PeptideAtlas; A8KA37; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProt. DR GO; GO:0005507; F:copper ion binding; 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; cd11016; CuRO_4_FVIII_like; 1. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 4. DR InterPro; IPR011707; Cu-oxidase-like_N. DR InterPro; IPR001117; Cu-oxidase_2nd. DR InterPro; IPR033138; Cu_oxidase_CS. DR InterPro; IPR008972; Cupredoxin. DR InterPro; IPR024715; Factor_5/8-like. 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; PF07732; Cu-oxidase_3; 2. DR PIRSF; PIRSF000354; Factors_V_VIII; 1. DR SUPFAM; SSF49503; Cupredoxins; 4. DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 1. PE 2: Evidence at transcript level; KW Disulfide bond {ECO:0000256|PIRSR:PIRSR000354-1}; KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..1090 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002722839" FT DOMAIN 90..197 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF07732" FT DOMAIN 224..348 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF00394" FT DOMAIN 454..572 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF07732" FT REGION 759..798 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" 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 COMPBIAS 759..783 FT /note="Polar residues" 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 NON_TER 1090 FT /evidence="ECO:0000313|EMBL:BAF85591.1" SQ SEQUENCE 1090 AA; 123201 MW; 040EA6D51B36A258 CRC64; MQIELSTCFF LCLLRFCFSA TRRYYLGAVE LSWDYMQSDL GELPVDARFP PRVPKSFPFN TSVVYKKTLF VEFTDHLFNI AKPRPPWMGL LGPTIQAEVY DTVVITLKNM ASHPVSLHAV GVSYWKASEG AEYDDQTSQR EKEDDKVFPG GSHTYVWQVL KENGPMASDP LCLTYSYLSH VDLVKDLNSG LIGALLVCRE GSLAKEKTQT LHKFILLFAV FDEGKSWHSE TKNSLMQDRD AASARAWPKM HTVNGYVNRS LPGLIGCHRK SVYWHVIGMG TTPEVHSIFL EGHTFLVRNH RQASLEIPPI TFLTAQTLLM DLGQFLLFCH ISSHQHDGME AYVKVDSCPE EPQLRMKNNE EAEDYDDDLT DSEMDVVRFD DDNSPSFIQI RSVAKKHPKT WVHYIAAEEE DWDYAPLVLA PDDRGYKSQY 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 IQNVSSSDLL MLSRQSPTPH GLSLSDLQEA KYETFSDDPS PGAIDSNNSL SEMTHFRPQL HHSGDMVFTP ESGLQLRLNE KLGTTAATEL KKLDFKVSST SNNLISTIPS DNLAAGTDNT SSLGPPSMPV HYDSQLDTTL FGKKSSPLTE SGGPLSLSEE NNDSKLLESG LMNSQESSWG KNVSSTESGR LFKGKRAHGP ALLTKDNALF KVSISLLKTN KTSNNSATNR KTHIDGPSLL IENSPSVWQN ILESDTEFKK VTPLIHDRML MDKNATALRL NHMSNKTTSS //