ID A8K5A4_HUMAN Unreviewed; 1065 AA. AC A8K5A4; DT 04-DEC-2007, integrated into UniProtKB/TrEMBL. DT 04-DEC-2007, sequence version 1. DT 24-JAN-2024, entry version 84. DE SubName: Full=cDNA FLJ76826, highly similar to Homo sapiens ceruloplasmin (ferroxidase) (CP), mRNA {ECO:0000313|EMBL:BAF83908.1}; 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:BAF83908.1}; RN [1] {ECO:0000313|EMBL:BAF83908.1} RP NUCLEOTIDE SEQUENCE. 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; AK291219; BAF83908.1; -; mRNA. DR AlphaFoldDB; A8K5A4; -. DR GO; GO:0005765; C:lysosomal membrane; HDA:UniProtKB. DR GO; GO:0005507; F:copper ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW. DR CDD; cd04222; CuRO_1_ceruloplasmin; 1. DR CDD; cd11021; CuRO_2_ceruloplasmin; 1. DR CDD; cd04224; CuRO_3_ceruloplasmin; 1. DR CDD; cd11022; CuRO_4_ceruloplasmin; 1. DR CDD; cd04225; CuRO_5_ceruloplasmin; 1. DR CDD; cd11012; CuRO_6_ceruloplasmin; 1. DR Gene3D; 2.60.40.420; Cupredoxins - blue copper proteins; 5. DR InterPro; IPR048236; Ceruloplasmin-like_CuRO_5. DR InterPro; IPR011707; Cu-oxidase-like_N. DR InterPro; IPR001117; Cu-oxidase_2nd. DR InterPro; IPR011706; Cu-oxidase_C. DR InterPro; IPR045087; Cu-oxidase_fam. DR InterPro; IPR033138; Cu_oxidase_CS. DR InterPro; IPR002355; Cu_oxidase_Cu_BS. DR InterPro; IPR008972; Cupredoxin. DR PANTHER; PTHR11709:SF226; CERULOPLASMIN; 1. DR PANTHER; PTHR11709; MULTI-COPPER OXIDASE; 1. DR Pfam; PF00394; Cu-oxidase; 1. DR Pfam; PF07731; Cu-oxidase_2; 1. DR Pfam; PF07732; Cu-oxidase_3; 2. DR SUPFAM; SSF49503; Cupredoxins; 6. DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3. DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1. PE 2: Evidence at transcript level; KW Copper {ECO:0000256|ARBA:ARBA00022796}; KW Copper transport {ECO:0000256|ARBA:ARBA00022796}; KW Ion transport {ECO:0000256|ARBA:ARBA00023065}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}; KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}; KW Signal {ECO:0000256|SAM:SignalP}; KW Transport {ECO:0000256|ARBA:ARBA00023065}. FT SIGNAL 1..19 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 20..1065 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5002725445" FT DOMAIN 92..202 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF07732" FT DOMAIN 222..357 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF00394" FT DOMAIN 807..867 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF07732" FT DOMAIN 956..1057 FT /note="Plastocyanin-like" FT /evidence="ECO:0000259|Pfam:PF07731" SQ SEQUENCE 1065 AA; 122172 MW; F3D160D4F0B59C75 CRC64; MKILILGIFL FLCSTPAWAK EKHYYIGIIE TTWDYASDHG EKKLISVDTE HSNIYLQNGP DRIGRLYKKA LYLQYTDETF RTTIEKPVWL GFLGPIIKAE TGDKVYVHLK NLASRPYTFH SHGITYYKEH EGAIYPDNTT DFQRADDKVY PGEQYTYMLL ATEEQSPGEG DGNCVTRIYH SHIDAPKDIA SGLIGPLIIC KKDSLDKEKE KHIDREFVVM FSVVDENFSW YLEDNIKTYC SEPEKVDKDN EDFQESNRMY SVNGYTFGSL PGLSMCAEDR VKWYLFGMGN EVDVHAAFFH GQALTNKNYR IDTINLFPAT LFDAYMVAQS PGEWMLSCQN LNHLKAGLQA FFQVQECNKS SSKDNIRGKH VRHYYIAAEE IIWNYAPSGI DIFTKENLTA PGSDSAVFFE QGTTRIGGSY KKLVHREYTD ASFTNRKERG PEEEHLGILG PVIWAEVGDT IRVTFHNKGA YPLSIEPIGV RFNKNNEGTY YSPNYNPQSR SVPPSASHVA PTETFTYEWT VPKEVGPTNA DPVCLAKMYY SAVDPTKDIF TGLIGPMKIC KKGSLHANGR QKDVDKEFYL FPTVFDENES LLLEDNIRMF TTAPDQVDKE DEDFQESNKM HSMNGFMYGN QPGLTMCKGD SVVWYLFSAG NEADVHGVYF SGNTYLWRGE RRDTANLFPQ TSLTLHMWPD TEGTFNVECL TTDHYTGGMK QKYTVNQCRR QSEDSTFYLG ERTYYIAAVE VEWDYSPQRE WEKELHHLQE QNVSNAFLDK GEFYIGSKYK KVVYRQYTDS TFRVPVERKA EEEHLGILGP QLHADVGDKV KIIFKNMATR PYSIHAHGVQ TESSTVTPTL PGETLTYVWK IPERSGAGTE DSACIPWAYY STVDQVKDLY SGLIGPLIVC RRPYLKVFNP RRKLEFALLF LVFDENESWY LDDNIKTYSD HPEKVNKDDE EFIESNKMHA INGRMFGNLQ GLTMHVGDEV NWYLMGMGNE IDLHTVHFHG HSFQYKHRGV YSSDVFDIFP GTYQTLEMFP RTPGIWLLHC HVTDHFHAGM ETTYTVLQNE DTKSG //