CERU_SHEEP
ID CERU_SHEEP Reviewed; 1048 AA.
AC Q9XT27;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Ceruloplasmin;
DE EC=1.16.3.1;
DE AltName: Full=Ferroxidase;
DE Flags: Precursor;
GN Name=CP;
OS Ovis aries (Sheep).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Ovis.
OX NCBI_TaxID=9940;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=10452945; DOI=10.1016/s0378-1119(99)00276-0;
RA Lockhart P.J., Mercer J.F.B.;
RT "Cloning and expression analysis of the sheep ceruloplasmin cDNA.";
RL Gene 236:251-257(1999).
CC -!- FUNCTION: Ceruloplasmin is a blue, copper-binding (6-7 atoms per
CC molecule) glycoprotein. It has ferroxidase activity oxidizing Fe(2+) to
CC Fe(3+) without releasing radical oxygen species. It is involved in iron
CC transport across the cell membrane (By similarity). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(2+) + 4 H(+) + O2 = 4 Fe(3+) + 2 H2O;
CC Xref=Rhea:RHEA:11148, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:15379, ChEBI:CHEBI:29033, ChEBI:CHEBI:29034; EC=1.16.3.1;
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378; Evidence={ECO:0000250};
CC Note=Binds 6 Cu cations per monomer. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Secreted.
CC -!- TISSUE SPECIFICITY: Expressed by the liver and secreted in plasma. Also
CC expressed in the hypothalamus, spleen and uterus. No expression in the
CC cortex, heart, intestine or kidney. {ECO:0000269|PubMed:10452945}.
CC -!- SIMILARITY: Belongs to the multicopper oxidase family. {ECO:0000305}.
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DR EMBL; AF134814; AAD41477.1; -; mRNA.
DR RefSeq; NP_001009733.1; NM_001009733.1.
DR AlphaFoldDB; Q9XT27; -.
DR SMR; Q9XT27; -.
DR STRING; 9940.ENSOARP00000005423; -.
DR GeneID; 443053; -.
DR KEGG; oas:443053; -.
DR CTD; 1356; -.
DR eggNOG; KOG1263; Eukaryota.
DR OrthoDB; 454773at2759; -.
DR Proteomes; UP000002356; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004322; F:ferroxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0006825; P:copper ion transport; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.420; -; 5.
DR InterPro; IPR001117; Cu-oxidase.
DR InterPro; IPR011706; Cu-oxidase_C.
DR InterPro; IPR045087; Cu-oxidase_fam.
DR InterPro; IPR011707; Cu-oxidase_N.
DR InterPro; IPR033138; Cu_oxidase_CS.
DR InterPro; IPR002355; Cu_oxidase_Cu_BS.
DR InterPro; IPR008972; Cupredoxin.
DR PANTHER; PTHR11709; PTHR11709; 3.
DR Pfam; PF00394; Cu-oxidase; 1.
DR Pfam; PF07731; Cu-oxidase_2; 1.
DR Pfam; PF07732; Cu-oxidase_3; 3.
DR SUPFAM; SSF49503; SSF49503; 6.
DR PROSITE; PS00079; MULTICOPPER_OXIDASE1; 3.
DR PROSITE; PS00080; MULTICOPPER_OXIDASE2; 1.
PE 2: Evidence at transcript level;
KW Copper; Copper transport; Glycoprotein; Ion transport; Metal-binding;
KW Oxidoreductase; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Signal; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1048
FT /note="Ceruloplasmin"
FT /id="PRO_0000227940"
FT DOMAIN 20..357
FT /note="F5/8 type A 1"
FT DOMAIN 20..200
FT /note="Plastocyanin-like 1"
FT DOMAIN 209..355
FT /note="Plastocyanin-like 2"
FT DOMAIN 370..712
FT /note="F5/8 type A 2"
FT DOMAIN 370..554
FT /note="Plastocyanin-like 3"
FT DOMAIN 564..710
FT /note="Plastocyanin-like 4"
FT DOMAIN 724..1044
FT /note="F5/8 type A 3"
FT DOMAIN 724..894
FT /note="Plastocyanin-like 5"
FT DOMAIN 902..1040
FT /note="Plastocyanin-like 6"
FT BINDING 120
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 122
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 180
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 182
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 295
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 338
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="4"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 650
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 693
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 698
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 703
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="5"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 977
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 980
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="1"
FT /note="type 2 copper site"
FT /evidence="ECO:0000250"
FT BINDING 982
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1022
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="3"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1023
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1024
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="2"
FT /note="type 3 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1028
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT BINDING 1033
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="6"
FT /note="type 1 copper site"
FT /evidence="ECO:0000250"
FT MOD_RES 716
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P00450"
FT CARBOHYD 138
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 227
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 556
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 582
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 756
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 920
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1048 AA; 119126 MW; 925F16D7B0549CBB CRC64;
MKIFLLCIFL ILCGTSVWAK DKHYYIGIIE TAWNYASDHA EKKLISVDTE HSNIYLQNGP
NRIGSVYKKA VYLQYTDENF RTVIEKPVWL GFLGPIIKAE TGDKVYVHLK NFASRPYTFH
AHGLTYYKEH EGAIYPDNTT DLQKADDKVQ PGEQCLYILH ANPEQGPGEE DSNCVTRIYH
SHIDAPKDIA SGLIGPLIHC KKDSLDEEKE KNIDKEFVVM FSVVDENLSW YLEENIKTYC
SEPEKVEQDN EDFQESNRMY SVNGYAFGSL PGLSMCAEDR VKWYLFGMGN EIDVHAAFFH
GQVLTSKNYR VDTINLFPAT LFDAFMVAQN PGQWMLSCQN LNHLKAGLQA FFWVQDCKKS
SSEDNIHGKN VRHYYIAAEE VIWNYAPSGI DAFTKENLRA PGSASEAFFE QGPTRIGGSY
KKLVYREYTD ASFSNQKERG PEEEHLGILG PVIAAEVGDT IRVTFHNKAA HPLSIEPIGV
RVDKNNEGTY YSPTGSGPPP SGSHVAPKGT FTYEWTVPKE VGPTYKDPVC LAKMYYSGST
KDIFTGLIGP MKICRNGSLL ANGRLKNVDK EFYLFPTVFD ENESLLLDDN IKMFTTAPDQ
VDKENEDFQE SNKMHSMNGF MYGNQPGLSM CQGDSVMWYL FSAGNEVDIH GIYFSGNTYL
SRGERRDTAN LFPQTSLSLF MQPDTAGTFD VECLTTDHYT GGMKQKYTVS QCGQRSEDLY
LYLGERTYYI AAVEVEWDYS PSRKWEKELH HLQEQNLSNA FLDKEEFYIG SKYKKVVYRQ
FTDSTFQVPV ERKGEEEHLG ILGPQLHADV GDKVNIIFKN MATRPYSIHA HGVKTESSTV
TPTAPGETRT YIWKIPERSG AGMGDSPCIP WVYYSTVDRV KDLFSGLIGP LIVCRKHYLK
VSNPIKKLEF SLLFLVFDEN ESWYLDDNIK TYSDHPEKVD KANEEFMESN KMHAINGRMF
GNLQGLTMHV GNEVDLHSVH FHGHSFQYQH RGIYTSDVFD LFPGTYQTLE MTPKTPGIWL
LHCHVTDHIH AGMETTYTVL PNEEIKSG
