ID A0A3L8SCZ5_CHLGU Unreviewed; 182 AA.
AC A0A3L8SCZ5;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=Copper transport protein {ECO:0000256|RuleBase:RU367022};
GN ORFNames=DV515_00008936 {ECO:0000313|EMBL:RLW00325.1};
OS Chloebia gouldiae (Gouldian finch) (Erythrura gouldiae).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Passeriformes; Passeroidea; Passeridae;
OC Chloebia.
OX NCBI_TaxID=44316 {ECO:0000313|EMBL:RLW00325.1, ECO:0000313|Proteomes:UP000276834};
RN [1] {ECO:0000313|EMBL:RLW00325.1, ECO:0000313|Proteomes:UP000276834}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Red01 {ECO:0000313|EMBL:RLW00325.1};
RC TISSUE=Muscle {ECO:0000313|EMBL:RLW00325.1};
RX PubMed=30282656;
RA Toomey M.B., Marques C.I., Andrade P., Araujo P.M., Sabatino S.,
RA Gazda M.A., Afonso S., Lopes R.J., Corbo J.C., Carneiro M.;
RT "A non-coding region near Follistatin controls head colour polymorphism in
RT the Gouldian finch.";
RL Proc. R. Soc. B 285:0-0(2018).
CC -!- FUNCTION: Mobilizes copper(1+) out of the endosomal compartment, making
CC copper(1+) available for export out of the cells.
CC {ECO:0000256|ARBA:ARBA00037299}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Ag(+)(out) = Ag(+)(in); Xref=Rhea:RHEA:75207,
CC ChEBI:CHEBI:49468; Evidence={ECO:0000256|ARBA:ARBA00036430};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cu(+)(out) = Cu(+)(in); Xref=Rhea:RHEA:75211,
CC ChEBI:CHEBI:49552; Evidence={ECO:0000256|ARBA:ARBA00036192};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Early
CC endosome membrane {ECO:0000256|ARBA:ARBA00004520}; Multi-pass membrane
CC protein {ECO:0000256|ARBA:ARBA00004520}. Late endosome membrane
CC {ECO:0000256|ARBA:ARBA00004107}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004107}. Membrane
CC {ECO:0000256|RuleBase:RU367022}; Multi-pass membrane protein
CC {ECO:0000256|RuleBase:RU367022}.
CC -!- SIMILARITY: Belongs to the copper transporter (Ctr) (TC 1.A.56) family.
CC SLC31A subfamily. {ECO:0000256|RuleBase:RU367022}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RLW00325.1}.
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DR EMBL; QUSF01000027; RLW00325.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3L8SCZ5; -.
DR STRING; 44316.ENSEGOP00005011368; -.
DR Proteomes; UP000276834; Unassembled WGS sequence.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016328; C:lateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005375; F:copper ion transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR InterPro; IPR007274; Cop_transporter.
DR PANTHER; PTHR12483:SF22; HIGH AFFINITY COPPER UPTAKE PROTEIN 1; 1.
DR PANTHER; PTHR12483; SOLUTE CARRIER FAMILY 31 COPPER TRANSPORTERS; 1.
DR Pfam; PF04145; Ctr; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Copper {ECO:0000256|RuleBase:RU367022};
KW Copper transport {ECO:0000256|RuleBase:RU367022};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Ion transport {ECO:0000256|RuleBase:RU367022};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU367022};
KW Oxidation {ECO:0000256|ARBA:ARBA00023097};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000276834};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU367022};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU367022}; Transport {ECO:0000256|RuleBase:RU367022}.
FT TRANSMEM 61..78
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367022"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 182 AA; 20240 MW; 5EC7E74FA8C1CAE0 CRC64;
MSHHMNSSML LTSHPPEHQH PSTTASGHGH DMMMMAMTFH FSCKNVPLLF SGLTINSPGE
MAGAFVAVFF LAMFYEGLKI ARECLLRKSQ VSIRYNSMPV PGPNGTILME THKTVGQQML
SLPHLLQTVL HIIQVVVSYF LMLIFMTYNG YLCIAVAAGA GTGYFFFSWK KAVVVDITEH
CH
//
