ID A0A2I0LSX9_COLLI Unreviewed; 218 AA.
AC A0A2I0LSX9;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 28-FEB-2018, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Copper transport protein {ECO:0000256|RuleBase:RU367022};
DE Flags: Fragment;
GN Name=SLC31A1 {ECO:0000313|EMBL:PKK20533.1};
GN ORFNames=A306_00011469 {ECO:0000313|EMBL:PKK20533.1};
OS Columba livia (Rock dove).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Columbiformes; Columbidae; Columba.
OX NCBI_TaxID=8932 {ECO:0000313|EMBL:PKK20533.1, ECO:0000313|Proteomes:UP000053872};
RN [1] {ECO:0000313|EMBL:PKK20533.1, ECO:0000313|Proteomes:UP000053872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC TISSUE=Blood {ECO:0000313|EMBL:PKK20533.1};
RX PubMed=23371554; DOI=10.1126/science.1230422;
RA Shapiro M.D., Kronenberg Z., Li C., Domyan E.T., Pan H., Campbell M.,
RA Tan H., Huff C.D., Hu H., Vickrey A.I., Nielsen S.C., Stringham S.A.,
RA Hu H., Willerslev E., Gilbert M.T., Yandell M., Zhang G., Wang J.;
RT "Genomic diversity and evolution of the head crest in the rock pigeon.";
RL Science 339:1063-1067(2013).
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:PKK20533.1}.
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; AKCR02000107; PKK20533.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2I0LSX9; -.
DR Proteomes; UP000053872; 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:UP000053872};
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 97..114
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU367022"
FT REGION 38..63
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:PKK20533.1"
SQ SEQUENCE 218 AA; 24030 MW; 700AD9647D9DF9CA CRC64;
RKGIGLETTS SEPAELTVCQ LDCRSLLRAF LNSSVAKMSH HGNGSMSPST HPPEHHHPTA
APGSGHDMMM MAMTFHFSYE NVPLLFSGLK INSPGEMAGA FVAVFFLAMF YEGLKIAREC
LLRKSQVSIR YNSMPVPGPN GTILMETHKT VGQQMLSFPH LLQTVLHVIQ VVVSYFLMLI
FMTYNGYLCI AVAAGAGTGY FFFSWKKAVV VDITEHCH
//
