COPT1_HUMAN
ID COPT1_HUMAN Reviewed; 190 AA.
AC O15431; A8K8Z6; Q53GR5; Q5T1M4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 176.
DE RecName: Full=High affinity copper uptake protein 1;
DE AltName: Full=Copper transporter 1;
DE Short=hCTR1;
DE AltName: Full=Solute carrier family 31 member 1;
GN Name=SLC31A1; Synonyms=COPT1, CTR1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9207117; DOI=10.1073/pnas.94.14.7481;
RA Zhou B., Gitschier J.;
RT "hCTR1: a human gene for copper uptake identified by complementation in
RT yeast.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:7481-7486(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Testis;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Liver;
RA Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y.,
RA Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP FUNCTION.
RX PubMed=11734551; DOI=10.1074/jbc.m104728200;
RA Lee J., Pena M.M., Nose Y., Thiele D.J.;
RT "Biochemical characterization of the human copper transporter Ctr1.";
RL J. Biol. Chem. 277:4380-4387(2002).
RN [9]
RP GLYCOSYLATION AT ASN-15 AND THR-27.
RX PubMed=17525160; DOI=10.1074/jbc.m701806200;
RA Maryon E.B., Molloy S.A., Kaplan J.H.;
RT "O-linked glycosylation at threonine 27 protects the copper transporter
RT hCTR1 from proteolytic cleavage in mammalian cells.";
RL J. Biol. Chem. 282:20376-20387(2007).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-114, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [11]
RP STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS) IN A NATIVE PHOSPHOLIPID
RP BILAYER, AND SUBUNIT.
RX PubMed=16501047; DOI=10.1073/pnas.0509929103;
RA Aller S.G., Unger V.M.;
RT "Projection structure of the human copper transporter CTR1 at 6-A
RT resolution reveals a compact trimer with a novel channel-like
RT architecture.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3627-3632(2006).
CC -!- FUNCTION: High-affinity, saturable copper transporter involved in
CC dietary copper uptake. {ECO:0000269|PubMed:11734551}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:16501047}.
CC -!- INTERACTION:
CC O15431; O15431: SLC31A1; NbExp=6; IntAct=EBI-15571835, EBI-15571835;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC Note=Localizes to the apical membrane in intestinal epithelial cells.
CC {ECO:0000250}.
CC -!- PTM: O-Glycosylation at Thr-27 protects from proteolytic cleavage in
CC the N-terminal extracellular domain. {ECO:0000269|PubMed:17525160}.
CC -!- SIMILARITY: Belongs to the copper transporter (Ctr) (TC 1.A.56) family.
CC SLC31A subfamily. {ECO:0000305}.
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DR EMBL; U83460; AAB66306.1; -; mRNA.
DR EMBL; AK222866; BAD96586.1; -; mRNA.
DR EMBL; AK292511; BAF85200.1; -; mRNA.
DR EMBL; AL831843; CAD38549.1; -; mRNA.
DR EMBL; AL449305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87357.1; -; Genomic_DNA.
DR EMBL; BC013611; AAH13611.1; -; mRNA.
DR CCDS; CCDS6789.1; -.
DR RefSeq; NP_001850.1; NM_001859.3.
DR PDB; 2LS2; NMR; -; A=64-87.
DR PDB; 2LS3; NMR; -; A=132-157.
DR PDB; 2LS4; NMR; -; A=156-179.
DR PDBsum; 2LS2; -.
DR PDBsum; 2LS3; -.
DR PDBsum; 2LS4; -.
DR AlphaFoldDB; O15431; -.
DR BMRB; O15431; -.
DR SMR; O15431; -.
DR BioGRID; 107712; 181.
DR DIP; DIP-48727N; -.
DR IntAct; O15431; 9.
DR STRING; 9606.ENSP00000363329; -.
DR DrugBank; DB00958; Carboplatin.
DR DrugBank; DB00515; Cisplatin.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB00526; Oxaliplatin.
DR TCDB; 1.A.56.1.2; the copper transporter (ctr) family.
DR GlyGen; O15431; 2 sites.
DR iPTMnet; O15431; -.
DR PhosphoSitePlus; O15431; -.
DR BioMuta; SLC31A1; -.
DR EPD; O15431; -.
DR jPOST; O15431; -.
DR MassIVE; O15431; -.
DR MaxQB; O15431; -.
DR PaxDb; O15431; -.
DR PeptideAtlas; O15431; -.
DR PRIDE; O15431; -.
DR ProteomicsDB; 48657; -.
DR Antibodypedia; 3008; 264 antibodies from 31 providers.
DR CPTC; O15431; 1 antibody.
DR DNASU; 1317; -.
DR Ensembl; ENST00000374212.5; ENSP00000363329.4; ENSG00000136868.11.
DR GeneID; 1317; -.
DR KEGG; hsa:1317; -.
DR MANE-Select; ENST00000374212.5; ENSP00000363329.4; NM_001859.4; NP_001850.1.
DR UCSC; uc004bgu.4; human.
DR CTD; 1317; -.
DR DisGeNET; 1317; -.
DR GeneCards; SLC31A1; -.
DR HGNC; HGNC:11016; SLC31A1.
DR HPA; ENSG00000136868; Tissue enhanced (liver).
DR MIM; 603085; gene.
DR neXtProt; NX_O15431; -.
DR OpenTargets; ENSG00000136868; -.
DR PharmGKB; PA118; -.
DR VEuPathDB; HostDB:ENSG00000136868; -.
DR eggNOG; KOG3386; Eukaryota.
DR GeneTree; ENSGT00940000155147; -.
DR HOGENOM; CLU_079690_2_0_1; -.
DR InParanoid; O15431; -.
DR OMA; MNMIFTW; -.
DR OrthoDB; 1389393at2759; -.
DR PhylomeDB; O15431; -.
DR TreeFam; TF315142; -.
DR BRENDA; 7.2.2.8; 2681.
DR PathwayCommons; O15431; -.
DR Reactome; R-HSA-425410; Metal ion SLC transporters.
DR SignaLink; O15431; -.
DR BioGRID-ORCS; 1317; 87 hits in 1076 CRISPR screens.
DR ChiTaRS; SLC31A1; human.
DR GeneWiki; SLC31A1; -.
DR GenomeRNAi; 1317; -.
DR Pharos; O15431; Tbio.
DR PRO; PR:O15431; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; O15431; protein.
DR Bgee; ENSG00000136868; Expressed in parotid gland and 179 other tissues.
DR ExpressionAtlas; O15431; baseline and differential.
DR Genevisible; O15431; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0014704; C:intercalated disc; IEA:Ensembl.
DR GO; GO:0005770; C:late endosome; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0055037; C:recycling endosome; IEA:Ensembl.
DR GO; GO:0005375; F:copper ion transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IBA:GO_Central.
DR GO; GO:0015677; P:copper ion import; IEA:Ensembl.
DR GO; GO:0006825; P:copper ion transport; TAS:ProtInc.
DR GO; GO:0051649; P:establishment of localization in cell; IEA:Ensembl.
DR InterPro; IPR007274; Cop_transporter.
DR PANTHER; PTHR12483; PTHR12483; 1.
DR Pfam; PF04145; Ctr; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Copper; Copper transport; Glycoprotein;
KW Ion transport; Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..190
FT /note="High affinity copper uptake protein 1"
FT /id="PRO_0000195040"
FT TOPO_DOM 1..61
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 83..132
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 133..153
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 154..156
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 157..177
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 178..190
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..35
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 114
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 15
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:17525160"
FT CARBOHYD 27
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000269|PubMed:17525160"
FT VARIANT 25
FT /note="P -> A (in dbSNP:rs2233915)"
FT /id="VAR_029338"
FT CONFLICT 168
FT /note="A -> G (in Ref. 3; BAD96586)"
FT /evidence="ECO:0000305"
FT HELIX 67..82
FT /evidence="ECO:0007829|PDB:2LS2"
FT TURN 83..85
FT /evidence="ECO:0007829|PDB:2LS2"
FT HELIX 134..155
FT /evidence="ECO:0007829|PDB:2LS3"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:2LS4"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:2LS4"
FT HELIX 174..177
FT /evidence="ECO:0007829|PDB:2LS4"
SQ SEQUENCE 190 AA; 21091 MW; 1E08FBAB72A9C014 CRC64;
MDHSHHMGMS YMDSNSTMQP SHHHPTTSAS HSHGGGDSSM MMMPMTFYFG FKNVELLFSG
LVINTAGEMA GAFVAVFLLA MFYEGLKIAR ESLLRKSQVS IRYNSMPVPG PNGTILMETH
KTVGQQMLSF PHLLQTVLHI IQVVISYFLM LIFMTYNGYL CIAVAAGAGT GYFLFSWKKA
VVVDITEHCH
