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Protein

High affinity copper uptake protein 1

Gene

SLC31A1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

High-affinity, saturable copper transporter involved in dietary copper uptake.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Copper transport, Ion transport, Transport

Keywords - Ligandi

Copper

Enzyme and pathway databases

ReactomeiREACT_20547. Metal ion SLC transporters.

Protein family/group databases

TCDBi1.A.56.1.2. the copper transporter (ctr) family.

Names & Taxonomyi

Protein namesi
Recommended name:
High affinity copper uptake protein 1
Alternative name(s):
Copper transporter 1
Short name:
hCTR1
Solute carrier family 31 member 1
Gene namesi
Name:SLC31A1
Synonyms:COPT1, CTR1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:11016. SLC31A1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6161ExtracellularSequence AnalysisAdd
BLAST
Transmembranei62 – 8221HelicalSequence AnalysisAdd
BLAST
Topological domaini83 – 13250CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei133 – 15321HelicalSequence AnalysisAdd
BLAST
Topological domaini154 – 1563ExtracellularSequence Analysis
Transmembranei157 – 17721HelicalSequence AnalysisAdd
BLAST
Topological domaini178 – 19013CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  • integral component of plasma membrane Source: ProtInc
  • late endosome Source: Ensembl
  • neuronal cell body Source: Ensembl
  • plasma membrane Source: Reactome
  • recycling endosome Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA118.

Chemistry

DrugBankiDB00188. Bortezomib.
DB00958. Carboplatin.
DB00515. Cisplatin.
DB00526. Oxaliplatin.

Polymorphism and mutation databases

BioMutaiSLC31A1.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 190190High affinity copper uptake protein 1PRO_0000195040Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi15 – 151N-linked (GlcNAc...)1 Publication
Glycosylationi27 – 271O-linked (GalNAc...)1 Publication

Post-translational modificationi

O-Glycosylation at Thr-27 protects from proteolytic cleavage in the N-terminal extracellular domain.1 Publication

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO15431.
PaxDbiO15431.
PRIDEiO15431.

PTM databases

PhosphoSiteiO15431.

Expressioni

Gene expression databases

BgeeiO15431.
CleanExiHS_SLC31A1.
ExpressionAtlasiO15431. baseline and differential.
GenevisibleiO15431. HS.

Organism-specific databases

HPAiHPA013810.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi107712. 9 interactions.
DIPiDIP-48727N.
MINTiMINT-5003806.
STRINGi9606.ENSP00000363329.

Structurei

Secondary structure

1
190
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi67 – 8216Combined sources
Turni83 – 853Combined sources
Helixi134 – 15522Combined sources
Beta strandi160 – 1623Combined sources
Helixi163 – 1686Combined sources
Helixi174 – 1774Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LS2NMR-A64-87[»]
2LS3NMR-A132-157[»]
2LS4NMR-A156-179[»]
ProteinModelPortaliO15431.
SMRiO15431. Positions 132-157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG323808.
GeneTreeiENSGT00530000063415.
HOGENOMiHOG000195393.
HOVERGENiHBG065767.
InParanoidiO15431.
KOiK14686.
OMAiQRNPEAP.
OrthoDBiEOG7S220Q.
PhylomeDBiO15431.
TreeFamiTF315142.

Family and domain databases

InterProiIPR007274. Cop_transporter.
[Graphical view]
PANTHERiPTHR12483. PTHR12483. 1 hit.
PfamiPF04145. Ctr. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O15431-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDHSHHMGMS YMDSNSTMQP SHHHPTTSAS HSHGGGDSSM MMMPMTFYFG
60 70 80 90 100
FKNVELLFSG LVINTAGEMA GAFVAVFLLA MFYEGLKIAR ESLLRKSQVS
110 120 130 140 150
IRYNSMPVPG PNGTILMETH KTVGQQMLSF PHLLQTVLHI IQVVISYFLM
160 170 180 190
LIFMTYNGYL CIAVAAGAGT GYFLFSWKKA VVVDITEHCH
Length:190
Mass (Da):21,091
Last modified:January 1, 1998 - v1
Checksum:i1E08FBAB72A9C014
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 1681A → G in BAD96586 (Ref. 3) Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti25 – 251P → A.
Corresponds to variant rs2233915 [ dbSNP | Ensembl ].
VAR_029338

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U83460 mRNA. Translation: AAB66306.1.
AK222866 mRNA. Translation: BAD96586.1.
AK292511 mRNA. Translation: BAF85200.1.
AL831843 mRNA. Translation: CAD38549.1.
AL449305 Genomic DNA. Translation: CAI10965.1.
CH471090 Genomic DNA. Translation: EAW87357.1.
BC013611 mRNA. Translation: AAH13611.1.
CCDSiCCDS6789.1.
RefSeqiNP_001850.1. NM_001859.3.
UniGeneiHs.532315.

Genome annotation databases

EnsembliENST00000374212; ENSP00000363329; ENSG00000136868.
GeneIDi1317.
KEGGihsa:1317.
UCSCiuc004bgu.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U83460 mRNA. Translation: AAB66306.1.
AK222866 mRNA. Translation: BAD96586.1.
AK292511 mRNA. Translation: BAF85200.1.
AL831843 mRNA. Translation: CAD38549.1.
AL449305 Genomic DNA. Translation: CAI10965.1.
CH471090 Genomic DNA. Translation: EAW87357.1.
BC013611 mRNA. Translation: AAH13611.1.
CCDSiCCDS6789.1.
RefSeqiNP_001850.1. NM_001859.3.
UniGeneiHs.532315.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LS2NMR-A64-87[»]
2LS3NMR-A132-157[»]
2LS4NMR-A156-179[»]
ProteinModelPortaliO15431.
SMRiO15431. Positions 132-157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107712. 9 interactions.
DIPiDIP-48727N.
MINTiMINT-5003806.
STRINGi9606.ENSP00000363329.

Chemistry

DrugBankiDB00188. Bortezomib.
DB00958. Carboplatin.
DB00515. Cisplatin.
DB00526. Oxaliplatin.

Protein family/group databases

TCDBi1.A.56.1.2. the copper transporter (ctr) family.

PTM databases

PhosphoSiteiO15431.

Polymorphism and mutation databases

BioMutaiSLC31A1.

Proteomic databases

MaxQBiO15431.
PaxDbiO15431.
PRIDEiO15431.

Protocols and materials databases

DNASUi1317.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000374212; ENSP00000363329; ENSG00000136868.
GeneIDi1317.
KEGGihsa:1317.
UCSCiuc004bgu.3. human.

Organism-specific databases

CTDi1317.
GeneCardsiGC09P115983.
HGNCiHGNC:11016. SLC31A1.
HPAiHPA013810.
MIMi603085. gene.
neXtProtiNX_O15431.
PharmGKBiPA118.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG323808.
GeneTreeiENSGT00530000063415.
HOGENOMiHOG000195393.
HOVERGENiHBG065767.
InParanoidiO15431.
KOiK14686.
OMAiQRNPEAP.
OrthoDBiEOG7S220Q.
PhylomeDBiO15431.
TreeFamiTF315142.

Enzyme and pathway databases

ReactomeiREACT_20547. Metal ion SLC transporters.

Miscellaneous databases

GeneWikiiSLC31A1.
GenomeRNAii1317.
NextBioi5387.
PROiO15431.
SOURCEiSearch...

Gene expression databases

BgeeiO15431.
CleanExiHS_SLC31A1.
ExpressionAtlasiO15431. baseline and differential.
GenevisibleiO15431. HS.

Family and domain databases

InterProiIPR007274. Cop_transporter.
[Graphical view]
PANTHERiPTHR12483. PTHR12483. 1 hit.
PfamiPF04145. Ctr. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "hCTR1: a human gene for copper uptake identified by complementation in yeast."
    Zhou B., Gitschier J.
    Proc. Natl. Acad. Sci. U.S.A. 94:7481-7486(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Testis.
  3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
    Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Liver.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Skeletal muscle.
  5. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Lung.
  8. "Biochemical characterization of the human copper transporter Ctr1."
    Lee J., Pena M.M., Nose Y., Thiele D.J.
    J. Biol. Chem. 277:4380-4387(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "O-linked glycosylation at threonine 27 protects the copper transporter hCTR1 from proteolytic cleavage in mammalian cells."
    Maryon E.B., Molloy S.A., Kaplan J.H.
    J. Biol. Chem. 282:20376-20387(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION AT ASN-15 AND THR-27.
  10. "Projection structure of the human copper transporter CTR1 at 6-A resolution reveals a compact trimer with a novel channel-like architecture."
    Aller S.G., Unger V.M.
    Proc. Natl. Acad. Sci. U.S.A. 103:3627-3632(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY ELECTRON MICROSCOPY (6 ANGSTROMS) IN A NATIVE PHOSPHOLIPID BILAYER, SUBUNIT.

Entry informationi

Entry nameiCOPT1_HUMAN
AccessioniPrimary (citable) accession number: O15431
Secondary accession number(s): A8K8Z6, Q53GR5, Q5T1M4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 11, 2001
Last sequence update: January 1, 1998
Last modified: July 22, 2015
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.