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O15431

- COPT1_HUMAN

UniProt

O15431 - COPT1_HUMAN

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Protein
High affinity copper uptake protein 1
Gene
SLC31A1, COPT1, CTR1
Organism
Homo sapiens (Human)
Status
Reviewed - 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

  1. copper ion transmembrane transporter activity Source: ProtInc

GO - Biological processi

  1. copper ion transport Source: ProtInc
  2. transmembrane transport Source: Reactome
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: Chromosome 9

Organism-specific databases

HGNCiHGNC:11016. SLC31A1.

Subcellular locationi

Cell membrane; Multi-pass membrane protein
Note: Localizes to the apical membrane in intestinal epithelial cells By similarity.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 6161Extracellular Reviewed prediction
Add
BLAST
Transmembranei62 – 8221Helical; Reviewed prediction
Add
BLAST
Topological domaini83 – 13250Cytoplasmic Reviewed prediction
Add
BLAST
Transmembranei133 – 15321Helical; Reviewed prediction
Add
BLAST
Topological domaini154 – 1563Extracellular Reviewed prediction
Transmembranei157 – 17721Helical; Reviewed prediction
Add
BLAST
Topological domaini178 – 19013Cytoplasmic Reviewed prediction
Add
BLAST

GO - Cellular componenti

  1. integral component of plasma membrane Source: ProtInc
  2. plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA118.

PTM / Processingi

Molecule processing

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

Keywords - PTMi

Glycoprotein

Proteomic databases

MaxQBiO15431.
PaxDbiO15431.
PRIDEiO15431.

PTM databases

PhosphoSiteiO15431.

Expressioni

Gene expression databases

ArrayExpressiO15431.
BgeeiO15431.
CleanExiHS_SLC31A1.
GenevestigatoriO15431.

Organism-specific databases

HPAiHPA013810.

Interactioni

Subunit structurei

Homotrimer.1 Publication

Protein-protein interaction databases

BioGridi107712. 2 interactions.
DIPiDIP-48727N.
MINTiMINT-5003806.
STRINGi9606.ENSP00000363329.

Structurei

Secondary structure

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

3D structure databases

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

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiNOG323808.
HOGENOMiHOG000195393.
HOVERGENiHBG065767.
InParanoidiO15431.
KOiK14686.
OMAiFFFSWKK.
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

MDHSHHMGMS YMDSNSTMQP SHHHPTTSAS HSHGGGDSSM MMMPMTFYFG    50
FKNVELLFSG LVINTAGEMA GAFVAVFLLA MFYEGLKIAR ESLLRKSQVS 100
IRYNSMPVPG PNGTILMETH KTVGQQMLSF PHLLQTVLHI IQVVISYFLM 150
LIFMTYNGYL CIAVAAGAGT GYFLFSWKKA VVVDITEHCH 190
Length:190
Mass (Da):21,091
Last modified:January 1, 1998 - v1
Checksum:i1E08FBAB72A9C014
GO

Natural variant

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

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti168 – 1681A → G in BAD96586. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS6789.1.
RefSeqi NP_001850.1. NM_001859.3.
UniGenei Hs.532315.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2LS2 NMR - A 64-87 [» ]
2LS3 NMR - A 132-157 [» ]
2LS4 NMR - A 156-179 [» ]
ProteinModelPortali O15431.
SMRi O15431. Positions 132-157.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 107712. 2 interactions.
DIPi DIP-48727N.
MINTi MINT-5003806.
STRINGi 9606.ENSP00000363329.

Protein family/group databases

TCDBi 1.A.56.1.2. the copper transporter (ctr) family.

PTM databases

PhosphoSitei O15431.

Proteomic databases

MaxQBi O15431.
PaxDbi O15431.
PRIDEi O15431.

Protocols and materials databases

DNASUi 1317.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374212 ; ENSP00000363329 ; ENSG00000136868 .
GeneIDi 1317.
KEGGi hsa:1317.
UCSCi uc004bgu.3. human.

Organism-specific databases

CTDi 1317.
GeneCardsi GC09P115983.
HGNCi HGNC:11016. SLC31A1.
HPAi HPA013810.
MIMi 603085. gene.
neXtProti NX_O15431.
PharmGKBi PA118.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG323808.
HOGENOMi HOG000195393.
HOVERGENi HBG065767.
InParanoidi O15431.
KOi K14686.
OMAi FFFSWKK.
OrthoDBi EOG7S220Q.
PhylomeDBi O15431.
TreeFami TF315142.

Enzyme and pathway databases

Reactomei REACT_20547. Metal ion SLC transporters.

Miscellaneous databases

GeneWikii SLC31A1.
GenomeRNAii 1317.
NextBioi 5387.
PROi O15431.
SOURCEi Search...

Gene expression databases

ArrayExpressi O15431.
Bgeei O15431.
CleanExi HS_SLC31A1.
Genevestigatori O15431.

Family and domain databases

InterProi IPR007274. Cop_transporter.
[Graphical view ]
PANTHERi PTHR12483. PTHR12483. 1 hit.
Pfami PF04145. Ctr. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: September 3, 2014
This is version 124 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

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