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O15431

- COPT1_HUMAN

UniProt

O15431 - COPT1_HUMAN

Protein

High affinity copper uptake protein 1

Gene

SLC31A1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Jan 1998)
      Previous versions | rss
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    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

    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

    GO - Cellular componenti

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

    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 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

    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

    1
    190
    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.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 6161ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini83 – 13250CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini154 – 1563ExtracellularSequence Analysis
    Topological domaini178 – 19013CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei62 – 8221HelicalSequence AnalysisAdd
    BLAST
    Transmembranei133 – 15321HelicalSequence AnalysisAdd
    BLAST
    Transmembranei157 – 17721HelicalSequence AnalysisAdd
    BLAST

    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

    Experimental Info

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

    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:
    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

    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: October 1, 2014
    This is version 125 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