COPT1_MOUSE
ID COPT1_MOUSE Reviewed; 196 AA.
AC Q8K211; Q3UAJ9; Q8BXJ1;
DT 23-NOV-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=High affinity copper uptake protein 1;
DE AltName: Full=Copper transporter 1;
DE Short=CTR1;
DE AltName: Full=Solute carrier family 31 member 1;
GN Name=Slc31a1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow, and Medulla oblongata;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Olfactory epithelium;
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 [4]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=20699218; DOI=10.1074/jbc.m110.143826;
RA Nose Y., Wood L.K., Kim B.E., Prohaska J.R., Fry R.S., Spears J.W.,
RA Thiele D.J.;
RT "Ctr1 is an apical copper transporter in mammalian intestinal epithelial
RT cells in vivo that is controlled at the level of protein stability.";
RL J. Biol. Chem. 285:32385-32392(2010).
CC -!- FUNCTION: High-affinity, saturable copper transporter involved in
CC dietary copper uptake. {ECO:0000269|PubMed:20699218}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20699218};
CC Multi-pass membrane protein {ECO:0000269|PubMed:20699218}.
CC Note=Localizes to the apical membrane in intestinal epithelial cells.
CC -!- SIMILARITY: Belongs to the copper transporter (Ctr) (TC 1.A.56) family.
CC SLC31A subfamily. {ECO:0000305}.
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DR EMBL; AK046835; BAC32891.1; -; mRNA.
DR EMBL; AK151337; BAE30315.1; -; mRNA.
DR EMBL; AL732548; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC034674; AAH34674.1; -; mRNA.
DR EMBL; BC058227; AAH58227.1; -; mRNA.
DR CCDS; CCDS18237.1; -.
DR RefSeq; NP_780299.2; NM_175090.4.
DR RefSeq; XP_006537774.1; XM_006537711.2.
DR AlphaFoldDB; Q8K211; -.
DR BMRB; Q8K211; -.
DR SMR; Q8K211; -.
DR BioGRID; 203308; 2.
DR STRING; 10090.ENSMUSP00000081574; -.
DR GlyGen; Q8K211; 2 sites.
DR PhosphoSitePlus; Q8K211; -.
DR jPOST; Q8K211; -.
DR MaxQB; Q8K211; -.
DR PaxDb; Q8K211; -.
DR PRIDE; Q8K211; -.
DR ProteomicsDB; 283352; -.
DR Antibodypedia; 3008; 264 antibodies from 31 providers.
DR DNASU; 20529; -.
DR Ensembl; ENSMUST00000084526; ENSMUSP00000081574; ENSMUSG00000066150.
DR GeneID; 20529; -.
DR KEGG; mmu:20529; -.
DR UCSC; uc008ten.2; mouse.
DR CTD; 1317; -.
DR MGI; MGI:1333843; Slc31a1.
DR VEuPathDB; HostDB:ENSMUSG00000066150; -.
DR eggNOG; KOG3386; Eukaryota.
DR GeneTree; ENSGT00940000155147; -.
DR HOGENOM; CLU_079690_2_0_1; -.
DR InParanoid; Q8K211; -.
DR OMA; MNMIFTW; -.
DR OrthoDB; 1389393at2759; -.
DR PhylomeDB; Q8K211; -.
DR TreeFam; TF315142; -.
DR Reactome; R-MMU-425410; Metal ion SLC transporters.
DR BioGRID-ORCS; 20529; 11 hits in 72 CRISPR screens.
DR ChiTaRS; Slc31a1; mouse.
DR PRO; PR:Q8K211; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q8K211; protein.
DR Bgee; ENSMUSG00000066150; Expressed in ileal epithelium and 270 other tissues.
DR ExpressionAtlas; Q8K211; baseline and differential.
DR Genevisible; Q8K211; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0014704; C:intercalated disc; IDA:MGI.
DR GO; GO:0005770; C:late endosome; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0055037; C:recycling endosome; IDA:MGI.
DR GO; GO:0005375; F:copper ion transmembrane transporter activity; IMP:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0006878; P:cellular copper ion homeostasis; IGI:MGI.
DR GO; GO:0072719; P:cellular response to cisplatin; ISO:MGI.
DR GO; GO:0015677; P:copper ion import; IMP:MGI.
DR GO; GO:0098705; P:copper ion import across plasma membrane; ISO:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IMP:MGI.
DR GO; GO:0055085; P:transmembrane transport; ISO:MGI.
DR InterPro; IPR007274; Cop_transporter.
DR PANTHER; PTHR12483; PTHR12483; 1.
DR Pfam; PF04145; Ctr; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Copper; Copper transport; Glycoprotein; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..196
FT /note="High affinity copper uptake protein 1"
FT /id="PRO_0000195041"
FT TOPO_DOM 1..74
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 75..95
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 96..138
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 139..159
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 160..162
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 184..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 19..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 27..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O15431"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 34
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000250"
FT CONFLICT 18
FT /note="N -> Y (in Ref. 1; BAC32891)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 196 AA; 21961 MW; A4EDDD2A9E51AF10 CRC64;
MNHMGMNHME MHHHMGMNHT DDNITMPPHH HPTTSASHSH GGGDSMMMMP MTFYFDFKNV
NLLFSGLVIN TPGEMAGAFV AVFLLAMFYE GLKIAREGLL RKSQVSIRYN SMPVPGPNGT
ILMETHKTVG QQMLSFPHLL QTVLHIIQVV ISYFLMLIFM TYNGYLCIAV AAGAGTGYFL
FSWKKAVVVD ITEHCH
