CUTC_HUMAN
ID CUTC_HUMAN Reviewed; 273 AA.
AC Q9NTM9; Q5TCZ8; Q9Y321;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Copper homeostasis protein cutC homolog;
GN Name=CUTC; ORFNames=CGI-32;
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 [LARGE SCALE MRNA].
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skeletal muscle;
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 GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [4]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung, and Skin;
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 [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16182249; DOI=10.1016/j.bbrc.2005.09.029;
RA Li J., Ji C., Chen J., Yang Z., Wang Y., Fei X., Zheng M., Gu X., Wen G.,
RA Xie Y., Mao Y.;
RT "Identification and characterization of a novel Cut family cDNA that
RT encodes human copper transporter protein CutC.";
RL Biochem. Biophys. Res. Commun. 337:179-183(2005).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS), COPPER-BINDING, FUNCTION, SUBUNIT,
RP AND MUTAGENESIS OF CYS-31 AND CYS-52.
RX PubMed=19878721; DOI=10.1016/j.jsb.2009.10.012;
RA Li Y., Du J., Zhang P., Ding J.;
RT "Crystal structure of human copper homeostasis protein CutC reveals a
RT potential copper-binding site.";
RL J. Struct. Biol. 169:399-405(2010).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-77.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May play a role in copper homeostasis. Can bind one Cu(1+)
CC per subunit. {ECO:0000269|PubMed:16182249,
CC ECO:0000269|PubMed:19878721}.
CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:19878721}.
CC -!- INTERACTION:
CC Q9NTM9; P54253: ATXN1; NbExp=3; IntAct=EBI-714918, EBI-930964;
CC Q9NTM9; P41182: BCL6; NbExp=3; IntAct=EBI-714918, EBI-765407;
CC Q9NTM9; Q16543: CDC37; NbExp=3; IntAct=EBI-714918, EBI-295634;
CC Q9NTM9; Q8TAP6: CEP76; NbExp=3; IntAct=EBI-714918, EBI-742887;
CC Q9NTM9; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-714918, EBI-2556193;
CC Q9NTM9; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-714918, EBI-16439278;
CC Q9NTM9; Q14696: MESD; NbExp=3; IntAct=EBI-714918, EBI-6165891;
CC Q9NTM9; Q6IA69: NADSYN1; NbExp=4; IntAct=EBI-714918, EBI-748610;
CC Q9NTM9; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-714918, EBI-741158;
CC Q9NTM9; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-714918, EBI-79165;
CC Q9NTM9; O00560: SDCBP; NbExp=6; IntAct=EBI-714918, EBI-727004;
CC Q9NTM9; Q9NZD8: SPG21; NbExp=8; IntAct=EBI-714918, EBI-742688;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:16182249}. Nucleus
CC {ECO:0000269|PubMed:16182249}. Note=The overexpressed protein is
CC detected in the cytoplasm, and depending on the cell line, also in the
CC nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous. {ECO:0000269|PubMed:16182249}.
CC -!- SIMILARITY: Belongs to the CutC family. {ECO:0000305}.
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DR EMBL; AF132966; AAD27741.1; -; mRNA.
DR EMBL; AK314687; BAG37239.1; -; mRNA.
DR EMBL; AL133353; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49854.1; -; Genomic_DNA.
DR EMBL; BC021105; AAH21105.1; -; mRNA.
DR EMBL; BC028948; AAH28948.1; -; mRNA.
DR CCDS; CCDS7483.1; -.
DR RefSeq; NP_057044.2; NM_015960.2.
DR PDB; 3IWP; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-273.
DR PDBsum; 3IWP; -.
DR AlphaFoldDB; Q9NTM9; -.
DR SMR; Q9NTM9; -.
DR BioGRID; 119267; 30.
DR IntAct; Q9NTM9; 20.
DR MINT; Q9NTM9; -.
DR STRING; 9606.ENSP00000359507; -.
DR TCDB; 9.B.158.1.1; the cut copper homeostasis (cut) family.
DR GlyGen; Q9NTM9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9NTM9; -.
DR PhosphoSitePlus; Q9NTM9; -.
DR BioMuta; CUTC; -.
DR DMDM; 54035909; -.
DR EPD; Q9NTM9; -.
DR jPOST; Q9NTM9; -.
DR MassIVE; Q9NTM9; -.
DR MaxQB; Q9NTM9; -.
DR PaxDb; Q9NTM9; -.
DR PeptideAtlas; Q9NTM9; -.
DR PRIDE; Q9NTM9; -.
DR ProteomicsDB; 82625; -.
DR Antibodypedia; 31094; 192 antibodies from 23 providers.
DR DNASU; 51076; -.
DR Ensembl; ENST00000370476.10; ENSP00000359507.5; ENSG00000119929.13.
DR GeneID; 51076; -.
DR KEGG; hsa:51076; -.
DR MANE-Select; ENST00000370476.10; ENSP00000359507.5; NM_015960.3; NP_057044.2.
DR UCSC; uc001kqd.5; human.
DR CTD; 51076; -.
DR DisGeNET; 51076; -.
DR GeneCards; CUTC; -.
DR HGNC; HGNC:24271; CUTC.
DR HPA; ENSG00000119929; Group enriched (skeletal muscle, tongue).
DR MIM; 610101; gene.
DR neXtProt; NX_Q9NTM9; -.
DR OpenTargets; ENSG00000119929; -.
DR PharmGKB; PA134901980; -.
DR VEuPathDB; HostDB:ENSG00000119929; -.
DR eggNOG; KOG4013; Eukaryota.
DR GeneTree; ENSGT00390000008454; -.
DR InParanoid; Q9NTM9; -.
DR OMA; FHRAFDQ; -.
DR OrthoDB; 1619869at2759; -.
DR PhylomeDB; Q9NTM9; -.
DR TreeFam; TF105937; -.
DR PathwayCommons; Q9NTM9; -.
DR Reactome; R-HSA-936837; Ion transport by P-type ATPases.
DR SignaLink; Q9NTM9; -.
DR BioGRID-ORCS; 51076; 9 hits in 1080 CRISPR screens.
DR ChiTaRS; CUTC; human.
DR EvolutionaryTrace; Q9NTM9; -.
DR GeneWiki; CUTC_(gene); -.
DR GenomeRNAi; 51076; -.
DR Pharos; Q9NTM9; Tbio.
DR PRO; PR:Q9NTM9; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; Q9NTM9; protein.
DR Bgee; ENSG00000119929; Expressed in skeletal muscle tissue of rectus abdominis and 188 other tissues.
DR ExpressionAtlas; Q9NTM9; baseline and differential.
DR Genevisible; Q9NTM9; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IDA:UniProtKB.
DR GO; GO:0055070; P:copper ion homeostasis; NAS:UniProtKB.
DR GO; GO:0006825; P:copper ion transport; NAS:UniProtKB.
DR GO; GO:0051262; P:protein tetramerization; IPI:UniProtKB.
DR Gene3D; 3.20.20.380; -; 1.
DR HAMAP; MF_00795; CutC; 1.
DR InterPro; IPR005627; Cu_homeostasis_CutC.
DR InterPro; IPR036822; CutC_dom_sf.
DR PANTHER; PTHR12598; PTHR12598; 1.
DR Pfam; PF03932; CutC; 1.
DR SUPFAM; SSF110395; SSF110395; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Cytoplasm; Metal-binding; Nucleus;
KW Reference proteome.
FT CHAIN 1..273
FT /note="Copper homeostasis protein cutC homolog"
FT /id="PRO_0000215088"
FT VARIANT 77
FT /note="P -> L (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036363"
FT MUTAGEN 31
FT /note="C->A: Reduces copper binding. Reduces copper binding
FT by 75%; when associated with A-52."
FT /evidence="ECO:0000269|PubMed:19878721"
FT MUTAGEN 52
FT /note="C->A: Reduces copper binding. Reduces copper binding
FT by 75%; when associated with A-31."
FT /evidence="ECO:0000269|PubMed:19878721"
FT CONFLICT 108
FT /note="L -> P (in Ref. 1; AAD27741)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="K -> N (in Ref. 1; AAD27741)"
FT /evidence="ECO:0000305"
FT STRAND 26..34
FT /evidence="ECO:0007829|PDB:3IWP"
FT HELIX 35..44
FT /evidence="ECO:0007829|PDB:3IWP"
FT STRAND 47..51
FT /evidence="ECO:0007829|PDB:3IWP"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:3IWP"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:3IWP"
FT STRAND 78..81
FT /evidence="ECO:0007829|PDB:3IWP"
FT STRAND 84..87
FT /evidence="ECO:0007829|PDB:3IWP"
FT HELIX 93..108
FT /evidence="ECO:0007829|PDB:3IWP"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:3IWP"
FT HELIX 127..137
FT /evidence="ECO:0007829|PDB:3IWP"
FT STRAND 142..144
FT /evidence="ECO:0007829|PDB:3IWP"
FT HELIX 146..150
FT /evidence="ECO:0007829|PDB:3IWP"
FT HELIX 154..164
FT /evidence="ECO:0007829|PDB:3IWP"
FT STRAND 167..171
FT /evidence="ECO:0007829|PDB:3IWP"
FT STRAND 175..177
FT /evidence="ECO:0007829|PDB:3IWP"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:3IWP"
FT HELIX 182..192
FT /evidence="ECO:0007829|PDB:3IWP"
FT STRAND 195..200
FT /evidence="ECO:0007829|PDB:3IWP"
FT TURN 206..208
FT /evidence="ECO:0007829|PDB:3IWP"
FT HELIX 209..216
FT /evidence="ECO:0007829|PDB:3IWP"
FT STRAND 219..223
FT /evidence="ECO:0007829|PDB:3IWP"
FT STRAND 226..229
FT /evidence="ECO:0007829|PDB:3IWP"
FT TURN 244..246
FT /evidence="ECO:0007829|PDB:3IWP"
FT STRAND 253..256
FT /evidence="ECO:0007829|PDB:3IWP"
FT HELIX 258..271
FT /evidence="ECO:0007829|PDB:3IWP"
SQ SEQUENCE 273 AA; 29341 MW; 63C007AAB05C5492 CRC64;
MKRQGASSER KRARIPSGKA GAANGFLMEV CVDSVESAVN AERGGADRIE LCSGLSEGGT
TPSMGVLQVV KQSVQIPVFV MIRPRGGDFL YSDREIEVMK ADIRLAKLYG ADGLVFGALT
EDGHIDKELC MSLMAICRPL PVTFHRAFDM VHDPMAALET LLTLGFERVL TSGCDSSALE
GLPLIKRLIE QAKGRIVVMP GGGITDRNLQ RILEGSGATE FHCSARSTRD SGMKFRNSSV
AMGASLSCSE YSLKVTDVTK VRTLNAIAKN ILV
