CNNM3_HUMAN
ID CNNM3_HUMAN Reviewed; 707 AA.
AC Q8NE01; B3KX67; Q8TBV4; Q96IW4; Q9NRK4; Q9NXW6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Metal transporter CNNM3;
DE AltName: Full=Ancient conserved domain-containing protein 3;
DE AltName: Full=Cyclin-M3;
GN Name=CNNM3; Synonyms=ACDP3;
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] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 313-707 (ISOFORM 2).
RC TISSUE=Adipose tissue, and Amygdala;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 275-707 (ISOFORM 3).
RC TISSUE=Adrenal cortex, Muscle, and Testis;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 294-707 (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=12657465; DOI=10.1016/s0378-1119(02)01210-6;
RA Wang C.-Y., Shi J.-D., Yang P., Kumar P.G., Li Q.-Z., Run Q.-G., Su Y.-C.,
RA Scott H.S., Kao K.-J., She J.-X.;
RT "Molecular cloning and characterization of a novel gene family of four
RT ancient conserved domain proteins (ACDP).";
RL Gene 306:37-44(2003).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661 AND SER-700, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Probable metal transporter. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8NE01; P35609: ACTN2; NbExp=3; IntAct=EBI-741032, EBI-77797;
CC Q8NE01; O95994: AGR2; NbExp=3; IntAct=EBI-741032, EBI-712648;
CC Q8NE01; Q8TD06: AGR3; NbExp=3; IntAct=EBI-741032, EBI-3925742;
CC Q8NE01; Q9ULX6: AKAP8L; NbExp=3; IntAct=EBI-741032, EBI-357530;
CC Q8NE01; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-741032, EBI-739580;
CC Q8NE01; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-741032, EBI-3866279;
CC Q8NE01; Q8NA61: CBY2; NbExp=3; IntAct=EBI-741032, EBI-741724;
CC Q8NE01; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-741032, EBI-11524851;
CC Q8NE01; O95273: CCNDBP1; NbExp=3; IntAct=EBI-741032, EBI-748961;
CC Q8NE01; Q9Y2V7: COG6; NbExp=3; IntAct=EBI-741032, EBI-3866319;
CC Q8NE01; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-741032, EBI-3867333;
CC Q8NE01; O95967: EFEMP2; NbExp=3; IntAct=EBI-741032, EBI-743414;
CC Q8NE01; Q96B26: EXOSC8; NbExp=3; IntAct=EBI-741032, EBI-371922;
CC Q8NE01; Q13643: FHL3; NbExp=9; IntAct=EBI-741032, EBI-741101;
CC Q8NE01; Q5TD97: FHL5; NbExp=3; IntAct=EBI-741032, EBI-750641;
CC Q8NE01; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-741032, EBI-5916454;
CC Q8NE01; P61978-2: HNRNPK; NbExp=3; IntAct=EBI-741032, EBI-7060731;
CC Q8NE01; P49639: HOXA1; NbExp=5; IntAct=EBI-741032, EBI-740785;
CC Q8NE01; O75031: HSF2BP; NbExp=3; IntAct=EBI-741032, EBI-7116203;
CC Q8NE01; Q5VWX1: KHDRBS2; NbExp=3; IntAct=EBI-741032, EBI-742808;
CC Q8NE01; O75525: KHDRBS3; NbExp=3; IntAct=EBI-741032, EBI-722504;
CC Q8NE01; Q5T749: KPRP; NbExp=3; IntAct=EBI-741032, EBI-10981970;
CC Q8NE01; Q15323: KRT31; NbExp=3; IntAct=EBI-741032, EBI-948001;
CC Q8NE01; Q14525: KRT33B; NbExp=3; IntAct=EBI-741032, EBI-1049638;
CC Q8NE01; Q6A162: KRT40; NbExp=3; IntAct=EBI-741032, EBI-10171697;
CC Q8NE01; Q07627: KRTAP1-1; NbExp=3; IntAct=EBI-741032, EBI-11959885;
CC Q8NE01; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-741032, EBI-11749135;
CC Q8NE01; P60370: KRTAP10-5; NbExp=3; IntAct=EBI-741032, EBI-10172150;
CC Q8NE01; P60409: KRTAP10-7; NbExp=5; IntAct=EBI-741032, EBI-10172290;
CC Q8NE01; P60410: KRTAP10-8; NbExp=6; IntAct=EBI-741032, EBI-10171774;
CC Q8NE01; P60411: KRTAP10-9; NbExp=6; IntAct=EBI-741032, EBI-10172052;
CC Q8NE01; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-741032, EBI-10176379;
CC Q8NE01; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-741032, EBI-11953334;
CC Q8NE01; Q9BYP8: KRTAP17-1; NbExp=5; IntAct=EBI-741032, EBI-11988175;
CC Q8NE01; P0C7H8: KRTAP2-3; NbExp=3; IntAct=EBI-741032, EBI-10196781;
CC Q8NE01; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-741032, EBI-9996449;
CC Q8NE01; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-741032, EBI-751260;
CC Q8NE01; P26371: KRTAP5-9; NbExp=6; IntAct=EBI-741032, EBI-3958099;
CC Q8NE01; Q9BYQ4: KRTAP9-2; NbExp=3; IntAct=EBI-741032, EBI-1044640;
CC Q8NE01; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-741032, EBI-1043191;
CC Q8NE01; Q9BYQ0: KRTAP9-8; NbExp=3; IntAct=EBI-741032, EBI-11958364;
CC Q8NE01; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-741032, EBI-741037;
CC Q8NE01; Q99750: MDFI; NbExp=6; IntAct=EBI-741032, EBI-724076;
CC Q8NE01; Q9UJV3-2: MID2; NbExp=3; IntAct=EBI-741032, EBI-10172526;
CC Q8NE01; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-741032, EBI-11522433;
CC Q8NE01; P0DPK4: NOTCH2NLC; NbExp=3; IntAct=EBI-741032, EBI-22310682;
CC Q8NE01; P07237: P4HB; NbExp=3; IntAct=EBI-741032, EBI-395883;
CC Q8NE01; Q8IYS1: PM20D2; NbExp=3; IntAct=EBI-741032, EBI-11339910;
CC Q8NE01; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-741032, EBI-302345;
CC Q8NE01; Q9UL42: PNMA2; NbExp=3; IntAct=EBI-741032, EBI-302355;
CC Q8NE01; Q9UL41: PNMA3; NbExp=3; IntAct=EBI-741032, EBI-11278955;
CC Q8NE01; P38159: RBMX; NbExp=3; IntAct=EBI-741032, EBI-743526;
CC Q8NE01; Q15415: RBMY1J; NbExp=3; IntAct=EBI-741032, EBI-8642021;
CC Q8NE01; Q93062-3: RBPMS; NbExp=3; IntAct=EBI-741032, EBI-740343;
CC Q8NE01; P84103: SRSF3; NbExp=3; IntAct=EBI-741032, EBI-372557;
CC Q8NE01; P22735: TGM1; NbExp=3; IntAct=EBI-741032, EBI-2562368;
CC Q8NE01; Q63HR2: TNS2; NbExp=3; IntAct=EBI-741032, EBI-949753;
CC Q8NE01; P14373: TRIM27; NbExp=3; IntAct=EBI-741032, EBI-719493;
CC Q8NE01; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-741032, EBI-947187;
CC Q8NE01; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-741032, EBI-739895;
CC Q8NE01; Q2TAL6: VWC2; NbExp=5; IntAct=EBI-741032, EBI-11957238;
CC Q8NE01; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-741032, EBI-12040603;
CC Q8NE01; Q9Y3S2: ZNF330; NbExp=3; IntAct=EBI-741032, EBI-373456;
CC Q8NE01; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-741032, EBI-527853;
CC Q8NE01-3; Q13643: FHL3; NbExp=3; IntAct=EBI-10269984, EBI-741101;
CC Q8NE01-3; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-10269984, EBI-10172052;
CC Q8NE01-3; Q9BYR7: KRTAP3-2; NbExp=3; IntAct=EBI-10269984, EBI-751260;
CC Q8NE01-3; Q9BRK4: LZTS2; NbExp=3; IntAct=EBI-10269984, EBI-741037;
CC Q8NE01-3; Q8ND90: PNMA1; NbExp=3; IntAct=EBI-10269984, EBI-302345;
CC Q8NE01-3; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-10269984, EBI-739895;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8NE01-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8NE01-2; Sequence=VSP_027082;
CC Name=3;
CC IsoId=Q8NE01-3; Sequence=VSP_027082, VSP_027083;
CC -!- TISSUE SPECIFICITY: Widely expressed. Expressed at higher level in
CC heart and spleen. {ECO:0000269|PubMed:12657465}.
CC -!- MISCELLANEOUS: Shares weak sequence similarity with the cyclin family,
CC hence its name. However, it has no cyclin-like function in vivo.
CC -!- SIMILARITY: Belongs to the ACDP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAF86377.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH07199.3; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA90891.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK000025; BAA90891.1; ALT_FRAME; mRNA.
DR EMBL; AK126847; BAG54379.1; -; mRNA.
DR EMBL; AC092636; AAY14964.1; -; Genomic_DNA.
DR EMBL; BC007199; AAH07199.3; ALT_INIT; mRNA.
DR EMBL; BC022944; AAH22944.1; -; mRNA.
DR EMBL; BC037272; AAH37272.1; -; mRNA.
DR EMBL; AF216965; AAF86377.1; ALT_INIT; mRNA.
DR CCDS; CCDS2025.1; -. [Q8NE01-1]
DR CCDS; CCDS2026.1; -. [Q8NE01-2]
DR RefSeq; NP_060093.3; NM_017623.4. [Q8NE01-1]
DR RefSeq; NP_951060.1; NM_199078.2. [Q8NE01-2]
DR PDB; 5K22; X-ray; 3.00 A; B=309-452.
DR PDB; 5K23; X-ray; 2.96 A; C=309-452.
DR PDB; 5K25; X-ray; 3.05 A; C=309-452.
DR PDB; 5TSR; X-ray; 3.19 A; B/D=309-452.
DR PDB; 6DFD; X-ray; 1.90 A; A/B=453-707.
DR PDB; 6MN6; X-ray; 3.36 A; A/B=299-658.
DR PDB; 6WUR; X-ray; 2.88 A; B=309-452.
DR PDBsum; 5K22; -.
DR PDBsum; 5K23; -.
DR PDBsum; 5K25; -.
DR PDBsum; 5TSR; -.
DR PDBsum; 6DFD; -.
DR PDBsum; 6MN6; -.
DR PDBsum; 6WUR; -.
DR AlphaFoldDB; Q8NE01; -.
DR SMR; Q8NE01; -.
DR BioGRID; 117712; 214.
DR IntAct; Q8NE01; 84.
DR MINT; Q8NE01; -.
DR STRING; 9606.ENSP00000305449; -.
DR TCDB; 1.A.112.1.3; the cyclin m mg2+ exporter (cnnm) family.
DR GlyGen; Q8NE01; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8NE01; -.
DR PhosphoSitePlus; Q8NE01; -.
DR BioMuta; CNNM3; -.
DR DMDM; 74751242; -.
DR EPD; Q8NE01; -.
DR jPOST; Q8NE01; -.
DR MassIVE; Q8NE01; -.
DR MaxQB; Q8NE01; -.
DR PaxDb; Q8NE01; -.
DR PeptideAtlas; Q8NE01; -.
DR PRIDE; Q8NE01; -.
DR ProteomicsDB; 73108; -. [Q8NE01-1]
DR ProteomicsDB; 73109; -. [Q8NE01-2]
DR ProteomicsDB; 73110; -. [Q8NE01-3]
DR TopDownProteomics; Q8NE01-1; -. [Q8NE01-1]
DR TopDownProteomics; Q8NE01-2; -. [Q8NE01-2]
DR TopDownProteomics; Q8NE01-3; -. [Q8NE01-3]
DR Antibodypedia; 3096; 217 antibodies from 27 providers.
DR DNASU; 26505; -.
DR Ensembl; ENST00000305510.4; ENSP00000305449.3; ENSG00000168763.16. [Q8NE01-1]
DR Ensembl; ENST00000377060.7; ENSP00000366260.3; ENSG00000168763.16. [Q8NE01-2]
DR GeneID; 26505; -.
DR KEGG; hsa:26505; -.
DR MANE-Select; ENST00000305510.4; ENSP00000305449.3; NM_017623.5; NP_060093.3.
DR UCSC; uc002swy.4; human. [Q8NE01-1]
DR CTD; 26505; -.
DR DisGeNET; 26505; -.
DR GeneCards; CNNM3; -.
DR HGNC; HGNC:104; CNNM3.
DR HPA; ENSG00000168763; Low tissue specificity.
DR MIM; 607804; gene.
DR neXtProt; NX_Q8NE01; -.
DR OpenTargets; ENSG00000168763; -.
DR PharmGKB; PA26670; -.
DR VEuPathDB; HostDB:ENSG00000168763; -.
DR eggNOG; KOG2118; Eukaryota.
DR GeneTree; ENSGT00940000161102; -.
DR HOGENOM; CLU_011310_1_1_1; -.
DR InParanoid; Q8NE01; -.
DR OMA; IYGNHLD; -.
DR OrthoDB; 1446644at2759; -.
DR PhylomeDB; Q8NE01; -.
DR TreeFam; TF101012; -.
DR PathwayCommons; Q8NE01; -.
DR SignaLink; Q8NE01; -.
DR BioGRID-ORCS; 26505; 19 hits in 1082 CRISPR screens.
DR ChiTaRS; CNNM3; human.
DR GenomeRNAi; 26505; -.
DR Pharos; Q8NE01; Tbio.
DR PRO; PR:Q8NE01; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8NE01; protein.
DR Bgee; ENSG00000168763; Expressed in gastrocnemius and 165 other tissues.
DR Genevisible; Q8NE01; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0010960; P:magnesium ion homeostasis; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR InterPro; IPR045095; ACDP.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR PANTHER; PTHR12064; PTHR12064; 1.
DR Pfam; PF00571; CBS; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; CBS domain; Cell membrane;
KW Glycoprotein; Ion transport; Membrane; Phosphoprotein; Reference proteome;
KW Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..707
FT /note="Metal transporter CNNM3"
FT /id="PRO_0000295763"
FT TRANSMEM 11..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 221..241
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 130..308
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 318..379
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 386..452
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 678..707
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 700
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 410..457
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_027082"
FT VAR_SEQ 694..707
FT /note="GVPVEGSPGRNPGV -> SLPLLPRGRDSAAYSDSDLFGLSHLVSAVTAFVW
FT P (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027083"
FT CONFLICT 315
FT /note="E -> Q (in Ref. 1; BAA90891)"
FT /evidence="ECO:0000305"
FT CONFLICT 404
FT /note="E -> Q (in Ref. 1; BAA90891)"
FT /evidence="ECO:0000305"
FT CONFLICT 407
FT /note="K -> M (in Ref. 1; BAA90891)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="K -> T (in Ref. 1; BAA90891)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="Q -> H (in Ref. 1; BAA90891)"
FT /evidence="ECO:0000305"
FT CONFLICT 533
FT /note="E -> A (in Ref. 1; BAA90891)"
FT /evidence="ECO:0000305"
FT CONFLICT 543
FT /note="A -> V (in Ref. 1; BAA90891)"
FT /evidence="ECO:0000305"
FT TURN 302..308
FT /evidence="ECO:0007829|PDB:6MN6"
FT TURN 309..311
FT /evidence="ECO:0007829|PDB:6WUR"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 318..320
FT /evidence="ECO:0007829|PDB:5TSR"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:6WUR"
FT HELIX 335..342
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 347..355
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 359..364
FT /evidence="ECO:0007829|PDB:6WUR"
FT HELIX 365..368
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 373..375
FT /evidence="ECO:0007829|PDB:5K23"
FT HELIX 379..385
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 392..394
FT /evidence="ECO:0007829|PDB:6WUR"
FT HELIX 399..407
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 412..420
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:6WUR"
FT STRAND 428..436
FT /evidence="ECO:0007829|PDB:6WUR"
FT HELIX 437..445
FT /evidence="ECO:0007829|PDB:6WUR"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:6MN6"
FT HELIX 494..507
FT /evidence="ECO:0007829|PDB:6DFD"
FT HELIX 509..511
FT /evidence="ECO:0007829|PDB:6DFD"
FT TURN 513..515
FT /evidence="ECO:0007829|PDB:6DFD"
FT HELIX 518..525
FT /evidence="ECO:0007829|PDB:6DFD"
FT HELIX 528..530
FT /evidence="ECO:0007829|PDB:6DFD"
FT STRAND 531..534
FT /evidence="ECO:0007829|PDB:6DFD"
FT STRAND 538..540
FT /evidence="ECO:0007829|PDB:6MN6"
FT HELIX 544..546
FT /evidence="ECO:0007829|PDB:6DFD"
FT STRAND 547..549
FT /evidence="ECO:0007829|PDB:6DFD"
FT STRAND 557..563
FT /evidence="ECO:0007829|PDB:6DFD"
FT STRAND 566..570
FT /evidence="ECO:0007829|PDB:6DFD"
FT TURN 571..574
FT /evidence="ECO:0007829|PDB:6DFD"
FT STRAND 575..579
FT /evidence="ECO:0007829|PDB:6DFD"
FT HELIX 587..590
FT /evidence="ECO:0007829|PDB:6DFD"
FT STRAND 627..634
FT /evidence="ECO:0007829|PDB:6DFD"
FT STRAND 636..642
FT /evidence="ECO:0007829|PDB:6DFD"
FT HELIX 643..654
FT /evidence="ECO:0007829|PDB:6DFD"
SQ SEQUENCE 707 AA; 76119 MW; 22BE4A950A8DA7F5 CRC64;
MAAAVAAAGR LGWLFAALCL GNAAGEAAPG PRVLGFCLEE DGAAGAGWVR GGAARDTPDA
TFLLRLFGPG FANSSWSWVA PEGAGCREEA ASPAGEWRAL LRLRLRAEAV RPHSALLAVR
VEPGGGAAEE AAPPWALGLG AAGLLALAAL ARGLQLSALA LAPAEVQVLR ESGSEAERAA
ARRLEPARRW AGCALGALLL LASLAQAALA VLLYRAAGQR AVPAVLGSAG LVFLVGEVVP
AAVSGRWTLA LAPRALGLSR LAVLLTLPVA LPVGQLLELA ARPGRLRERV LELARGGGDP
YSDLSKGVLR CRTVEDVLTP LEDCFMLDAS TVLDFGVLAS IMQSGHTRIP VYEEERSNIV
DMLYLKDLAF VDPEDCTPLS TITRFYNHPL HFVFNDTKLD AVLEEFKRGK SHLAIVQKVN
NEGEGDPFYE VLGLVTLEDV IEEIIRSEIL DESEDYRDTV VKRKPASLMA PLKRKEEFSL
FKVSDDEYKV TISPQLLLAT QRFLSREVDV FSPLRISEKV LLHLLKHPSV NQEVRFDESN
RLATHHYLYQ RSQPVDYFIL ILQGRVEVEI GKEGLKFENG AFTYYGVSAL TVPSSVHQSP
VSSLQPIRHD LQPDPGDGTH SSAYCPDYTV RALSDLQLIK VTRLQYLNAL LATRAQNLPQ
SPENTDLQVI PGSQTRLLGE KTTTAAGSSH SRPGVPVEGS PGRNPGV
