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 27-MAR-2024, entry version 184. 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 227. DR IntAct; Q8NE01; 92. DR MINT; Q8NE01; -. DR STRING; 9606.ENSP00000305449; -. DR TCDB; 1.A.112.1.3; the cyclin m mg2+ exporter (cnnm) family. DR GlyCosmos; Q8NE01; 1 site, No reported glycans. DR GlyGen; Q8NE01; 2 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q8NE01; -. DR PhosphoSitePlus; Q8NE01; -. DR SwissPalm; Q8NE01; -. DR BioMuta; CNNM3; -. DR DMDM; 74751242; -. DR EPD; Q8NE01; -. DR jPOST; Q8NE01; -. DR MassIVE; Q8NE01; -. DR MaxQB; Q8NE01; -. DR PaxDb; 9606-ENSP00000305449; -. DR PeptideAtlas; Q8NE01; -. DR ProteomicsDB; 73108; -. [Q8NE01-1] DR ProteomicsDB; 73109; -. [Q8NE01-2] DR ProteomicsDB; 73110; -. [Q8NE01-3] DR Pumba; Q8NE01; -. DR TopDownProteomics; Q8NE01-1; -. [Q8NE01-1] DR TopDownProteomics; Q8NE01-2; -. [Q8NE01-2] DR TopDownProteomics; Q8NE01-3; -. [Q8NE01-3] DR Antibodypedia; 3096; 231 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 AGR; HGNC:104; -. 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; YGNHLDK; -. DR OrthoDB; 248389at2759; -. DR PhylomeDB; Q8NE01; -. DR TreeFam; TF101012; -. DR PathwayCommons; Q8NE01; -. DR SignaLink; Q8NE01; -. DR BioGRID-ORCS; 26505; 20 hits in 1160 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 167 other cell types or tissues. 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:0010960; P:magnesium ion homeostasis; IEA:InterPro. DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW. DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1. DR Gene3D; 3.10.580.10; CBS-domain; 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; METAL TRANSPORTER CNNM; 1. DR PANTHER; PTHR12064:SF27; METAL TRANSPORTER CNNM3; 1. DR Pfam; PF00571; CBS; 1. DR SUPFAM; SSF54631; CBS-domain pair; 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS51846; CNNM; 1. DR Genevisible; Q8NE01; HS. 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 //