CNNM3_MOUSE
ID CNNM3_MOUSE Reviewed; 713 AA.
AC Q32NY4; A3KML7; Q3UFE5; Q7TSZ4; Q8C342; Q9JIM6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Metal transporter CNNM3;
DE AltName: Full=Ancient conserved domain-containing protein 3;
DE Short=mACDP3;
DE AltName: Full=Cyclin-M3;
GN Name=Cnnm3; Synonyms=Acdp3;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 246-713 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 300-713 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 300-713 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=14723793; DOI=10.1186/1471-2164-5-7;
RA Wang C.-Y., Yang P., Shi J.-D., Purohit S., Guo D., An H., Gu J.-G.,
RA Ling J., Dong Z., She J.-X.;
RT "Molecular cloning and characterization of the mouse Acdp gene family.";
RL BMC Genomics 5:7-7(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 601-713 (ISOFORM 2), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 624-713 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung, and Sympathetic ganglion;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-706, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, and Pancreas;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP TISSUE SPECIFICITY.
RX PubMed=22399287; DOI=10.1074/jbc.m112.342204;
RA de Baaij J.H., Stuiver M., Meij I.C., Lainez S., Kopplin K., Venselaar H.,
RA Mueller D., Bindels R.J., Hoenderop J.G.;
RT "Membrane topology and intracellular processing of Cyclin M2 (CNNM2).";
RL J. Biol. Chem. 287:13644-13655(2012).
CC -!- FUNCTION: Probable metal transporter. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q32NY4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q32NY4-2; Sequence=VSP_027084;
CC -!- TISSUE SPECIFICITY: Widely expressed with highest levels in brain,
CC kidney, liver, lung and heart. {ECO:0000269|PubMed:22399287}.
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=AAF86376.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI08418.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC084391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC052714; AAH52714.1; -; mRNA.
DR EMBL; BC108417; AAI08418.1; ALT_INIT; mRNA.
DR EMBL; BC132285; AAI32286.1; -; mRNA.
DR EMBL; AF216964; AAF86376.1; ALT_INIT; mRNA.
DR EMBL; AK087028; BAC39785.1; -; mRNA.
DR EMBL; AK148549; BAE28616.1; -; mRNA.
DR CCDS; CCDS14880.1; -. [Q32NY4-1]
DR CCDS; CCDS14881.1; -. [Q32NY4-2]
DR RefSeq; NP_001034640.1; NM_001039551.2. [Q32NY4-2]
DR RefSeq; NP_001318138.1; NM_001331209.1.
DR RefSeq; NP_444416.2; NM_053186.3. [Q32NY4-1]
DR PDB; 5K24; X-ray; 3.10 A; C/D=315-456.
DR PDBsum; 5K24; -.
DR AlphaFoldDB; Q32NY4; -.
DR SMR; Q32NY4; -.
DR STRING; 10090.ENSMUSP00000001166; -.
DR TCDB; 1.A.112.1.2; the cyclin m mg2+ exporter (cnnm) family.
DR GlyGen; Q32NY4; 1 site.
DR iPTMnet; Q32NY4; -.
DR PhosphoSitePlus; Q32NY4; -.
DR SwissPalm; Q32NY4; -.
DR EPD; Q32NY4; -.
DR jPOST; Q32NY4; -.
DR MaxQB; Q32NY4; -.
DR PaxDb; Q32NY4; -.
DR PeptideAtlas; Q32NY4; -.
DR PRIDE; Q32NY4; -.
DR ProteomicsDB; 283405; -. [Q32NY4-1]
DR ProteomicsDB; 283406; -. [Q32NY4-2]
DR Antibodypedia; 3096; 217 antibodies from 27 providers.
DR DNASU; 94218; -.
DR Ensembl; ENSMUST00000001166; ENSMUSP00000001166; ENSMUSG00000001138. [Q32NY4-1]
DR Ensembl; ENSMUST00000097776; ENSMUSP00000095383; ENSMUSG00000001138. [Q32NY4-2]
DR GeneID; 94218; -.
DR KEGG; mmu:94218; -.
DR UCSC; uc007aqi.1; mouse. [Q32NY4-2]
DR UCSC; uc007aqj.1; mouse. [Q32NY4-1]
DR CTD; 26505; -.
DR MGI; MGI:2151055; Cnnm3.
DR VEuPathDB; HostDB:ENSMUSG00000001138; -.
DR eggNOG; KOG2118; Eukaryota.
DR GeneTree; ENSGT00940000161102; -.
DR HOGENOM; CLU_011310_1_1_1; -.
DR InParanoid; Q32NY4; -.
DR OMA; IYGNHLD; -.
DR OrthoDB; 1446644at2759; -.
DR PhylomeDB; Q32NY4; -.
DR TreeFam; TF101012; -.
DR BioGRID-ORCS; 94218; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Cnnm3; mouse.
DR PRO; PR:Q32NY4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q32NY4; protein.
DR Bgee; ENSMUSG00000001138; Expressed in aortic valve and 232 other tissues.
DR Genevisible; Q32NY4; MM.
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: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 Pfam; PF01595; DUF21; 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..713
FT /note="Metal transporter CNNM3"
FT /id="PRO_0000295764"
FT TRANSMEM 7..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 137..157
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 199..219
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 136..314
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 324..385
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 392..458
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 664..713
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 684..703
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 667
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NE01"
FT MOD_RES 706
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT CARBOHYD 73
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 693..713
FT /note="GSTNSRPSIPVEESPGRNPGV -> AFPVHLSLFGTLGNCS (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_027084"
FT CONFLICT 463..464
FT /note="SD -> Y (in Ref. 2; AAH52714)"
FT /evidence="ECO:0000305"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 327..329
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 341..350
FT /evidence="ECO:0007829|PDB:5K24"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:5K24"
FT STRAND 365..370
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 371..375
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 385..392
FT /evidence="ECO:0007829|PDB:5K24"
FT STRAND 398..400
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 405..414
FT /evidence="ECO:0007829|PDB:5K24"
FT STRAND 418..426
FT /evidence="ECO:0007829|PDB:5K24"
FT STRAND 429..431
FT /evidence="ECO:0007829|PDB:5K24"
FT STRAND 434..442
FT /evidence="ECO:0007829|PDB:5K24"
FT HELIX 443..447
FT /evidence="ECO:0007829|PDB:5K24"
FT TURN 448..450
FT /evidence="ECO:0007829|PDB:5K24"
SQ SEQUENCE 713 AA; 76279 MW; BDD9AA76620A96C0 CRC64;
MAAAAAAVVG WLGWVLAAFC LGSTAGEAAP APGAGLLNFC TEEDSAPGAG SLRGRAAPEA
TLCLRLFCSG LANSSWTWVA AEGAGCPEGG RATEPEEAAA PTGEWRALLR LRAEAGHPRS
ALLAVRVEPG GGAAEEAAPP WALGLGAAGL LALAAVARGL QLSALALAPA EVQVLRESGS
EAERAAARRL EPARRWAGCA LGALLLLASL AQAALAVLLY GAAGQRAVPA VLGCAGLVFL
VGEVLPAAVS GRWALALAPR ALGLSRLAVL LTLPVALPVG QLLELAARPG RLRERVLELA
RGGGDPYSDL SKGVLRSRTV EDVLTPLEDC FMLDSGTVLD FSVLASIMQS GHTRIPVYEE
ERSNIVDMLY LKDLAIVEPE DCTPLSTITR FYNHPLHFVF NDTKLDAVLE EFKRGKSHLA
IVQKVNNEGE GDPFYEVLGL VTLEDVIEEI IKSEILDESE DYSDTKVRKK TVALGAPLKR
KEEFSLFKVS DDEYKVKISP QLLLATQRFL SREVDVFSPL RVSEKVLLHL LKHPSVNQEV
TFDESNRLAA HHYLYQRSQP VDYFILILQG RVEVEIGKEG LKFENGAFTY YGVSALTAPS
SAHQSPVSSR QLIRHDVQPE PADGTRSCTY CPDYTVRALS DLQLIKVTRL QYLNALLATR
AQSLPPSPEN AELQAIPGSQ TRLLGDKSRE TAGSTNSRPS IPVEESPGRN PGV
