CNNM4_MOUSE
ID CNNM4_MOUSE Reviewed; 771 AA.
AC Q69ZF7; Q9JIM7;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 2.
DT 03-AUG-2022, entry version 133.
DE RecName: Full=Metal transporter CNNM4;
DE AltName: Full=Ancient conserved domain-containing protein 4;
DE Short=mACDP4;
DE AltName: Full=Cyclin-M4;
GN Name=Cnnm4; Synonyms=Acdp4, Kiaa1592;
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 TISSUE=Embryonic tail;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 99-771, AND TISSUE SPECIFICITY.
RC 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 [3]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19200527; DOI=10.1016/j.ajhg.2009.01.006;
RA Polok B., Escher P., Ambresin A., Chouery E., Bolay S., Meunier I., Nan F.,
RA Hamel C., Munier F.L., Thilo B., Megarbane A., Schorderet D.F.;
RT "Mutations in CNNM4 cause recessive cone-rod dystrophy with amelogenesis
RT imperfecta.";
RL Am. J. Hum. Genet. 84:259-265(2009).
RN [4]
RP TISSUE SPECIFICITY, AND FUNCTION.
RX PubMed=19200525; DOI=10.1016/j.ajhg.2009.01.009;
RA Parry D.A., Mighell A.J., El-Sayed W., Shore R.C., Jalili I.K., Dollfus H.,
RA Bloch-Zupan A., Carlos R., Carr I.M., Downey L.M., Blain K.M.,
RA Mansfield D.C., Shahrabi M., Heidari M., Aref P., Abbasi M.,
RA Michaelides M., Moore A.T., Kirkham J., Inglehearn C.F.;
RT "Mutations in CNNM4 cause Jalili syndrome, consisting of autosomal-
RT recessive cone-rod dystrophy and amelogenesis imperfecta.";
RL Am. J. Hum. Genet. 84:266-273(2009).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-661 AND SER-766, AND
RP IDENTIFICATION BY 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-661, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Testis;
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. The interaction with the metal
CC ion chaperone COX11 suggests that it may play a role in sensory neuron
CC functions (By similarity). May play a role in biomineralization and
CC retinal function. {ECO:0000250, ECO:0000269|PubMed:19200525,
CC ECO:0000269|PubMed:19200527}.
CC -!- SUBUNIT: Interacts with COX11. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Cornea, retina, teeth (at protein level). In the
CC retina it is predominantly localized to the outer plexiform layer,
CC inner plexiform layer and ganglion cell layer. In the tooth strongest
CC expression is observed in the cell body of the ameloblasts. Expressed
CC at high levels in the gastrointestinal tract and testis.
CC {ECO:0000269|PubMed:14723793, ECO:0000269|PubMed:19200525,
CC ECO:0000269|PubMed:19200527, 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=AAF86375.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD32487.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK173209; BAD32487.1; ALT_INIT; mRNA.
DR EMBL; AF216963; AAF86375.1; ALT_INIT; mRNA.
DR CCDS; CCDS14879.2; -.
DR RefSeq; NP_291048.2; NM_033570.2.
DR AlphaFoldDB; Q69ZF7; -.
DR SMR; Q69ZF7; -.
DR STRING; 10090.ENSMUSP00000121317; -.
DR GlyConnect; 2511; 5 N-Linked glycans (1 site).
DR GlyGen; Q69ZF7; 1 site, 5 N-linked glycans (1 site).
DR iPTMnet; Q69ZF7; -.
DR PhosphoSitePlus; Q69ZF7; -.
DR EPD; Q69ZF7; -.
DR jPOST; Q69ZF7; -.
DR MaxQB; Q69ZF7; -.
DR PaxDb; Q69ZF7; -.
DR PeptideAtlas; Q69ZF7; -.
DR PRIDE; Q69ZF7; -.
DR ProteomicsDB; 283456; -.
DR Antibodypedia; 17482; 156 antibodies from 21 providers.
DR Ensembl; ENSMUST00000153128; ENSMUSP00000121317; ENSMUSG00000037408.
DR GeneID; 94220; -.
DR KEGG; mmu:94220; -.
DR UCSC; uc007aqg.2; mouse.
DR CTD; 26504; -.
DR MGI; MGI:2151060; Cnnm4.
DR VEuPathDB; HostDB:ENSMUSG00000037408; -.
DR eggNOG; KOG2118; Eukaryota.
DR GeneTree; ENSGT00940000156317; -.
DR HOGENOM; CLU_011310_1_1_1; -.
DR InParanoid; Q69ZF7; -.
DR OMA; KLMFMHA; -.
DR OrthoDB; 1446644at2759; -.
DR PhylomeDB; Q69ZF7; -.
DR TreeFam; TF101012; -.
DR BioGRID-ORCS; 94220; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Cnnm4; mouse.
DR PRO; PR:Q69ZF7; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q69ZF7; protein.
DR Bgee; ENSMUSG00000037408; Expressed in spermatocyte and 65 other tissues.
DR Genevisible; Q69ZF7; MM.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0030425; C:dendrite; ISO:MGI.
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:0043025; C:neuronal cell body; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IDA:MGI.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; IDA:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0070166; P:enamel mineralization; IMP:MGI.
DR GO; GO:0010960; P:magnesium ion homeostasis; IMP:MGI.
DR GO; GO:0015693; P:magnesium ion transport; IMP:MGI.
DR GO; GO:0055065; P:metal ion homeostasis; ISO:MGI.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 2.60.120.10; -; 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; IPR018490; cNMP-bd-like.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR014710; RmlC-like_jellyroll.
DR PANTHER; PTHR12064; PTHR12064; 1.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF01595; DUF21; 1.
DR SUPFAM; SSF51206; SSF51206; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 1: Evidence at protein level;
KW Biomineralization; CBS domain; Cell membrane; Glycoprotein; Ion transport;
KW Membrane; Phosphoprotein; Reference proteome; Repeat; Sensory transduction;
KW Transmembrane; Transmembrane helix; Transport; Vision.
FT CHAIN 1..771
FT /note="Metal transporter CNNM4"
FT /id="PRO_0000295766"
FT TOPO_DOM 1..175
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 197..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..261
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 262..282
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 283..290
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 291..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 314..771
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 175..355
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 374..435
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 442..508
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT MOD_RES 657
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4Q7"
FT MOD_RES 661
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 766
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 771 AA; 86626 MW; C4207E51992D1DA2 CRC64;
MAPGGGGGRR DGWPARGRLL LAALLLLWTR AASGQSSPQQ SVILGMRLAS CNKSCGMNPD
GIIFVSEGST VNLRLYGHSL GDISSNLISF TEVDDAEAVH NSTNCLELTK DLVVQRLVNV
SRGNTSGMLV VITKFLRRSE NMKLYALCTR PRADGPWTRW TDKDSLLFMV EEHGRFLPLW
LHILLVMVLL VLSGIFSGLN LGLMALDPME LRIVQNCGTE KERKYARKIE PIRRKGNYLL
CSLLLGNVLV NTSLTILLDN LIGSGIMAVA SSTIGIVIFG EILPQALCSR HGLAVGANTI
VLTKVFMLLT FPLSFPISKL LDFVLGQEIR TVYNREKLME MLKVTEPYND LVKEELNMIQ
GALELRTKTV EDIMTQLHDC FMIRSDAILD FNTMSEIMES GYTRIPVFED EQSNIVDILY
VKDLAFVDPD DCTPLKTITR FYNHPVHFVF HDTKLDAMLE EFKKGKSHLA IVQKVNNEGE
GDPFYEVLGL VTLEDVIEEI IKSEILDESD MYTDNRTRKR VSVKNKRDFS AFKDTDNELK
VKISPQLLLA AHRFLATEVP QFSPSLMSEK ILLRLLKYPD VIQELRFNEH NRYCVRHYLY
TRNKPADCFV LILQGKVEVE AGKENMKFET GAFSYYGTMA LSVAPPDRSP ALPTPLSRSA
SLSYPDRNTD LTSTSLAGSN QFGSCILGQY VSDFSVRALT DLQYIKITRQ QYQNGLMASR
MDNSPQPTFD GCATCSENFM ERPELPPVDE TTTLLNERNS LLHRASEEET I
