CNNM4_RAT
ID CNNM4_RAT Reviewed; 772 AA.
AC P0C588;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 24-JUL-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Metal transporter CNNM4;
DE AltName: Full=Ancient conserved domain-containing protein 4;
DE AltName: Full=Cyclin-M4;
GN Name=Cnnm4; Synonyms=Acdp4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15840172; DOI=10.1186/1744-8069-1-15;
RA Guo D., Ling J., Wang M.-H., She J.-X., Gu J., Wang C.-Y.;
RT "Physical interaction and functional coupling between ACDP4 and the
RT intracellular ion chaperone COX11, an implication of the role of ACDP4 in
RT essential metal ion transport and homeostasis.";
RL Mol. Pain 1:15-15(2005).
RN [3]
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662 AND SER-767, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(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. May play a role in biomineralization and retinal function.
CC {ECO:0000269|PubMed:15840172, ECO:0000269|PubMed:19200525}.
CC -!- SUBUNIT: Interacts with COX11. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:15840172};
CC Multi-pass membrane protein {ECO:0000305|PubMed:15840172}.
CC -!- TISSUE SPECIFICITY: Present in spinal cord dorsal horn neurons and in
CC developing teeth (at protein level). In the tooth, higher expression is
CC found in the ameloblasts during the transition and maturation phases of
CC amelogenesis; reduced eypression in the odontoblasts.
CC {ECO:0000269|PubMed:15840172, ECO:0000269|PubMed:19200525}.
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}.
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DR EMBL; AABR03067911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR03068531; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001257979.1; NM_001271050.1.
DR AlphaFoldDB; P0C588; -.
DR SMR; P0C588; -.
DR STRING; 10116.ENSRNOP00000021434; -.
DR GlyGen; P0C588; 1 site.
DR iPTMnet; P0C588; -.
DR PhosphoSitePlus; P0C588; -.
DR PaxDb; P0C588; -.
DR PRIDE; P0C588; -.
DR Ensembl; ENSRNOT00000021434; ENSRNOP00000021434; ENSRNOG00000015886.
DR GeneID; 363216; -.
DR KEGG; rno:363216; -.
DR UCSC; RGD:1305571; rat.
DR CTD; 26504; -.
DR RGD; 1305571; Cnnm4.
DR eggNOG; KOG2118; Eukaryota.
DR GeneTree; ENSGT00940000156317; -.
DR InParanoid; P0C588; -.
DR OMA; KLMFMHA; -.
DR OrthoDB; 1446644at2759; -.
DR PhylomeDB; P0C588; -.
DR TreeFam; TF101012; -.
DR PRO; PR:P0C588; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000015886; Expressed in jejunum and 19 other tissues.
DR ExpressionAtlas; P0C588; baseline and differential.
DR Genevisible; P0C588; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
DR GO; GO:0030425; C:dendrite; IDA:UniProtKB.
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; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0015081; F:sodium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0070166; P:enamel mineralization; ISO:RGD.
DR GO; GO:0010960; P:magnesium ion homeostasis; ISO:RGD.
DR GO; GO:0015693; P:magnesium ion transport; ISO:RGD.
DR GO; GO:0055065; P:metal ion homeostasis; ISO:RGD.
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..772
FT /note="Metal transporter CNNM4"
FT /id="PRO_0000295767"
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..772
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 176..356
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 375..436
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 443..509
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 647..676
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 655..676
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 658
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P4Q7"
FT MOD_RES 662
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 767
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 772 AA; 86692 MW; 992604232F9F70C9 CRC64;
MAPGGGGGRR DGWPARGRLL LAALLLLLWT RAASGQSSPQ QSVILGMRLA SCNKSCGMNP
DGIIFVSEGS TVNLRLYGHR LGEISSNLIS FTEVDDAETV HNSTNCLELT KDLVVQRLVN
VSRGNTSGML VVITKFLRRS ENMKLYALCT RTRADGPWLK WTDKDSLLFM VEEHGRFLPL
WLHILLVLVL LVLSGIFSGL NLGLMALDPM ELRIVQNCGT EKERRYARKI EPIRRKGNYL
LCSLLLGNVL VNTSLTILLD NLIGSGIMAV ASSTIGIVIF GEILPQALCS RHGLAVGANT
IVLTKIFMLL TFPLSFPISK LLDFVLGQEI RTVYNREKLM EMLKVTEPYN DLVKEELNMI
QGALELRTKT VEDIMTQLHD CFMIRSDAIL DFNTMSEIME SGYTRIPVFE DEQSNIVDIL
YVKDLAFVDP DDCTPLKTIT RFYNHPVHFV FHDTKLDAML EEFKKGKSHL AIVQKVNNEG
EGDPFYEVLG LVTLEDVIEE IIKSEILDES DTYTDNRTRK RVSMKNKRDF SAFKDADNEL
KVKISPQLLL AAHRFLATEV PQFSPSLMSE KILLRLLKYP DVIQELRFDE HNKHCTRHYL
YTRNKPADCF ILILQGKVEV EAGKENMKFE TGAFSYYGTM ALSLAPPDRS PAHPTPLSRS
ASLSYPDRNT DMTPSSLAGS NQFGSCILGQ YVSDFSVRAL TDLQYIKVTR QQYQNGLLAS
RMDNSPQLTL DGCATCTENL SERPELPVVD ETTTLLNERN LLLHRASQEG TI
