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Protein

Metal transporter CNNM4

Gene

Cnnm4

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Probable metal transporter. The interaction with the metal ion chaperone COX11 suggests that it may play a role in sensory neuron functions. May play a role in biomineralization and retinal function.2 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Biomineralization, Ion transport, Sensory transduction, Transport, Vision

Names & Taxonomyi

Protein namesi
Recommended name:
Metal transporter CNNM4
Alternative name(s):
Ancient conserved domain-containing protein 4
Cyclin-M4
Gene namesi
Name:Cnnm4
Synonyms:Acdp4
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi1305571. Cnnm4.

Subcellular locationi

  • Cell membrane 1 Publication; Multi-pass membrane protein 1 Publication

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 175175ExtracellularSequence analysisAdd
BLAST
Transmembranei176 – 19621HelicalSequence analysisAdd
BLAST
Topological domaini197 – 23741CytoplasmicSequence analysisAdd
BLAST
Intramembranei238 – 25821HelicalSequence analysisAdd
BLAST
Topological domaini259 – 2613CytoplasmicSequence analysis
Transmembranei262 – 28221HelicalSequence analysisAdd
BLAST
Topological domaini283 – 2908ExtracellularSequence analysis
Transmembranei291 – 31323HelicalSequence analysisAdd
BLAST
Topological domaini314 – 772459CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 772772Metal transporter CNNM4PRO_0000295767Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence analysis
Modified residuei658 – 6581PhosphoserineBy similarity
Modified residuei662 – 6621PhosphoserineCombined sources
Modified residuei767 – 7671PhosphoserineCombined sources

Keywords - PTMi

Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP0C588.
PRIDEiP0C588.

PTM databases

iPTMnetiP0C588.
PhosphoSiteiP0C588.

Expressioni

Tissue specificityi

Present in spinal cord dorsal horn neurons and in developing teeth (at protein level). In the tooth, higher expression is found in the ameloblasts during the transition and maturation phases of amelogenesis; reduced eypression in the odontoblasts.2 Publications

Gene expression databases

ExpressionAtlasiP0C588. baseline and differential.
GenevisibleiP0C588. RN.

Interactioni

Subunit structurei

Interacts with COX11.By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021434.

Structurei

3D structure databases

ProteinModelPortaliP0C588.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini183 – 356174DUF21Add
BLAST
Domaini375 – 43662CBS 1PROSITE-ProRule annotationAdd
BLAST
Domaini443 – 50967CBS 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ACDP family.Curated
Contains 2 CBS domains.PROSITE-ProRule annotation
Contains 1 DUF21 domain.Curated

Keywords - Domaini

CBS domain, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG2118. Eukaryota.
COG1253. LUCA.
GeneTreeiENSGT00390000002383.
HOGENOMiHOG000231947.
HOVERGENiHBG074775.
InParanoidiP0C588.
KOiK16302.
OMAiWLKWTDK.
OrthoDBiEOG72ZCD7.
PhylomeDBiP0C588.
TreeFamiTF101012.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR000644. CBS_dom.
IPR018490. cNMP-bd-like.
IPR002550. DUF21.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00571. CBS. 1 hit.
PF01595. DUF21. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
PROSITEiPS51371. CBS. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0C588-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAPGGGGGRR DGWPARGRLL LAALLLLLWT RAASGQSSPQ QSVILGMRLA
60 70 80 90 100
SCNKSCGMNP DGIIFVSEGS TVNLRLYGHR LGEISSNLIS FTEVDDAETV
110 120 130 140 150
HNSTNCLELT KDLVVQRLVN VSRGNTSGML VVITKFLRRS ENMKLYALCT
160 170 180 190 200
RTRADGPWLK WTDKDSLLFM VEEHGRFLPL WLHILLVLVL LVLSGIFSGL
210 220 230 240 250
NLGLMALDPM ELRIVQNCGT EKERRYARKI EPIRRKGNYL LCSLLLGNVL
260 270 280 290 300
VNTSLTILLD NLIGSGIMAV ASSTIGIVIF GEILPQALCS RHGLAVGANT
310 320 330 340 350
IVLTKIFMLL TFPLSFPISK LLDFVLGQEI RTVYNREKLM EMLKVTEPYN
360 370 380 390 400
DLVKEELNMI QGALELRTKT VEDIMTQLHD CFMIRSDAIL DFNTMSEIME
410 420 430 440 450
SGYTRIPVFE DEQSNIVDIL YVKDLAFVDP DDCTPLKTIT RFYNHPVHFV
460 470 480 490 500
FHDTKLDAML EEFKKGKSHL AIVQKVNNEG EGDPFYEVLG LVTLEDVIEE
510 520 530 540 550
IIKSEILDES DTYTDNRTRK RVSMKNKRDF SAFKDADNEL KVKISPQLLL
560 570 580 590 600
AAHRFLATEV PQFSPSLMSE KILLRLLKYP DVIQELRFDE HNKHCTRHYL
610 620 630 640 650
YTRNKPADCF ILILQGKVEV EAGKENMKFE TGAFSYYGTM ALSLAPPDRS
660 670 680 690 700
PAHPTPLSRS ASLSYPDRNT DMTPSSLAGS NQFGSCILGQ YVSDFSVRAL
710 720 730 740 750
TDLQYIKVTR QQYQNGLLAS RMDNSPQLTL DGCATCTENL SERPELPVVD
760 770
ETTTLLNERN LLLHRASQEG TI
Length:772
Mass (Da):86,692
Last modified:July 24, 2007 - v1
Checksum:i992604232F9F70C9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03067911 Genomic DNA. No translation available.
AABR03068531 Genomic DNA. No translation available.
RefSeqiNP_001257979.1. NM_001271050.1.
UniGeneiRn.857.

Genome annotation databases

EnsembliENSRNOT00000021434; ENSRNOP00000021434; ENSRNOG00000015886.
GeneIDi363216.
KEGGirno:363216.
UCSCiRGD:1305571. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR03067911 Genomic DNA. No translation available.
AABR03068531 Genomic DNA. No translation available.
RefSeqiNP_001257979.1. NM_001271050.1.
UniGeneiRn.857.

3D structure databases

ProteinModelPortaliP0C588.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000021434.

PTM databases

iPTMnetiP0C588.
PhosphoSiteiP0C588.

Proteomic databases

PaxDbiP0C588.
PRIDEiP0C588.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000021434; ENSRNOP00000021434; ENSRNOG00000015886.
GeneIDi363216.
KEGGirno:363216.
UCSCiRGD:1305571. rat.

Organism-specific databases

CTDi26504.
RGDi1305571. Cnnm4.

Phylogenomic databases

eggNOGiKOG2118. Eukaryota.
COG1253. LUCA.
GeneTreeiENSGT00390000002383.
HOGENOMiHOG000231947.
HOVERGENiHBG074775.
InParanoidiP0C588.
KOiK16302.
OMAiWLKWTDK.
OrthoDBiEOG72ZCD7.
PhylomeDBiP0C588.
TreeFamiTF101012.

Miscellaneous databases

PROiP0C588.

Gene expression databases

ExpressionAtlasiP0C588. baseline and differential.
GenevisibleiP0C588. RN.

Family and domain databases

Gene3Di2.60.120.10. 2 hits.
InterProiIPR000644. CBS_dom.
IPR018490. cNMP-bd-like.
IPR002550. DUF21.
IPR014710. RmlC-like_jellyroll.
[Graphical view]
PfamiPF00571. CBS. 1 hit.
PF01595. DUF21. 1 hit.
[Graphical view]
SUPFAMiSSF51206. SSF51206. 2 hits.
PROSITEiPS51371. CBS. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the Brown Norway rat yields insights into mammalian evolution."
    Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J., Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G., Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G., Morgan M.
    , Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G., Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S., Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T., Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D., Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L., Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D., Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M., Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C., Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J., Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H., Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X., Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q., Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P., Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A., Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C., Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J., Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J., Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F., Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A., Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A., Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J., Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E., Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M., Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C., Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L., Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W., Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y., Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V., Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M., Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S., Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B., Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R., Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J., Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D., Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S., Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S., Mockrin S., Collins F.S.
    Nature 428:493-521(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Brown Norway.
  2. "Physical interaction and functional coupling between ACDP4 and the intracellular ion chaperone COX11, an implication of the role of ACDP4 in essential metal ion transport and homeostasis."
    Guo D., Ling J., Wang M.-H., She J.-X., Gu J., Wang C.-Y.
    Mol. Pain 1:15-15(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  3. Cited for: TISSUE SPECIFICITY, FUNCTION.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-662 AND SER-767, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiCNNM4_RAT
AccessioniPrimary (citable) accession number: P0C588
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: July 24, 2007
Last modified: July 6, 2016
This is version 62 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Shares weak sequence similarity with the cyclin family, hence its name. However, it has no cyclin-like function in vivo.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.