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Metal transporter CNNM2 (Ancient conserved domain-containing protein 2) (mACDP2) (Cyclin-M2)

 CNNM2_MOUSE             Reviewed;         875 AA.
Q3TWN3; A0PJF1; E9PUH1; Q7TT07; Q8C8V4; Q9JIM8;
24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
27-JUL-2011, sequence version 3.
10-MAY-2017, entry version 96.
RecName: Full=Metal transporter CNNM2;
AltName: Full=Ancient conserved domain-containing protein 2;
Short=mACDP2;
AltName: Full=Cyclin-M2;
Name=Cnnm2; Synonyms=Acdp2;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
STRAIN=C57BL/6J; TISSUE=Retina;
PubMed=16141072; DOI=10.1126/science.1112014;
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M.,
Davis M.J., Wilming L.G., Aidinis V., Allen J.E.,
Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L.,
Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M.,
Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R.,
Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G.,
di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G.,
Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M.,
Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N.,
Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T.,
Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H.,
Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K.,
Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J.,
Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L.,
Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K.,
Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P.,
Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O.,
Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G.,
Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M.,
Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B.,
Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K.,
Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A.,
Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K.,
Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C.,
Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J.,
Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y.,
Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T.,
Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N.,
Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N.,
Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S.,
Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J.,
Hayashizaki Y.;
"The transcriptional landscape of the mammalian genome.";
Science 309:1559-1563(2005).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=C57BL/6J;
PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S.,
She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W.,
Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T.,
Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J.,
Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z.,
Lindblad-Toh K., Eichler E.E., Ponting C.P.;
"Lineage-specific biology revealed by a finished genome assembly of
the mouse.";
PLoS Biol. 7:E1000112-E1000112(2009).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 14-875 (ISOFORM 1).
STRAIN=C57BL/6J, and FVB/N; TISSUE=Mammary gland, and Mammary tumor;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
PROTEIN SEQUENCE OF 27-36, AND IDENTIFICATION BY MASS SPECTROMETRY.
STRAIN=OF1; TISSUE=Hippocampus;
Lubec G., Sunyer B., Chen W.-Q.;
Submitted (JAN-2009) to UniProtKB.
[5]
NUCLEOTIDE SEQUENCE [MRNA] OF 176-875 (ISOFORM 1), AND TISSUE
SPECIFICITY.
TISSUE=Brain;
PubMed=14723793; DOI=10.1186/1471-2164-5-7;
Wang C.-Y., Yang P., Shi J.-D., Purohit S., Guo D., An H., Gu J.-G.,
Ling J., Dong Z., She J.-X.;
"Molecular cloning and characterization of the mouse Acdp gene
family.";
BMC Genomics 5:7-7(2004).
[6]
FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
PubMed=15899945; DOI=10.1152/physiolgenomics.00058.2005;
Goytain A., Quamme G.A.;
"Functional characterization of ACDP2 (ancient conserved domain
protein), a divalent metal transporter.";
Physiol. Genomics 22:382-389(2005).
[7]
GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-112.
PubMed=19349973; DOI=10.1038/nbt.1532;
Wollscheid B., Bausch-Fluck D., Henderson C., O'Brien R., Bibel M.,
Schiess R., Aebersold R., Watts J.D.;
"Mass-spectrometric identification and relative quantification of N-
linked cell surface glycoproteins.";
Nat. Biotechnol. 27:378-386(2009).
[8]
DIMERIZATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MEMBRANE
TOPOLOGY, MUTAGENESIS OF 62-GLY--ALA-65; ASN-112; ASN-327; ASN-527 AND
ASN-591, AND GLYCOSYLATION AT ASN-112.
PubMed=22399287; DOI=10.1074/jbc.M112.342204;
de Baaij J.H., Stuiver M., Meij I.C., Lainez S., Kopplin K.,
Venselaar H., Mueller D., Bindels R.J., Hoenderop J.G.;
"Membrane topology and intracellular processing of Cyclin M2
(CNNM2).";
J. Biol. Chem. 287:13644-13655(2012).
-!- FUNCTION: Divalent metal cation transporter. Mediates transport of
divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) >
Sr(2+) > Ba(2+) > Cu(2+) > Fe(2+). {ECO:0000269|PubMed:15899945}.
-!- SUBUNIT: Isoform 1 and isoform 2 may interact with each other.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:22399287};
Multi-pass membrane protein {ECO:0000269|PubMed:22399287}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1; Synonyms=CNNM2a;
IsoId=Q3TWN3-1; Sequence=Displayed;
Name=2; Synonyms=CNNM2b;
IsoId=Q3TWN3-2; Sequence=VSP_027081;
-!- TISSUE SPECIFICITY: Widely expressed, with highest levels in
kidney, lung, spleen and testis. In the kidney, predominantly
expressed in the distal convoluted tubule and, at lower levels, in
the connecting tubule (at protein level).
{ECO:0000269|PubMed:14723793, ECO:0000269|PubMed:15899945,
ECO:0000269|PubMed:22399287}.
-!- INDUCTION: By low Mg(2+) concentration.
{ECO:0000269|PubMed:15899945}.
-!- PTM: The N-terminus is cleaved within the endoplasmic reticulum.
The signal peptidase complex seems to be involved in the
processing, but the exact cleavage site has not been identified
(PubMed:22399287). {ECO:0000269|PubMed:22399287}.
-!- MISCELLANEOUS: Shares weak sequence similarity with the cyclin
family, hence its name. However, it has no cyclin-like function in
vivo.
-!- SIMILARITY: Belongs to the ACDP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAF86373.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH27387.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
Sequence=AAH52513.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AK044400; BAC31904.1; -; mRNA.
EMBL; AK159616; BAE35233.1; -; mRNA.
EMBL; AC122442; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC161865; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC027387; AAH27387.1; ALT_SEQ; mRNA.
EMBL; BC052513; AAH52513.1; ALT_INIT; mRNA.
EMBL; AF216961; AAF86373.1; ALT_INIT; mRNA.
CCDS; CCDS50459.1; -. [Q3TWN3-1]
CCDS; CCDS50460.1; -. [Q3TWN3-2]
RefSeq; NP_001095941.1; NM_001102471.1. [Q3TWN3-2]
RefSeq; NP_291047.2; NM_033569.3. [Q3TWN3-1]
UniGene; Mm.306903; -.
PDB; 4P1G; X-ray; 2.60 A; A=430-580.
PDB; 4P1O; X-ray; 3.06 A; A/B=430-580.
PDB; 5LXQ; X-ray; 3.33 A; A/H=430-584.
PDB; 5MMZ; X-ray; 2.40 A; A=430-584.
PDBsum; 4P1G; -.
PDBsum; 4P1O; -.
PDBsum; 5LXQ; -.
PDBsum; 5MMZ; -.
ProteinModelPortal; Q3TWN3; -.
SMR; Q3TWN3; -.
STRING; 10090.ENSMUSP00000096972; -.
TCDB; 9.A.40.3.1; the hlyc/corc (hcc) family.
iPTMnet; Q3TWN3; -.
PhosphoSitePlus; Q3TWN3; -.
SwissPalm; Q3TWN3; -.
MaxQB; Q3TWN3; -.
PaxDb; Q3TWN3; -.
PeptideAtlas; Q3TWN3; -.
PRIDE; Q3TWN3; -.
Ensembl; ENSMUST00000077666; ENSMUSP00000076850; ENSMUSG00000064105. [Q3TWN3-2]
Ensembl; ENSMUST00000099373; ENSMUSP00000096972; ENSMUSG00000064105. [Q3TWN3-1]
GeneID; 94219; -.
KEGG; mmu:94219; -.
UCSC; uc008hue.1; mouse. [Q3TWN3-1]
UCSC; uc008huf.1; mouse. [Q3TWN3-2]
CTD; 54805; -.
MGI; MGI:2151054; Cnnm2.
eggNOG; KOG2118; Eukaryota.
eggNOG; COG1253; LUCA.
GeneTree; ENSGT00390000002383; -.
HOGENOM; HOG000231947; -.
HOVERGEN; HBG074775; -.
InParanoid; Q3TWN3; -.
KO; K16302; -.
OMA; VMASRMD; -.
OrthoDB; EOG091G02YS; -.
TreeFam; TF101012; -.
ChiTaRS; Cnnm2; mouse.
PRO; PR:Q3TWN3; -.
Proteomes; UP000000589; Chromosome 19.
Bgee; ENSMUSG00000064105; -.
CleanEx; MM_CNNM2; -.
Genevisible; Q3TWN3; MM.
GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
GO; GO:0005886; C:plasma membrane; IDA:MGI.
GO; GO:0005524; F:ATP binding; IDA:MGI.
GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IDA:MGI.
GO; GO:0010960; P:magnesium ion homeostasis; ISO:MGI.
GO; GO:0015693; P:magnesium ion transport; IDA:MGI.
Gene3D; 2.60.120.10; -; 1.
InterPro; IPR000644; CBS_dom.
InterPro; IPR002550; DUF21.
InterPro; IPR014710; RmlC-like_jellyroll.
Pfam; PF00571; CBS; 1.
Pfam; PF01595; DUF21; 1.
PROSITE; PS51371; CBS; 2.
1: Evidence at protein level;
3D-structure; Alternative splicing; CBS domain; Cell membrane;
Complete proteome; Direct protein sequencing; Glycoprotein;
Ion transport; Membrane; Phosphoprotein; Reference proteome; Repeat;
Transmembrane; Transmembrane helix; Transport.
CHAIN 1 875 Metal transporter CNNM2.
/FTId=PRO_0000295761.
TOPO_DOM 1 250 Extracellular. {ECO:0000255}.
TRANSMEM 251 271 Helical. {ECO:0000255}.
TOPO_DOM 272 313 Cytoplasmic. {ECO:0000255}.
INTRAMEM 314 334 Helical. {ECO:0000255}.
TOPO_DOM 335 338 Cytoplasmic. {ECO:0000255}.
TRANSMEM 339 359 Helical. {ECO:0000255}.
TOPO_DOM 360 368 Extracellular. {ECO:0000255}.
TRANSMEM 369 389 Helical. {ECO:0000255}.
TOPO_DOM 390 875 Cytoplasmic. {ECO:0000255}.
DOMAIN 258 430 DUF21.
DOMAIN 450 511 CBS 1. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
DOMAIN 518 584 CBS 2. {ECO:0000255|PROSITE-
ProRule:PRU00703}.
MOD_RES 761 761 Phosphoserine.
{ECO:0000250|UniProtKB:Q9H8M5}.
CARBOHYD 112 112 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:19349973,
ECO:0000269|PubMed:22399287}.
VAR_SEQ 721 742 Missing (in isoform 2).
{ECO:0000303|PubMed:16141072}.
/FTId=VSP_027081.
MUTAGEN 62 65 GCTA->LLLV: Impairs N-terminal cleavage.
{ECO:0000269|PubMed:22399287}.
MUTAGEN 62 64 GCT->LCL: No effect on N-terminal
cleavage.
MUTAGEN 63 65 CTA->LTV: No effect on N-terminal
cleavage.
MUTAGEN 112 112 N->A: Loss of N-glycosylation; 90%
decrease of plasma membrane expression.
{ECO:0000269|PubMed:22399287}.
MUTAGEN 327 327 N->A: No effect on N-glycosylation.
{ECO:0000269|PubMed:22399287}.
MUTAGEN 527 527 N->A: No effect on N-glycosylation.
{ECO:0000269|PubMed:22399287}.
MUTAGEN 591 591 N->A: No effect on N-glycosylation.
{ECO:0000269|PubMed:22399287}.
CONFLICT 131 131 S -> G (in Ref. 1; BAC31904 and 2;
AAH27387). {ECO:0000305}.
CONFLICT 664 664 Y -> C (in Ref. 1; BAE35233).
{ECO:0000305}.
HELIX 430 440 {ECO:0000244|PDB:5MMZ}.
TURN 441 443 {ECO:0000244|PDB:5MMZ}.
HELIX 446 449 {ECO:0000244|PDB:5MMZ}.
STRAND 450 452 {ECO:0000244|PDB:5MMZ}.
HELIX 453 455 {ECO:0000244|PDB:5MMZ}.
STRAND 464 466 {ECO:0000244|PDB:4P1G}.
HELIX 467 476 {ECO:0000244|PDB:5MMZ}.
STRAND 479 487 {ECO:0000244|PDB:5MMZ}.
STRAND 491 496 {ECO:0000244|PDB:5MMZ}.
HELIX 497 500 {ECO:0000244|PDB:5MMZ}.
HELIX 505 507 {ECO:0000244|PDB:5MMZ}.
HELIX 511 517 {ECO:0000244|PDB:5MMZ}.
STRAND 523 526 {ECO:0000244|PDB:5MMZ}.
HELIX 531 540 {ECO:0000244|PDB:5MMZ}.
STRAND 545 552 {ECO:0000244|PDB:5MMZ}.
STRAND 555 557 {ECO:0000244|PDB:5MMZ}.
STRAND 560 568 {ECO:0000244|PDB:5MMZ}.
HELIX 569 577 {ECO:0000244|PDB:5MMZ}.
SEQUENCE 875 AA; 96704 MW; 8074D56C079E0F6C CRC64;
MIGCGACEPE VKMAGGQAAA ALPTWKMAAR RSLSARGRGV LQAAAGRLLP LLLLSCCWGA
GGCTAAGENE ETVIIGLRLE DTNDVSFMEG GALRVSERTR VKLRVYGQNI NNETWSRIAF
TEHERRRHTP SERGLGGPAP PEPDSGPQRC GIRTSDIIIL PHIILNRRTS GIIEIEIKPL
RKMEKSKSYY LCTSLSTPAL GAGGSGSASG TVGGKGGAGV AGLPPPPWAE TTWIYHDGED
TKMIVGEEKK FLLPFWLQVI FISLLLCLSG MFSGLNLGLM ALDPMELRIV QNCGTEKEKN
YAKRIEPVRR QGNYLLCSLL LGNVLVNTTL TILLDDIAGS GLVAVVVSTI GIVIFGEIVP
QAICSRHGLA VGANTIFLTK FFMMMTFPAS YPVSKLLDCV LGQEIGTVYN REKLLEMLRV
TDPYNDLVKE ELNIIQGALE LRTKTVEDVM TPLRDCFMIT GEAILDFNTM SEIMESGYTR
IPVFEGERSN IVDLLFVKDL AFVDPDDCTP LKTITKFYNH PLHFVFNDTK LDAMLEEFKK
GKSHLAIVQR VNNEGEGDPF YEVLGIVTLE DVIEEIIKSE ILDETDLYTD NRTKKKVAHR
ERKQDFSAFK QTDSEMKVKI SPQLLLAMHR FLATEVEAFS PSQMSEKILL RLLKHPNVIQ
ELKYDEKNKK APECYLYQRN KPVDYFVLIL QGKVEVEAGK EGMKFEASAF SYYGVMALTA
SPVPLSLSRT FVVSRTEVLA AGSPGENKSP PRPCGLNHSD SLSRSDRIDA MTPTLGSSNN
QLSSSFLQVY IPDYSVRALS DLQFVKISRQ QYQNALMASR MDKTPQSSDS ENTKIELTLT
ELHDGLPDET ANLLNEQNCV SHNKANHSLH SEGAI


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