CNNM2_RAT
ID CNNM2_RAT Reviewed; 875 AA.
AC Q5U2P1;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Metal transporter CNNM2;
DE AltName: Full=Ancient conserved domain-containing protein 2;
DE AltName: Full=Cyclin-M2;
GN Name=Cnnm2; Synonyms=Acdp2;
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 MRNA].
RC TISSUE=Kidney;
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).
CC -!- FUNCTION: Divalent metal cation transporter. Mediates transport of
CC divalent metal cations in an order of Mg(2+) > Co(2+) > Mn(2+) > Sr(2+)
CC > Ba(2+) > Cu(2+) > Fe(2+).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass membrane
CC protein {ECO:0000250}.
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; BC085930; AAH85930.1; -; mRNA.
DR RefSeq; NP_001011942.1; NM_001011942.1.
DR AlphaFoldDB; Q5U2P1; -.
DR SMR; Q5U2P1; -.
DR STRING; 10116.ENSRNOP00000051583; -.
DR GlyGen; Q5U2P1; 1 site.
DR iPTMnet; Q5U2P1; -.
DR PhosphoSitePlus; Q5U2P1; -.
DR jPOST; Q5U2P1; -.
DR PaxDb; Q5U2P1; -.
DR Ensembl; ENSRNOT00000054699; ENSRNOP00000051583; ENSRNOG00000020113.
DR GeneID; 294014; -.
DR KEGG; rno:294014; -.
DR UCSC; RGD:1308162; rat.
DR CTD; 54805; -.
DR RGD; 1308162; Cnnm2.
DR eggNOG; KOG2118; Eukaryota.
DR GeneTree; ENSGT00940000159034; -.
DR HOGENOM; CLU_011310_1_1_1; -.
DR InParanoid; Q5U2P1; -.
DR OMA; CFMITAE; -.
DR OrthoDB; 1446644at2759; -.
DR PhylomeDB; Q5U2P1; -.
DR TreeFam; TF101012; -.
DR PRO; PR:Q5U2P1; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020113; Expressed in kidney and 19 other tissues.
DR Genevisible; Q5U2P1; RN.
DR GO; GO:0016323; C:basolateral plasma membrane; ISO:RGD.
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; ISO:RGD.
DR GO; GO:0005524; F:ATP binding; ISO:RGD.
DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; ISO:RGD.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0010960; P:magnesium ion homeostasis; ISO:RGD.
DR GO; GO:0015693; P:magnesium ion transport; ISO:RGD.
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; 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; SSF54631; SSF54631; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 2: Evidence at transcript level;
KW CBS domain; Cell membrane; Glycoprotein; Ion transport; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..875
FT /note="Metal transporter CNNM2"
FT /id="PRO_0000295762"
FT TOPO_DOM 1..250
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 251..271
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 272..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT INTRAMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 335..338
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 339..359
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 360..368
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 390..875
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 251..431
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 450..511
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 518..584
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 122..148
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 741..763
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 761
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H8M5"
FT CARBOHYD 112
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 875 AA; 96609 MW; 67F24F5315D6BD11 CRC64;
MIGCGACEPE VKMAGGQAAA ALPTWKMAAR RSLSARGRGV LQAAAGRLLP LLLLSCCCSA
GGCTAAGENE ETVIIGLRLE DTNDVSFMEG GALRVSERTR VKLRVYGQNI NNETWSRIAF
TEHERRRHTP GERGLGGPAP 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 QTDSETKVKI SPQLLLAMHR FLATEVEAFS PSQMSEKILL RLLKHPNVIQ
ELKYDEKNKK APECYLYQRN KPVDYFVLIL QGKVEVEAGK EGMKFEASAF SYYGVMALTA
SPVPLSLSRT FVVSRTEVLA AGSPGENKSP PRPCGLNHSD SLSRSDRIDA MTPTLGSSNN
QLSSSFLQVY IPDYSVRALS DLQFVKISRQ QYQNALMASR MDKTPQSSDS ENTKIELTLT
EMHDGLPDET ANLLNEQNCV SHNKANHSLH SEGAI
