CNNM1_MOUSE
ID CNNM1_MOUSE Reviewed; 951 AA.
AC Q0GA42; Q9JIQ6;
DT 24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-OCT-2010, sequence version 5.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Metal transporter CNNM1;
DE AltName: Full=Ancient conserved domain-containing protein 1;
DE Short=mACDP1;
DE AltName: Full=Cyclin-M1;
DE AltName: Full=Cyclin-like protein 1;
DE Short=CLP-1;
GN Name=Cnnm1; Synonyms=Acdp1;
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 GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-176.
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 257-951, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RC STRAIN=C57BL/6J; 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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 366-951.
RC STRAIN=SWR/J; TISSUE=Testis;
RA Chandran U., Laloraya M., Kumar P.G.;
RT "Cyclin-like protein 1 (CLP-1) in mouse testis.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-821; THR-824 AND SER-850, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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 [6]
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. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14723793};
CC Multi-pass membrane protein {ECO:0000269|PubMed:14723793}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in brain and testis, and,
CC at lower levels, in kidney. In the brain, expressed in hippocampal
CC neurons (at protein level). {ECO:0000269|PubMed:14723793,
CC ECO:0000269|PubMed:22399287}.
CC -!- MISCELLANEOUS: Shares weak sequence similarity with the cyclin family,
CC explaining 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=AAF86371.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAF86371.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AC140375; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BB645731; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AF202994; AAF86371.1; ALT_SEQ; mRNA.
DR EMBL; DQ885890; ABI34706.5; -; mRNA.
DR CCDS; CCDS50442.1; -.
DR RefSeq; NP_113573.2; NM_031396.2.
DR AlphaFoldDB; Q0GA42; -.
DR SMR; Q0GA42; -.
DR STRING; 10090.ENSMUSP00000131830; -.
DR iPTMnet; Q0GA42; -.
DR PhosphoSitePlus; Q0GA42; -.
DR SwissPalm; Q0GA42; -.
DR MaxQB; Q0GA42; -.
DR PaxDb; Q0GA42; -.
DR PRIDE; Q0GA42; -.
DR ProteomicsDB; 283404; -.
DR Antibodypedia; 52446; 56 antibodies from 17 providers.
DR DNASU; 83674; -.
DR Ensembl; ENSMUST00000165311; ENSMUSP00000131830; ENSMUSG00000025189.
DR GeneID; 83674; -.
DR KEGG; mmu:83674; -.
DR UCSC; uc008hoh.2; mouse.
DR CTD; 26507; -.
DR MGI; MGI:1891366; Cnnm1.
DR VEuPathDB; HostDB:ENSMUSG00000025189; -.
DR eggNOG; KOG2118; Eukaryota.
DR GeneTree; ENSGT00940000157525; -.
DR HOGENOM; CLU_011310_1_1_1; -.
DR InParanoid; Q0GA42; -.
DR OrthoDB; 1446644at2759; -.
DR PhylomeDB; Q0GA42; -.
DR TreeFam; TF101012; -.
DR BioGRID-ORCS; 83674; 1 hit in 73 CRISPR screens.
DR PRO; PR:Q0GA42; -.
DR Proteomes; UP000000589; Chromosome 19.
DR RNAct; Q0GA42; protein.
DR Bgee; ENSMUSG00000025189; Expressed in visual cortex and 115 other tissues.
DR ExpressionAtlas; Q0GA42; baseline and differential.
DR Genevisible; Q0GA42; MM.
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; IDA:MGI.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0010960; P:magnesium ion homeostasis; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 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 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 1: Evidence at protein level;
KW CBS domain; Cell membrane; Ion transport; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..951
FT /note="Metal transporter CNNM1"
FT /id="PRO_0000295759"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 222..242
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 319..339
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 218..414
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 433..495
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 502..568
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 114..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 731..754
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 795..830
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 903..951
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 916..939
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 821
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 824
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 850
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 708
FT /note="C -> F (in Ref. 3; AAF86371)"
FT /evidence="ECO:0000305"
FT CONFLICT 726
FT /note="L -> I (in Ref. 4; ABI34706)"
FT /evidence="ECO:0000305"
FT CONFLICT 730
FT /note="P -> L (in Ref. 4; ABI34706)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 951 AA; 103980 MW; F43F9F794C2C9830 CRC64;
MAAAAAAAAA LGVRLRDCCS RGAVLLLFFS LSPRPPAAAA WLLGLRPEDT AGGRVSLEGG
TLRAAEGTSF LLRVYFQPGP PVPAAPVPAP SLAPGENGTG DWAPRLVFIE EPPGAGGAAP
SAVPTRPPGP QRCREQSDWA SDVEVLGPLR PGGVAGSALV QVRVRELRKG EAERGGAGGG
GKLFSLCAWD GRAWHHHGAA GGFLLRVRPR LYGPGGDLLP PAWLRALGAL LLLALSALFS
GLRLSLLSLD PVELRVLRNS GSAAEQEQAR RVQAVRGRGT HLLCTLLLGQ AGANAALAGW
LYASLPPGVG DPGEDSGEAG VHFPWLPALV CTGAVFLGAE ICPYSVCSRH GLAIASHSVC
LTRLLMAAAF PVCYPLGRLL DWALRQEIST FYTREKLLET LRAADPYSDL VKEELNIIQG
ALELRTKVVE EVLTPLGDCF MLRSDAVLDF ATVSEILRSG YTRIPVYEGD QRHNIVDILF
VKDLAFVDPD DCTPLLTVTR FYNRPLHCVF NDTRLDTVLE EFKKGKSHLA IVQRVNNEGE
GDPFYEVMGI VTLEDIIEEI IKSEILDETD LYTDNRKKQR VPHRERRRHD FSLFKLSDSE
IRVKISPQLL LATHRFMATE VEPFKSLYLS EKILLRLLKH PNVIQELKFD ERNKKAPEHY
LYQRNRPVDY FVLLLQGKVE VEVGKEGLRF ENGAFTYYGV PAIMTSACSD NDVRKVGSLA
GSSVFLNRSP SRCSGLNRSE SPNRERSDFG GSNTQLYSSS NNLYTPDYSV HILSDVQFVK
ITRQQYQNAL TACHMDSSPQ SPDMEAFTDG DSTKAPTTRG TPQTPKDDPV LTLLSNRTSL
PCSRSDGLRS PGEVVYLRME EMAFPQEEMP NFEEHRSQQV SLSPVAVPTT AASDPECCNI
HLDPEASPCS SDSEENMGKK LLRTLSGRKR KKSADGERAS EENSNLTPLI T
