GenomeNet

Database: UniProt
Entry: CNNM2_CAEEL
LinkDB: CNNM2_CAEEL
Original site: CNNM2_CAEEL 
ID   CNNM2_CAEEL             Reviewed;         760 AA.
AC   Q9GYL2;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2023, sequence version 3.
DT   27-MAR-2024, entry version 125.
DE   RecName: Full=Metal transporter cnnm-2 {ECO:0000305};
DE   AltName: Full=CNNM family homolog 2 {ECO:0000312|WormBase:R04E5.2};
DE   Flags: Precursor;
GN   Name=cnnm-2 {ECO:0000312|WormBase:R04E5.2};
GN   ORFNames=R04E5.2 {ECO:0000312|WormBase:R04E5.2};
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN   [1] {ECO:0000312|Proteomes:UP000001940}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
RX   PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for investigating
RT   biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RX   PubMed=27564576; DOI=10.1371/journal.pgen.1006276;
RA   Ishii T., Funato Y., Hashizume O., Yamazaki D., Hirata Y., Nishiwaki K.,
RA   Kono N., Arai H., Miki H.;
RT   "Mg2+ extrusion from intestinal epithelia by CNNM proteins is essential for
RT   gonadogenesis via AMPK-TORC1 signaling in Caenorhabditis elegans.";
RL   PLoS Genet. 12:E1006276-E1006276(2016).
CC   -!- FUNCTION: Probable metal transporter. Probably acts redundantly with
CC       the other metal transport proteins cnnm-1, cnnm-3, cnnm-4 and cnnm-5 to
CC       regulate Mg(2+) homeostasis. {ECO:0000305|PubMed:27564576}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Double knockout with cnnm-3
CC       results in 22% sterility. Quintuple knockout with cnnm-1, cnnm-3, cnnm-
CC       4 and cnnm-5 results in a reduced lifespan and 100% sterility.
CC       {ECO:0000269|PubMed:27564576}.
CC   -!- SIMILARITY: Belongs to the ACDP family. {ECO:0000305}.
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DR   EMBL; BX284606; CCD65954.2; -; Genomic_DNA.
DR   RefSeq; NP_509493.1; NM_077092.3.
DR   AlphaFoldDB; Q9GYL2; -.
DR   SMR; Q9GYL2; -.
DR   STRING; 6239.R04E5.2.1; -.
DR   GlyCosmos; Q9GYL2; 6 sites, No reported glycans.
DR   EPD; Q9GYL2; -.
DR   PaxDb; 6239-R04E5-2; -.
DR   PeptideAtlas; Q9GYL2; -.
DR   EnsemblMetazoa; R04E5.2.1; R04E5.2.1; WBGene00019869.
DR   UCSC; R04E5.2; c. elegans.
DR   AGR; WB:WBGene00019869; -.
DR   WormBase; R04E5.2; CE53658; WBGene00019869; cnnm-2.
DR   eggNOG; KOG2118; Eukaryota.
DR   HOGENOM; CLU_011310_1_2_1; -.
DR   InParanoid; Q9GYL2; -.
DR   OMA; HICYKER; -.
DR   PhylomeDB; Q9GYL2; -.
DR   PRO; PR:Q9GYL2; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00019869; Expressed in material anatomical entity and 3 other cell types or tissues.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0008340; P:determination of adult lifespan; IGI:UniProtKB.
DR   GO; GO:0010960; P:magnesium ion homeostasis; IEA:InterPro.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR   GO; GO:1905941; P:positive regulation of gonad development; IGI:UniProtKB.
DR   CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 1.
DR   InterPro; IPR045095; ACDP.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR002550; CNNM.
DR   InterPro; IPR044751; Ion_transp-like_CBS.
DR   PANTHER; PTHR12064; METAL TRANSPORTER CNNM; 1.
DR   PANTHER; PTHR12064:SF23; METAL TRANSPORTER CNNM-2; 1.
DR   Pfam; PF01595; CNNM; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   PROSITE; PS51846; CNNM; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Glycoprotein; Ion transport; Membrane; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix; Transport.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..760
FT                   /note="Metal transporter cnnm-2"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_5004327911"
FT   TOPO_DOM        22..153
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        175..208
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        230
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        231..251
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        252..261
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        262..282
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        283..760
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          145..323
FT                   /note="CNNM transmembrane"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT   DOMAIN          344..406
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          442..512
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          708..734
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        302
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        528
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        592
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        667
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   760 AA;  85012 MW;  F9BDD800544D36F8 CRC64;
     MIIKVFLRLL LLCAHIVCID GKLEIRPVVS GVRIESDVDA SGFLGYGDAG ELLVEANTEV
     DLVIFGHGLE NVEMVTFTDS VCVTSEFNVS ESTFYIHKDM KIVFKYAFVA WPQPWRICLK
     SECHGLIQID DDRTWIQAVQ STHETFMPVW AQCAILCLLF SISALCSGLT LGLMALTPQE
     LSILMKSGSQ REKKHAAAIY PIRCHGNRLL CTVIIMNVIV NTGITLLFDD LAEGLIAFVA
     STVGIVVFGE ILPQSICVKY GLAVGANTIF ITKFFMFLLF PITWPLGKIL DKYAGVDIDV
     VNRSRMVEML KMNMENDACD IDLSTLKIAI GAMELTKKSV RDVMTDIDDV FMLSEDQVLN
     AETMTKISDS GYTRIPVFEG NNRNKVKNLL YVSDLALIGK DNNITVKAVA RFNKRRLRIV
     DESMPLTALM DEFKLGDYHL AMVAKATEVK KHHHGKFADG TVDSFILKSM KLVEATMMPQ
     VENPEDHPVT LVGLITLEDI TEELLQAEIT DETDCYVTDD AQKKRRTNTS KKSAAELFCS
     EKKSERLSLH MLEMTEKWLL EKTPLFGNMN PKAFENLIQR NIREVLIVPP KNSTSPGTLN
     LFEAGVMSKR FLLILEGKAT IRFNEKDLIF ECGPWTCFGE AILEKMEMCI SDRKEPSTGF
     FFLPDYNLTV SGPCRFLQIS TSSLLHSLRI TQFVKEIRTP KISITSDDDF GSPTRKASIL
     DSSPNSRKRS STSVMNSLAL PTARLAAKIA SVEELKPLME
//
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