位置:首页 > 蛋白库 > CNNM2_CAEEL
CNNM2_CAEEL
ID   CNNM2_CAEEL             Reviewed;         762 AA.
AC   Q9GYL2;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   25-MAY-2022, entry version 118.
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX284606; CCD65954.1; -; Genomic_DNA.
DR   RefSeq; NP_509493.1; NM_077092.3.
DR   AlphaFoldDB; Q9GYL2; -.
DR   SMR; Q9GYL2; -.
DR   STRING; 6239.R04E5.2; -.
DR   EPD; Q9GYL2; -.
DR   PaxDb; Q9GYL2; -.
DR   PeptideAtlas; Q9GYL2; -.
DR   EnsemblMetazoa; R04E5.2.1; R04E5.2.1; WBGene00019869.
DR   UCSC; R04E5.2; c. elegans.
DR   WormBase; R04E5.2; CE28746; WBGene00019869; cnnm-2.
DR   eggNOG; KOG2118; Eukaryota.
DR   HOGENOM; CLU_011310_1_2_1; -.
DR   InParanoid; Q9GYL2; -.
DR   OMA; INLMKMT; -.
DR   OrthoDB; 1446644at2759; -.
DR   PhylomeDB; Q9GYL2; -.
DR   PRO; PR:Q9GYL2; -.
DR   Proteomes; UP000001940; Chromosome X.
DR   Bgee; WBGene00019869; Expressed in material anatomical entity and 3 other tissues.
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; 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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR   GO; GO:0010960; P:magnesium ion homeostasis; IEA:InterPro.
DR   GO; GO:1905941; P:positive regulation of gonad development; IGI:UniProtKB.
DR   Gene3D; 3.10.580.10; -; 1.
DR   InterPro; IPR045095; ACDP.
DR   InterPro; IPR046342; CBS_dom_sf.
DR   InterPro; IPR002550; CNNM.
DR   PANTHER; PTHR12064; PTHR12064; 1.
DR   Pfam; PF01595; DUF21; 1.
DR   SUPFAM; SSF54631; SSF54631; 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..762
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..762
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..408
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          444..514
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          710..736
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        405
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        530
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        594
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        669
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   762 AA;  85182 MW;  B1A2A93275FB6708 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 NNRNKVAVKN LLYVSDLALI GKDNNITVKA VARFNKRRLR
     IVDESMPLTA LMDEFKLGDY HLAMVAKATE VKKHHHGKFA DGTVDSFILK SMKLVEATMM
     PQVENPEDHP VTLVGLITLE DITEELLQAE ITDETDCYVT DDAQKKRRTN TSKKSAAELF
     CSEKKSERLS LHMLEMTEKW LLEKTPLFGN MNPKAFENLI QRNIREVLIV PPKNSTSPGT
     LNLFEAGVMS KRFLLILEGK ATIRFNEKDL IFECGPWTCF GEAILEKMEM CISDRKEPST
     GFFFLPDYNL TVSGPCRFLQ ISTSSLLHSL RITQFVKEIR TPKISITSDD DFGSPTRKAS
     ILDSSPNSRK RSSTSVMNSL ALPTARLAAK IASVEELKPL ME
 
 
维奥蛋白资源库 - 中文蛋白资源 CopyRight © 2010-2024