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CNNM1_CAEEL
ID   CNNM1_CAEEL             Reviewed;         811 AA.
AC   A3QM97;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Metal transporter cnnm-1 {ECO:0000305};
DE   AltName: Full=CNNM family homolog 1 {ECO:0000312|WormBase:C52D10.12};
DE   Flags: Precursor;
GN   Name=cnnm-1 {ECO:0000303|PubMed:27564576, ECO:0000312|WormBase:C52D10.12};
GN   ORFNames=C52D10.12 {ECO:0000312|WormBase:C52D10.12};
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] {ECO:0000305}
RP   FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP   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-2, cnnm-3, cnnm-4 and cnnm-5 to
CC       regulate Mg(2+) homeostasis. Promotes postembryonic gonad development
CC       by regulating Mg(2+) levels, probably via AMPK signaling.
CC       {ECO:0000269|PubMed:27564576}.
CC   -!- SUBCELLULAR LOCATION: Basolateral cell membrane
CC       {ECO:0000269|PubMed:27564576}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the intestine and in neurons,
CC       but it is also expressed in a variety of tissues including the pharynx,
CC       hypodermis, rectum and in muscles. {ECO:0000269|PubMed:27564576}.
CC   -!- DISRUPTION PHENOTYPE: No visible phenotype. Double knockout with cnnm-3
CC       results in increased levels of intestinal Mg(2+) and reduced levels in
CC       other tissues. This Mg(2+) deficiency in tissues leads to a reduced
CC       lifespan, 100% sterility, and smaller animals that exhibit a
CC       developmental delay with defective gonad development and which
CC       therefore do not produce oocytes or form vulva. In addition, the gonad
CC       development defect in the cnnm-1 and cnnm-3 double knockout is rescued
CC       when the AMPK alpha subunit aak-2 is also knocked out. Quintuple
CC       knockout with cnnm-2, cnnm-3, cnnm-4 and cnnm-5 results in a reduced
CC       lifespan and 100% sterility. {ECO:0000269|PubMed:27564576}.
CC   -!- SIMILARITY: Belongs to the ACDP family. {ECO:0000305}.
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DR   EMBL; BX284604; CAM36329.1; -; Genomic_DNA.
DR   RefSeq; NP_503052.1; NM_070651.3.
DR   AlphaFoldDB; A3QM97; -.
DR   SMR; A3QM97; -.
DR   STRING; 6239.C52D10.12.1; -.
DR   iPTMnet; A3QM97; -.
DR   EPD; A3QM97; -.
DR   PaxDb; A3QM97; -.
DR   PeptideAtlas; A3QM97; -.
DR   EnsemblMetazoa; C52D10.12.1; C52D10.12.1; WBGene00016879.
DR   EnsemblMetazoa; C52D10.12.2; C52D10.12.2; WBGene00016879.
DR   GeneID; 178499; -.
DR   KEGG; cel:CELE_C52D10.12; -.
DR   UCSC; C52D10.12.1; c. elegans.
DR   CTD; 178499; -.
DR   WormBase; C52D10.12; CE28434; WBGene00016879; cnnm-1.
DR   eggNOG; KOG2118; Eukaryota.
DR   GeneTree; ENSGT00940000169533; -.
DR   HOGENOM; CLU_011310_1_2_1; -.
DR   InParanoid; A3QM97; -.
DR   OMA; IYGNHLD; -.
DR   OrthoDB; 1446644at2759; -.
DR   PhylomeDB; A3QM97; -.
DR   PRO; PR:A3QM97; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00016879; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR   GO; GO:0016323; C:basolateral plasma membrane; 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: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; IMP:UniProtKB.
DR   GO; GO:0010960; P:magnesium ion homeostasis; IGI:UniProtKB.
DR   GO; GO:0015693; P:magnesium ion transport; IGI:UniProtKB.
DR   GO; GO:1905941; P:positive regulation of gonad development; IGI:UniProtKB.
DR   GO; GO:0040018; P:positive regulation of multicellular organism growth; IGI:UniProtKB.
DR   GO; GO:0040026; P:positive regulation of vulval development; IGI:UniProtKB.
DR   GO; GO:0032026; P:response to magnesium ion; IGI:UniProtKB.
DR   CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR   Gene3D; 3.10.580.10; -; 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; PTHR12064; 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   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW   Transport.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..811
FT                   /note="Metal transporter cnnm-1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_5002658165"
FT   TOPO_DOM        25..204
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        205..225
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        226..259
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        260..280
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        281..284
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        285..305
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        306..315
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        316..336
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        337..811
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   DOMAIN          197..376
FT                   /note="CNNM transmembrane"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT   DOMAIN          394..456
FT                   /note="CBS 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   DOMAIN          462..530
FT                   /note="CBS 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT   REGION          741..760
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        741..757
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        20
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        49
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        61
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        122
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        435
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        453
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        745
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        752
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   811 AA;  89495 MW;  F9A49FE3031A8296 CRC64;
     MSASCLRLLT LSLFILGQCN VTAAQNGVDD EVTTVTAILD SATTAAADNS TVPTQSASNN
     NTSQSSKIPT IFGMRVELPA DDPFGYDKHG VCSVTPEEEF KVVIYGNHLD KIHQIIWTFT
     NNCSEPAYVI DALNHFKVHF NHKATFHLTL KLLPEMVHAY KMCVKPKVAP GSPPLGEIYP
     LDDISTWLTT ERPPKEYFLP LPLQIACIGF LLCLSALFSG LTLGLMSLTP QELELVIKSG
     AIKEQKCAAK ILPVRKKGNL LLCSLLLGNV IVNSAISILM GELTTGIYAL IGSTMGIVIF
     GEILPQSICV KKGLEVGAHT ISITQLFIFL TFPIAWPVSK LLDCLLGDEY QAYDRKRLME
     LIKMSITDNG QVSNELKIAV GAMEIADKVV KDVMTKIEDV FMLPDTTVLN AKTVMEIVKM
     GYTRIPVYQY GDKNNVTDML FVKDLALLDP DDNFTVKTVC GYHKHPVKFV MNDTPLPNLL
     EAFKKGEGHL AMVKRLINTD DKHDPSYVLV GVVTLEDIVE EILQAEINDE FDIVSDNVNK
     VKIKKEQNRD ATKYFGDHEA PQTMISMQLQ MVALQWLVSN ERGFRQEFLD TNVLERLIRS
     SARRVDVSAL MAMGDDAINV PRLAKVYTKD ELSDKYILIL EGRIQVTIGA SGMMFEAGPW
     HHFGGEIMAK LVDGAATLGR SMSIVGTSEL SARRPDLMFK PDYSAVVKED CTYLEISVSA
     YINAYKASLM QRERPLNDLS DVSHNSSAHN SNLSLVEKPG PITDPSAMLV PENVRKPSVV
     SMDSPKILVG LGQHPVAPVA EEEEMALLDQ P
 
 
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