CNNM5_CAEEL
ID CNNM5_CAEEL Reviewed; 722 AA.
AC G5ED05;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 61.
DE RecName: Full=Metal transporter cnnm-5 {ECO:0000305};
DE AltName: Full=CNNM family homolog 5 {ECO:0000312|WormBase:R13G10.4};
DE Flags: Precursor;
GN Name=cnnm-5 {ECO:0000312|WormBase:R13G10.4};
GN ORFNames=R13G10.4 {ECO:0000312|WormBase:R13G10.4};
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, 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-2, cnnm-3 and cnnm-4 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. Quintuple knockout with
CC cnnm-1, cnnm-2, cnnm-3 and cnnm-4 results in a reduced lifespan and
CC 100% sterility. {ECO:0000269|PubMed:27564576}.
CC -!- SIMILARITY: Belongs to the ACDP family. {ECO:0000305}.
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DR EMBL; BX284603; CAA84672.1; -; Genomic_DNA.
DR PIR; T19772; T19772.
DR RefSeq; NP_497773.1; NM_065372.1.
DR AlphaFoldDB; G5ED05; -.
DR SMR; G5ED05; -.
DR STRING; 6239.R13G10.4; -.
DR PaxDb; G5ED05; -.
DR EnsemblMetazoa; R13G10.4.1; R13G10.4.1; WBGene00011260.
DR GeneID; 187872; -.
DR KEGG; cel:CELE_R13G10.4; -.
DR CTD; 187872; -.
DR WormBase; R13G10.4; CE03570; WBGene00011260; cnnm-5.
DR eggNOG; KOG2118; Eukaryota.
DR GeneTree; ENSGT00940000171934; -.
DR HOGENOM; CLU_024276_0_0_1; -.
DR InParanoid; G5ED05; -.
DR OMA; CILMSAY; -.
DR OrthoDB; 926815at2759; -.
DR PhylomeDB; G5ED05; -.
DR PRO; PR:G5ED05; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00011260; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 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 3: Inferred from homology;
KW CBS domain; Cell membrane; Glycoprotein; Ion transport; Membrane;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Transport.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..722
FT /note="Metal transporter cnnm-5"
FT /id="PRO_0000438477"
FT TOPO_DOM 18..139
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 140..160
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 161..196
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..227
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 249..257
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 258..278
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 279..722
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT DOMAIN 132..318
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 333..396
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 413..473
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT REGION 584..607
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 686..722
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..712
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 102
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 114
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 320
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 349
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 371
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 639
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ SEQUENCE 722 AA; 81104 MW; 47F4E722B32386EB CRC64;
MSLFLFAIFQ LALGSPGAPN GPNVPLQLTG VRRGLDHVQK LPSEAFSFKL FGKNLAEDGY
YFTTATRCED SHLSTVSTVR ATVKESYCSY AILSVPEGLP FNVSTSVYHL CHKNATIYTQ
KFLVVHEKKA AAAKYMGDEI VFCFFCILMS AYASGMTLGY MKFSMIDLNT MLKIAEGDAA
KKRVRRIMHF RRRSTQLVVT FSLFSSVFTV LFTTTCEKML HGVSNEDVLK MAVPALICLI
FAEMIPQAVC NSKFGFNLAA SLWFVTVIIF FVTLPIAYPA SLVLGRFLKR DVREVMTPEE
KTCLLRSMAQ NEREKTILEN ATTFTLKKVG QLMVPIEEVF MLSRSQKLNR STVLTLVEKG
YTRIPVYDNK NRSVIVGMLN MKNFNLLMVK TNLIDEPTVK EALHALELLK DRTVKFAVKY
VNIEMNAHLL LNRMKTGDFH FACVVEYSAY DSKVVGIITI EDILEKLIGK IDEINELRVR
SSIDDRGDNA VIGWCREAGS DKKYPLPFSQ QLRILQHLLS ECQVLKSLDI GIMKAKQILS
LDRIRVGKKN DKLELHDLLL VIFEGTVLVT NEVETFERVI DVPSQRSSST VNSQQHRQQT
TDNSRSTPVP VLIIGKPLLN RLMKSLGSPF SEPLGPKDNV SELVVVSEEA SYFKLRLEDL
MNSINGCRKV DRNGHTTTGE SLLQTLNSRA STSTSTTPAC RTPLSVDARS QDETTPFMEK
QE
