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CHAT1_CAEEL
ID   CHAT1_CAEEL             Reviewed;         348 AA.
AC   H2L0H3; H2L0H4; Q2L6W0; U4PMW1;
DT   20-JAN-2016, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 1.
DT   03-AUG-2022, entry version 65.
DE   RecName: Full=CDC50 family protein chat-1 {ECO:0000303|PubMed:21170358};
GN   Name=chat-1 {ECO:0000312|WormBase:R08C7.2a};
GN   ORFNames=R08C7.2 {ECO:0000312|WormBase:R08C7.2a};
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, DEVELOPMENTAL STAGE, AND DISRUPTION
RP   PHENOTYPE.
RX   PubMed=21170358; DOI=10.1371/journal.pgen.1001235;
RA   Chen B., Jiang Y., Zeng S., Yan J., Li X., Zhang Y., Zou W., Wang X.;
RT   "Endocytic sorting and recycling require membrane phosphatidylserine
RT   asymmetry maintained by TAT-1/CHAT-1.";
RL   PLoS Genet. 6:E1001235-E1001235(2010).
CC   -!- FUNCTION: Probable chaperone protein for the phospholipid-transporting
CC       ATPase tat-1. Regulates cell membrane structure and function. Plays a
CC       role in maintaining the membrane phosphatidylserine asymmetry and the
CC       formation of the tubular membrane structure. Involved in membrane
CC       trafficking and is specifically involved in the recycling and
CC       degradation of endocytic cargo and this is likely with the
CC       phospholipid-transporting ATPase tat-1. {ECO:0000269|PubMed:21170358}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:21170358};
CC       Multi-pass membrane protein {ECO:0000255}. Early endosome membrane
CC       {ECO:0000269|PubMed:21170358}; Multi-pass membrane protein. Recycling
CC       endosome membrane {ECO:0000269|PubMed:21170358}; Multi-pass membrane
CC       protein. Endoplasmic reticulum {ECO:0000269|PubMed:21170358}.
CC       Note=Colocalizes with phospholipid-transporting ATPase tat-1 at apical
CC       and basolateral cell membranes, on early endosomes and on recycling
CC       endosomes. Also localizes to intracellular tubular and vesicular
CC       structures. {ECO:0000269|PubMed:21170358}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=a {ECO:0000312|WormBase:R08C7.2a};
CC         IsoId=H2L0H3-1; Sequence=Displayed;
CC       Name=b {ECO:0000312|WormBase:R08C7.2b};
CC         IsoId=H2L0H3-2; Sequence=VSP_058022, VSP_058023;
CC       Name=c {ECO:0000312|WormBase:R08C7.2c};
CC         IsoId=H2L0H3-3; Sequence=VSP_058021;
CC       Name=d {ECO:0000312|WormBase:R08C7.2d};
CC         IsoId=H2L0H3-4; Sequence=VSP_058020;
CC   -!- DEVELOPMENTAL STAGE: Expressed from early embryogenesis to adulthood in
CC       various cell types. {ECO:0000269|PubMed:21170358}.
CC   -!- DISRUPTION PHENOTYPE: RNAi-mediated knockdown results in the appearance
CC       of abnormal vacuoles in the intestines and defective recycling of
CC       endocytic cargo with the accumulation of cargo within abnormal early
CC       endosomes. {ECO:0000269|PubMed:21170358}.
CC   -!- SIMILARITY: Belongs to the CDC50/LEM3 family. {ECO:0000305}.
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DR   EMBL; BX284604; CCD73083.1; -; Genomic_DNA.
DR   EMBL; BX284604; CCD73084.1; -; Genomic_DNA.
DR   EMBL; BX284604; CCD73085.1; -; Genomic_DNA.
DR   EMBL; BX284604; CDH93430.1; -; Genomic_DNA.
DR   RefSeq; NP_001023332.1; NM_001028161.3. [H2L0H3-1]
DR   RefSeq; NP_001040979.1; NM_001047514.2. [H2L0H3-3]
DR   RefSeq; NP_001294623.1; NM_001307694.1.
DR   AlphaFoldDB; H2L0H3; -.
DR   SMR; H2L0H3; -.
DR   STRING; 6239.R08C7.2a; -.
DR   TCDB; 8.A.27.1.8; the cdc50 p-type atpase lipid flippase subunit (cdc50) family.
DR   EPD; H2L0H3; -.
DR   PaxDb; H2L0H3; -.
DR   PeptideAtlas; H2L0H3; -.
DR   EnsemblMetazoa; R08C7.2a.1; R08C7.2a.1; WBGene00019946. [H2L0H3-1]
DR   EnsemblMetazoa; R08C7.2c.1; R08C7.2c.1; WBGene00019946. [H2L0H3-3]
DR   EnsemblMetazoa; R08C7.2d.1; R08C7.2d.1; WBGene00019946. [H2L0H3-4]
DR   GeneID; 177213; -.
DR   KEGG; cel:CELE_R08C7.2; -.
DR   UCSC; R08C7.2a; c. elegans.
DR   CTD; 177213; -.
DR   WormBase; R08C7.2a; CE07425; WBGene00019946; chat-1. [H2L0H3-1]
DR   WormBase; R08C7.2b; CE33681; WBGene00019946; chat-1. [H2L0H3-2]
DR   WormBase; R08C7.2c; CE39610; WBGene00019946; chat-1. [H2L0H3-3]
DR   WormBase; R08C7.2d; CE48798; WBGene00019946; chat-1. [H2L0H3-4]
DR   eggNOG; KOG2952; Eukaryota.
DR   GeneTree; ENSGT00390000004660; -.
DR   HOGENOM; CLU_025025_1_0_1; -.
DR   InParanoid; H2L0H3; -.
DR   OMA; TWNNDQP; -.
DR   OrthoDB; 889671at2759; -.
DR   PhylomeDB; H2L0H3; -.
DR   Reactome; R-CEL-6798695; Neutrophil degranulation.
DR   PRO; PR:H2L0H3; -.
DR   Proteomes; UP000001940; Chromosome IV.
DR   Bgee; WBGene00019946; Expressed in pharyngeal muscle cell (C elegans) and 4 other tissues.
DR   GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0055038; C:recycling endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0033036; P:macromolecule localization; IEA:UniProt.
DR   InterPro; IPR005045; CDC50/LEM3_fam.
DR   PANTHER; PTHR10926; PTHR10926; 1.
DR   Pfam; PF03381; CDC50; 1.
DR   PIRSF; PIRSF015840; DUF284_TM_euk; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Endoplasmic reticulum; Endosome;
KW   Membrane; Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..348
FT                   /note="CDC50 family protein chat-1"
FT                   /evidence="ECO:0000305"
FT                   /id="PRO_0000435142"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        309..329
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..241
FT                   /note="Missing (in isoform d)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058020"
FT   VAR_SEQ         1..181
FT                   /note="Missing (in isoform c)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058021"
FT   VAR_SEQ         216..219
FT                   /note="NTTK -> VLTS (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058022"
FT   VAR_SEQ         220..348
FT                   /note="Missing (in isoform b)"
FT                   /evidence="ECO:0000305"
FT                   /id="VSP_058023"
SQ   SEQUENCE   348 AA;  38572 MW;  A1BB018706407492 CRC64;
     MPPRDAVPTS TQVSGIGADG VQTEKVLKNR PKASALRQQK LPAWQPILTA TTVIPTVFVI
     GAIFLPIGVF LFIASDAVSE FTVEYTNCLS PCQLQINLPN AFDGDVFLYY NLENYYQNHR
     RYVKSRNDQQ YLGDLTNVKD CAPFDIDPAT KKPIAPCGAI ANSIFNDTFT LAHRADTGIV
     TMVPVTTQGV IWNVDKDRKF KNPPLNDGNL CDAFNNTTKP PNWSKNPCEV GGFENVDFIV
     WMRTAALPYF KKLWRIVDRT TNPLFSNGLP QGTYILTVEN NYPVQSFGGK KEFVISTTSW
     AGGKNSFLGI AYLVVGSLAI VLGVVFIVIH MKFGHSMNEL SNVSEIHH
 
 
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