ID   CLPT1_DANRE             Reviewed;         631 AA.
AC   Q6DEL2;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-AUG-2004, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Putative lipid scramblase CLPTM1;
DE   AltName: Full=Cleft lip and palate transmembrane protein 1 homolog;
GN   Name=clptm1; ORFNames=zgc:100803;
OS   Danio rerio (Zebrafish) (Brachydanio rerio).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Danionidae; Danioninae; Danio.
OX   NCBI_TaxID=7955;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
RG   NIH - Zebrafish Gene Collection (ZGC) project;
RL   Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Involved in GABAergic but not glutamatergic transmission.
CC       Binds and traps GABAA receptors in the endoplasmic reticulum (ER).
CC       Modulates postsynaptic GABAergic transmission, and therefore inhibitory
CC       neurotransmission, by reducing the plasma membrane expression of these
CC       receptors. Altered GABAergic signaling is one among many causes of
CC       cleft palate (By similarity). Might function as a lipid scramblase,
CC       translocating lipids in membranes from one leaflet to the other one (By
CC       similarity). Required for efficient glycosylphosphatidylinositol (GPI)
CC       inositol deacylation in the ER, which is a crucial step to switch GPI-
CC       anchored proteins (GPI-APs) from protein folding to transport states
CC       (By similarity). May play a role in T-cell development (By similarity).
CC       {ECO:0000250|UniProtKB:O96005, ECO:0000250|UniProtKB:Q8VBZ3,
CC       ECO:0000250|UniProtKB:Q96KA5}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- SIMILARITY: Belongs to the CLPTM1 family. {ECO:0000305}.
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DR   EMBL; BC077099; AAH77099.1; -; mRNA.
DR   AlphaFoldDB; Q6DEL2; -.
DR   STRING; 7955.ENSDARP00000046647; -.
DR   PaxDb; Q6DEL2; -.
DR   ZFIN; ZDB-GENE-040801-265; clptm1.
DR   eggNOG; KOG2489; Eukaryota.
DR   InParanoid; Q6DEL2; -.
DR   PhylomeDB; Q6DEL2; -.
DR   PRO; PR:Q6DEL2; -.
DR   Proteomes; UP000000437; Genome assembly.
DR   Proteomes; UP000814640; Unplaced.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   InterPro; IPR008429; CLPTM1.
DR   InterPro; IPR030434; CLPTM1L.
DR   PANTHER; PTHR21347; PTHR21347; 1.
DR   PANTHER; PTHR21347:SF0; PTHR21347:SF0; 1.
DR   Pfam; PF05602; CLPTM1; 1.
PE   2: Evidence at transcript level;
KW   Developmental protein; Differentiation; Glycoprotein; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..631
FT                   /note="Putative lipid scramblase CLPTM1"
FT                   /id="PRO_0000245098"
FT   TOPO_DOM        1..352
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        353..373
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        374..388
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        389..409
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        410..414
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        415..435
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        436..475
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        476..496
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        497..500
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        501..521
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        522..631
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          599..631
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        117
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        159
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        239
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        293
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        411
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   631 AA;  72898 MW;  3D60CBF5FA86C3CD CRC64;
     MAAQETQATQ QSSVSNGEVS SNGAAASGQV AQTGATAQDP QQQQQQQPSA WQVIKGVLFR
     IFIIWAISSW FRRGPSTPDP NTPAGAPRVP SRNLFPKDTL MDLYVYISQS EIFTDFNNTE
     ELFWYQQDLV YGEWTTGDSG DGCYEYYKEL DLSESVKQNG SIYMHIYFTK SGFHPDPKRK
     GQYRRLSTVH ATRMLNKYKR RKFLKTKNLL TGETEADPEM IKRAESHGPV EIISHWHPNL
     TINMVDDHTA WVKGSVPPPL DQHVKFDAVS GDYYPIVYFN DYWNLQKDYY PINDTLLNLP
     LRLTYCPLSL WRWQLYAAQS ARSPWNFLGE DTYEQSDEDQ DSVKVALLET NPYLLGLTIV
     VSIVHSIFEF LAFKNDIQFW NSRQSLEGLS VRSIIFGVFQ SLVVLLYILD NETNFVVQVS
     VFIGLLIDFW KITKVMDVRL DRENRIAGIV PRLVFKDKST YVESSTKIYD DMAFKYLSWL
     LYPLFGCYAV YSLLYVEHKG WYSWVLSMLY GFLLTFGFIT MTPQLFINYK MKSVAHLPWR
     MLTYKALNTF IDDLFAFVIK MPMMYRIGCL RDDVVFFIYL YQRWIYRVDP NRVNEFGTSG
     VDHSKDSSAQ PAAGETPAAI TEKPEGEKKN D