CLPT1_BOVIN
ID CLPT1_BOVIN Reviewed; 670 AA.
AC Q2NL17;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=Putative lipid scramblase CLPTM1;
DE AltName: Full=Cleft lip and palate transmembrane protein 1 homolog;
GN Name=CLPTM1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Liver;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (DEC-2005) 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; BC111212; AAI11213.1; -; mRNA.
DR RefSeq; NP_001040078.1; NM_001046613.1.
DR AlphaFoldDB; Q2NL17; -.
DR STRING; 9913.ENSBTAP00000027395; -.
DR PaxDb; Q2NL17; -.
DR PRIDE; Q2NL17; -.
DR Ensembl; ENSBTAT00000027395; ENSBTAP00000027395; ENSBTAG00000020560.
DR GeneID; 618037; -.
DR KEGG; bta:618037; -.
DR CTD; 1209; -.
DR VEuPathDB; HostDB:ENSBTAG00000020560; -.
DR VGNC; VGNC:27460; CLPTM1.
DR eggNOG; KOG2489; Eukaryota.
DR GeneTree; ENSGT00530000063461; -.
DR InParanoid; Q2NL17; -.
DR OMA; NMLYGYL; -.
DR OrthoDB; 1106937at2759; -.
DR Proteomes; UP000009136; Chromosome 18.
DR Bgee; ENSBTAG00000020560; Expressed in pigment epithelium of eye and 103 other tissues.
DR GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0050811; F:GABA receptor binding; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; IEA:Ensembl.
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 Acetylation; Developmental protein; Differentiation; Glycoprotein;
KW Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:O96005"
FT CHAIN 2..670
FT /note="Putative lipid scramblase CLPTM1"
FT /id="PRO_0000245095"
FT TOPO_DOM 2..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..502
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..670
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 609..670
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..642
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 643..657
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:O96005"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O96005"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 670 AA; 75881 MW; CD526AF5B0CE3F19 CRC64;
MAAAQEADGA GSAVVAAGGG SSGQVTSNGS VGRDPPAETQ PQNPPPQPAP NAWQVIKGVL
FRIFIIWAIS SWFRRGPAPQ DQAGPGGAPR VASRNLFPKD TLMNLHVYIS EHEHFTDFNA
TSALFWEQQD LVYGDWTSGE NSDGCYEHFA ELDIPQSVQQ NGSIYIHVYF TKSGFHPDPR
QKALYRRLAT VHMSRMINKY KRRRFQKTKN LLTGETEADP EMIKRAEDYG PVEVISHWHP
NITINIVDDH TPWVKGSVPP PLDQYVKFDA VSGDYYPIIY FNDYWNLQKD YYPINESLAS
LPLRVSFCPL SLWRWQLYAA QSAKSPWNFL GDELYEQSDE EQDSVKVALL ETNPYLLALT
IIVSIVHSVF EFLAFKNDIQ FWNSRQSLEG LSVRSVFFGV FQSFVVLLYI LDNETNFVVQ
VSVFIGVLID LWKITKVMDV RLDREHKVAG LLPRPTFQDK STYVESSTKV YDDMAFRYLS
WILFPLLGCY AVYSLLYLEH KGWYSWVLSM LYGFLLTFGF ITMTPQLFIN YKLKSVAHLP
WRMLTYKALN TFIDDLFAFV IKMPVMYRIG CLRDDVVFFI YLYQRWIYRV DPTRVNEFGM
SGEAPTAAAP VAEAPPAAGA LSSAPSPTTT TEAAREEAST PPPSQAPQGP SSASEPQEAP
PKPAEDKKRD
