CLP1L_BOVIN
ID CLP1L_BOVIN Reviewed; 538 AA.
AC A2VE61;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=Lipid scramblase CLPTM1L {ECO:0000305};
DE AltName: Full=Cisplatin resistance-related protein 9 {ECO:0000250|UniProtKB:Q96KA5};
DE Short=CRR9p;
DE AltName: Full=Cleft lip and palate transmembrane protein 1-like protein;
DE Short=CLPTM1-like protein;
GN Name=CLPTM1L;
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=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Scramblase that mediates the translocation of
CC glucosaminylphosphatidylinositol (alpha-D-GlcN-(1-6)-(1,2-diacyl-sn-
CC glycero-3-phospho)-1D-myo-inositol, GlcN-PI) across the endoplasmic
CC reticulum (ER) membrane, from the cytosolic leaflet to the luminal
CC leaflet of the ER membrane, where it participates in the biosynthesis
CC of glycosylphosphatidylinositol (GPI). GPI is a lipid glycoconjugate
CC involved in post-translational modification of proteins. Can also
CC translocate 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)
CC (phosphatidylinositol or PI), as well as several other phospholipids
CC (1,2-diacyl-sn-glycero-3-phosphocholine, 1,2-diacyl-sn-glycero-3-
CC phosphoethanolamine), and N-acetylglucosaminylphosphatidylinositol
CC (GlcNAc-PI) in vitro. {ECO:0000250|UniProtKB:Q96KA5}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-phospho)-1D-
CC myo-inositol(in) = an alpha-D-GlcN-(1->6)-(1,2-diacyl-sn-glycero-3-
CC phospho)-1D-myo-inositol(out); Xref=Rhea:RHEA:71491,
CC ChEBI:CHEBI:57997; Evidence={ECO:0000250|UniProtKB:Q96KA5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=6-(alpha-D-glucosaminyl)-(1-octadecanoyl,2-(9Z)-octadecenoyl-
CC sn-glycero-3-phospho)-1D-myo-inositol(in) = 6-(alpha-D-glucosaminyl)-
CC (1-octadecanoyl,2-(9Z)-octadecenoyl-sn-glycero-3-phospho)-1D-myo-
CC inositol(out); Xref=Rhea:RHEA:71495, ChEBI:CHEBI:190691;
CC Evidence={ECO:0000250|UniProtKB:Q96KA5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(in) = a
CC 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-inositol)(out);
CC Xref=Rhea:RHEA:38691, ChEBI:CHEBI:57880;
CC Evidence={ECO:0000250|UniProtKB:Q96KA5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphocholine(in) = a 1,2-diacyl-
CC sn-glycero-3-phosphocholine(out); Xref=Rhea:RHEA:38571,
CC ChEBI:CHEBI:57643; Evidence={ECO:0000250|UniProtKB:Q96KA5};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phosphoethanolamine(in) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine(out); Xref=Rhea:RHEA:38895,
CC ChEBI:CHEBI:64612; Evidence={ECO:0000250|UniProtKB:Q96KA5};
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000305};
CC Multi-pass membrane protein {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the CLPTM1 family. {ECO:0000305}.
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DR EMBL; BC133589; AAI33590.1; -; mRNA.
DR RefSeq; NP_001075895.1; NM_001082426.2.
DR AlphaFoldDB; A2VE61; -.
DR STRING; 9913.ENSBTAP00000001754; -.
DR PaxDb; A2VE61; -.
DR PRIDE; A2VE61; -.
DR GeneID; 506200; -.
DR KEGG; bta:506200; -.
DR CTD; 81037; -.
DR eggNOG; KOG2489; Eukaryota.
DR InParanoid; A2VE61; -.
DR OrthoDB; 1106937at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISS:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0017128; F:phospholipid scramblase activity; ISS:UniProtKB.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR InterPro; IPR008429; CLPTM1.
DR InterPro; IPR030434; CLPTM1L.
DR PANTHER; PTHR21347; PTHR21347; 1.
DR PANTHER; PTHR21347:SF12; PTHR21347:SF12; 1.
DR Pfam; PF05602; CLPTM1; 1.
PE 2: Evidence at transcript level;
KW Apoptosis; Endoplasmic reticulum; Glycoprotein; Lipid transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..538
FT /note="Lipid scramblase CLPTM1L"
FT /id="PRO_0000331299"
FT TOPO_DOM 1..10
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..284
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 285..305
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 306..324
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 325..341
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 342..402
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..428
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..538
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT CARBOHYD 91
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 538 AA; 62101 MW; 1A4E16C2CA6CAC64 CRC64;
MWSGRSSFTS LVVGVFVVYV VHTCWVMYGI VYTRPCSGHG RCIQPYLAQR PKLQLSVYTT
TRSNLGSENN VDLVLNVEDF DVESKFERTV NVSVPKKTRN NGTLYAYVFL HHAGVLPWND
AKQVHLVSPL TTYMVPRPEE VSLLAGGPAA QQIEAEKRPT SALDEPVSHW RPRLTLNVMV
DNFVFDGASL PADVQRYMKM IQLGKTVQYL PILFIDQLSN RVKDLMVINR SSTELPLTVS
YDKISLGRLR FWIHMQDAVY SLQQFGFSEK DADEVKGIFV DTNLYFLALT FFVAAFHLLF
DFLAFKNDIS FWKKKKSMIG MSTKAVLWRC FSTVVIFLFL LDEQTSLPVL VPAGIGAAIE
LWKVKKALKM TVIWRGLWPT FQFGTYSESE RRTEEYDAQA MKYLSYLLYP LCIGGAIYSL
LNIKYKSWYS WLINSFVNGV YAFGFLFMLP QLFVNYKMKS VAHLPWKAFT YKAFNTFIDD
VFAFIITMPT SHRLACFRDD VVFLVYLYQR WLYPVDKSRV NEFGESYEDT PQRKPHTD
