CLP1L_PONAB
ID CLP1L_PONAB Reviewed; 538 AA.
AC Q5R7B1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 48.
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 Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) 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; CR860207; CAH92349.1; -; mRNA.
DR RefSeq; NP_001126382.1; NM_001132910.1.
DR AlphaFoldDB; Q5R7B1; -.
DR STRING; 9601.ENSPPYP00000017110; -.
DR GeneID; 100173363; -.
DR KEGG; pon:100173363; -.
DR CTD; 81037; -.
DR eggNOG; KOG2489; Eukaryota.
DR InParanoid; Q5R7B1; -.
DR OrthoDB; 1106937at2759; -.
DR Proteomes; UP000001595; 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: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_0000331302"
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..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..346
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 347..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 365..402
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 424..428
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 450..538
FT /note="Cytoplasmic"
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; 62132 MW; 8833609900A867D0 CRC64;
MWSGRSSFTS LVVGVFVVYV VHTCWVMYGI VYTRPCSGDA NCIQPYLARR PKLQLSVYTT
TRSHLGAENN IDLVLNVEDF DVESKFERTV NVSVPKKTRN NGTLYAYIFL HHAGVLPWHD
GKQVHLVSPL TTYMVPKPEE INLLTGESDT QQIEAEKKPT SALDEPVSHW RPRLALNVMA
DNFVFDGSSL PADVHRYMKM IQLGKTVHYL PILFIDQLSN RVKDLMVINR STTELPLTVS
YDKVSLGRLR FWIHMQDAVY SLQQFGFSEK DADEVKGIFV DTNLYFLALT FFVAAFHLLF
DFLAFKNDIS FWKKKKSMIG MSTKAVLWRC FSTVVIFLFL LDEQTSLLVL VPAGVGAAIE
LWKVKKALKM TILWRGLMPE FELGTYSESE RKTEEYDTQA MKYLSYLLYP LCVGGAVYSL
LNIKYKSWYS WLINSFVNGV YAFGFLFMLP QLFVNYKLKS VAHLPWKAFT YKAFNTFIDD
VFAFIITMPT SHRLACFRDD VVFLVYLYQR WLYPVDKRRV NEFGESYEEK AARAPHTD
