CLP1L_DANRE
ID CLP1L_DANRE Reviewed; 538 AA.
AC Q6DHU1;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 84.
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; ORFNames=zgc:92063;
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].
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (JUL-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; BC075876; AAH75876.1; -; mRNA.
DR RefSeq; NP_001002380.1; NM_001002380.1.
DR AlphaFoldDB; Q6DHU1; -.
DR STRING; 7955.ENSDARP00000008246; -.
DR PaxDb; Q6DHU1; -.
DR Ensembl; ENSDART00000004585; ENSDARP00000008246; ENSDARG00000021048.
DR GeneID; 436653; -.
DR KEGG; dre:436653; -.
DR CTD; 81037; -.
DR ZFIN; ZDB-GENE-040718-75; clptm1l.
DR eggNOG; KOG2489; Eukaryota.
DR GeneTree; ENSGT00530000063461; -.
DR HOGENOM; CLU_019907_4_1_1; -.
DR InParanoid; Q6DHU1; -.
DR OMA; QFDRQGM; -.
DR OrthoDB; 1106937at2759; -.
DR PhylomeDB; Q6DHU1; -.
DR TreeFam; TF318501; -.
DR PRO; PR:Q6DHU1; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Chromosome 19.
DR Bgee; ENSDARG00000021048; Expressed in mature ovarian follicle and 26 other tissues.
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_0000331304"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..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 REGION 140..166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 149..166
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 90
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 229
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 538 AA; 62497 MW; 2AF5A298D1BE6362 CRC64;
MFPKTSFTSL IVGVFLLYVL HTCWVMYGIV YTKPCEKRRA ESCISPYLAA KPRLQLSVYT
ALRPNADGGH SLIHREEEFD VNTKFEKLVN VSLPKKTRKN GTLYAMVFLH QAGVSPWQDP
HQVHLVTQLT TYMLPKPPEI SLITGQDEPE KPDQQKQSSD SELDRPVSHW RSRLTLNVVS
ENFLFDREAL PGDVHRYMRV YQSGKKMIYL PLLFVDELSN RVKDLMEINS SSTELPLTIT
YDSIALGKLR FWIHMQDAVY SLQQFGFTEK DADEIKGIFV DTNLYFLALT FFVAAFHLLF
DFLAFKNDIS FWKHKKSMVG MSSKAVLWRC FSTIVIFLYL LDEQTSLLVL VPAGIGSLIE
VWKVKKAFKI HVIWRGLTPT FLFGKLDESE KRTEEYDTLA MKYLSYLLYP LCVGGAVYAL
VFVKYKSWYS WIINSLVNGV YAFGFLFMLP QLFVNYKLKS VAHLPWKAFM YKAFNTFIDD
VFAFIITMPT SHRLACFRDD VVFLVYLYQR WLYPVDRSRV NEYGVSYDEK PKGKSHED
