CLP1L_MOUSE
ID CLP1L_MOUSE Reviewed; 539 AA.
AC Q8BXA5; Q3U176; Q8C053; Q8R0P2;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Embryonic head, Olfactory bulb, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 22-539.
RC TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver, Pancreas, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26562.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC27798.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK032295; BAC27798.1; ALT_FRAME; mRNA.
DR EMBL; AK048357; BAC33311.1; -; mRNA.
DR EMBL; AK156203; BAE33624.1; -; mRNA.
DR EMBL; BC026562; AAH26562.1; ALT_INIT; mRNA.
DR CCDS; CCDS56894.1; -.
DR RefSeq; NP_666159.2; NM_146047.2.
DR AlphaFoldDB; Q8BXA5; -.
DR STRING; 10090.ENSMUSP00000022102; -.
DR GlyConnect; 2219; 7 N-Linked glycans (3 sites).
DR GlyGen; Q8BXA5; 3 sites, 7 N-linked glycans (3 sites).
DR PhosphoSitePlus; Q8BXA5; -.
DR EPD; Q8BXA5; -.
DR jPOST; Q8BXA5; -.
DR MaxQB; Q8BXA5; -.
DR PaxDb; Q8BXA5; -.
DR PeptideAtlas; Q8BXA5; -.
DR PRIDE; Q8BXA5; -.
DR ProteomicsDB; 283313; -.
DR Antibodypedia; 3079; 217 antibodies from 22 providers.
DR Ensembl; ENSMUST00000022102; ENSMUSP00000022102; ENSMUSG00000021610.
DR GeneID; 218335; -.
DR KEGG; mmu:218335; -.
DR UCSC; uc007rdo.2; mouse.
DR CTD; 81037; -.
DR MGI; MGI:2442892; Clptm1l.
DR VEuPathDB; HostDB:ENSMUSG00000021610; -.
DR eggNOG; KOG2489; Eukaryota.
DR GeneTree; ENSGT00530000063461; -.
DR HOGENOM; CLU_019907_4_1_1; -.
DR InParanoid; Q8BXA5; -.
DR OMA; QFDRQGM; -.
DR OrthoDB; 1106937at2759; -.
DR PhylomeDB; Q8BXA5; -.
DR TreeFam; TF318501; -.
DR BioGRID-ORCS; 218335; 1 hit in 72 CRISPR screens.
DR ChiTaRS; Clptm1l; mouse.
DR PRO; PR:Q8BXA5; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q8BXA5; protein.
DR Bgee; ENSMUSG00000021610; Expressed in lacrimal gland and 250 other tissues.
DR Genevisible; Q8BXA5; MM.
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 1: Evidence at protein level;
KW Apoptosis; Endoplasmic reticulum; Glycoprotein; Lipid transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..539
FT /note="Lipid scramblase CLPTM1L"
FT /id="PRO_0000331301"
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..285
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 307..325
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 326..342
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 343..403
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 425..429
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 451..539
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"
FT CONFLICT 212
FT /note="P -> L (in Ref. 1; BAE33624)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 539 AA; 62183 MW; D08CF6B6E31B7AD9 CRC64;
MWSGRSSFTS LVVGVFLVYV VHTCWVMYGI VYTRPCSGDS NCIQPYLALR PKLQLSVYTT
TRSSLGAENN VDLILNVEDF DVDSKFERTV NVSVPKKTRN NGTLYAYIFL HHAGILPWQD
GKQVHVVSTL TTYMIPKPEE INLLTGESAT QQQIEAEKKP SNALDEPVSH WRPRLTLNVM
VDDFVFDGSS LPADVHRYMK MIQLGKTVHY LPILFIDQLS NRVKDLMVIN RSTTELPLTV
SYDKISLGRL RFWIHMQDAV YSLQQFGFSE KDADELKGIF VDTNLYLLAL TFFVAAFHLL
FDFLAFKSDI SFWKKKKSMI GMSTKAVLWR CFSTVVIFLF LLDEQTSLLV LIPAGVGAAI
ELWKVKKALK ITVAWRGLRP VFQFGTHSES ERKTEKYDAQ AMKYLSYLLY PLCVGGAVYS
LLNIKYKSWY SWLINSFVNG VYAFGFLFML PQLFVNYKMK SVAHLPWKAF TYKAFNTFID
DVFAFIITMP TSHRLACFRD DVVFLVYLYQ RWLYPVDKSR VNEFGESYEE QPKRKPHPD
