CLPT1_MOUSE
ID CLPT1_MOUSE Reviewed; 664 AA.
AC Q8VBZ3; O08708; Q3U758; Q3U823; Q3UG77; Q8VEJ6;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Putative lipid scramblase CLPTM1 {ECO:0000250|UniProtKB:O96005};
DE AltName: Full=Cleft lip and palate transmembrane protein 1 homolog;
DE AltName: Full=Thymic epithelial cell surface antigen {ECO:0000303|PubMed:9218588};
GN Name=Clptm1; Synonyms=N14;
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 [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC STRAIN=BALB/cJ; TISSUE=Thymus;
RX PubMed=9218588;
RA Takeuchi T., Kuro-o M., Miyazawa H., Ohtsuki Y., Yamamoto H.;
RT "Transgenic expression of a novel thymic epithelial cell antigen stimulates
RT aberrant development of thymocytes.";
RL J. Immunol. 159:726-733(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Bone marrow;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary tumor, and Salivary gland;
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 [4]
RP DEVELOPMENTAL STAGE, AND SUBCELLULAR LOCATION.
RX PubMed=9828125; DOI=10.1006/geno.1998.5577;
RA Yoshiura K., Machida J., Daack-Hirsch S., Patil S.R., Ashworth L.K.,
RA Hecht J.T., Murray J.C.;
RT "Characterization of a novel gene disrupted by a balanced chromosomal
RT translocation t(2;19)(q11.2;q13.3) in a family with cleft lip and palate.";
RL Genomics 54:231-240(1998).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC 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).
RN [6]
RP FUNCTION.
RX PubMed=29395912; DOI=10.1016/j.neuron.2017.12.038;
RA Ge Y., Kang Y., Cassidy R.M., Moon K.M., Lewis R., Wong R.O.L.,
RA Foster L.J., Craig A.M.;
RT "Clptm1 Limits Forward Trafficking of GABAA Receptors to Scale Inhibitory
RT Synaptic Strength.";
RL Neuron 97:596-610(2018).
CC -!- FUNCTION: Involved in GABAergic but not glutamatergic transmission
CC (PubMed:29395912). Binds and traps GABAA receptors in the endoplasmic
CC reticulum (ER) (PubMed:29395912). Modulates postsynaptic GABAergic
CC transmission, and therefore inhibitory neurotransmission, by reducing
CC the plasma membrane expression of these receptors (PubMed:29395912).
CC Altered GABAergic signaling is one among many causes of cleft palate
CC (PubMed:29395912). Might function as a lipid scramblase, translocating
CC lipids in membranes from one leaflet to the other one (By similarity).
CC Required for efficient glycosylphosphatidylinositol (GPI) inositol
CC deacylation in the ER, which is a crucial step to switch GPI-anchored
CC proteins (GPI-APs) from protein folding to transport states (By
CC similarity). May play a role in T-cell development (PubMed:9218588).
CC {ECO:0000250|UniProtKB:O96005, ECO:0000250|UniProtKB:Q96KA5,
CC ECO:0000269|PubMed:29395912, ECO:0000269|PubMed:9218588,
CC ECO:0000303|PubMed:29395912}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305|PubMed:9828125}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:9218588, PubMed:9828125).
CC Expressed by subcapsular and outer cortical thymic cells
CC (PubMed:9218588). {ECO:0000269|PubMed:9218588,
CC ECO:0000269|PubMed:9828125}.
CC -!- DEVELOPMENTAL STAGE: Ubiquitously expressed in mouse embryo.
CC {ECO:0000269|PubMed:9828125}.
CC -!- MISCELLANEOUS: Mice overexpressing Clptm1 exhibit an aberrant
CC development of thymocytes.
CC -!- SIMILARITY: Belongs to the CLPTM1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA19836.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; D67067; BAA19836.1; ALT_FRAME; mRNA.
DR EMBL; AK148080; BAE28332.1; -; mRNA.
DR EMBL; AK152410; BAE31196.1; -; mRNA.
DR EMBL; AK152809; BAE31514.1; -; mRNA.
DR EMBL; BC018389; AAH18389.1; -; mRNA.
DR EMBL; BC022172; AAH22172.1; -; mRNA.
DR CCDS; CCDS39800.1; -.
DR RefSeq; NP_062623.2; NM_019649.2.
DR AlphaFoldDB; Q8VBZ3; -.
DR BioGRID; 207996; 4.
DR STRING; 10090.ENSMUSP00000051293; -.
DR GlyConnect; 2218; 7 N-Linked glycans (2 sites).
DR GlyGen; Q8VBZ3; 6 sites, 7 N-linked glycans (2 sites).
DR iPTMnet; Q8VBZ3; -.
DR PhosphoSitePlus; Q8VBZ3; -.
DR SwissPalm; Q8VBZ3; -.
DR EPD; Q8VBZ3; -.
DR jPOST; Q8VBZ3; -.
DR MaxQB; Q8VBZ3; -.
DR PaxDb; Q8VBZ3; -.
DR PeptideAtlas; Q8VBZ3; -.
DR PRIDE; Q8VBZ3; -.
DR ProteomicsDB; 285493; -.
DR Antibodypedia; 31237; 165 antibodies from 29 providers.
DR DNASU; 56457; -.
DR Ensembl; ENSMUST00000055242; ENSMUSP00000051293; ENSMUSG00000002981.
DR GeneID; 56457; -.
DR KEGG; mmu:56457; -.
DR UCSC; uc009fmq.1; mouse.
DR CTD; 1209; -.
DR MGI; MGI:1927155; Clptm1.
DR VEuPathDB; HostDB:ENSMUSG00000002981; -.
DR eggNOG; KOG2489; Eukaryota.
DR GeneTree; ENSGT00530000063461; -.
DR HOGENOM; CLU_019907_3_1_1; -.
DR InParanoid; Q8VBZ3; -.
DR OMA; NMLYGYL; -.
DR OrthoDB; 1106937at2759; -.
DR PhylomeDB; Q8VBZ3; -.
DR TreeFam; TF318501; -.
DR BioGRID-ORCS; 56457; 13 hits in 74 CRISPR screens.
DR ChiTaRS; Clptm1; mouse.
DR PRO; PR:Q8VBZ3; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q8VBZ3; protein.
DR Bgee; ENSMUSG00000002981; Expressed in embryonic brain and 257 other tissues.
DR Genevisible; Q8VBZ3; MM.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
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; IDA:UniProtKB.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; IMP:BHF-UCL.
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 1: Evidence at protein 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..664
FT /note="Putative lipid scramblase CLPTM1"
FT /id="PRO_0000245097"
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..664
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 618..664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..38
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 618..649
FT /note="Polar 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"
FT CONFLICT 161
FT /note="N -> Y (in Ref. 2; BAE28332)"
FT /evidence="ECO:0000305"
FT CONFLICT 470
FT /note="V -> A (in Ref. 2; BAE31514)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 664 AA; 75291 MW; 6F78F58549CC7EE1 CRC64;
MAAAQEADGA GSAVVAAGGG SSGQVTSNGS IGRDTPAETQ PQNPPPQPAP NAWQVIKGVL
FRIFIIWAIS SWFRRGPSPQ DQSGPGGAPR VASRNLFPKD TLMNLHVYIS EHEHFTDFNA
TSALFWEQHD LVYGDWTSGE NSDGCYEHFA ELDIPQSVQQ NGSIYIHVYF TKSGFHPDPR
QKALYRRLAT VHMSRMINKY KRRRFQKTKN LLTGETEADP EMIKRAEDYG PVEVISHWHP
NITINIVDDH TPWVKGSVPP PLDQYVKFDA VSGDYYPIIY FNDYWNLQKD YYPINESLAS
LPLRVSFCPL SLWRWQLYAA QSTKSPWNFL GDELYEQSDE EQDSVKVALL ETSPYLLALT
IIVSIVHSVF EFLAFKNDIQ FWNSRQSLEG LSVRSVFFGV FQSFVVLLYI LDNETNFVVQ
VSVFIGVLID LWKITKVMDV RLDREHRVAG IFPCPTFKDK STYIESSTKV YDDMAFRYLS
WILFPLLGCY AVYSLLYLEH KGWYSWVLSM LYGFLLTFGF ITMTPQLFIN YKLKSVAHLP
WRMLTYKALN TFIDDLFAFV IKMPVMYRIG CLRDDVVFFI YLYQRWIYRV DPTRVNEFGM
SGEDVSAAAS RAQASTAAGA LTPAPSTAVS GEDASTVPKA TSGACTASQP QEAPPKPAED
KKKD
