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   27-MAR-2024, entry version 128.
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,
RC   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).
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; 5.
DR   STRING; 10090.ENSMUSP00000051293; -.
DR   GlyConnect; 2218; 7 N-Linked glycans (2 sites).
DR   GlyCosmos; Q8VBZ3; 6 sites, 7 glycans.
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; 10090-ENSMUSP00000051293; -.
DR   PeptideAtlas; Q8VBZ3; -.
DR   ProteomicsDB; 285493; -.
DR   Pumba; Q8VBZ3; -.
DR   Antibodypedia; 31237; 190 antibodies from 29 providers.
DR   DNASU; 56457; -.
DR   Ensembl; ENSMUST00000055242.11; ENSMUSP00000051293.10; ENSMUSG00000002981.11.
DR   GeneID; 56457; -.
DR   KEGG; mmu:56457; -.
DR   UCSC; uc009fmq.1; mouse.
DR   AGR; MGI:1927155; -.
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; TLWAHFY; -.
DR   OrthoDB; 31537at2759; -.
DR   PhylomeDB; Q8VBZ3; -.
DR   TreeFam; TF318501; -.
DR   BioGRID-ORCS; 56457; 13 hits in 79 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 261 other cell types or tissues.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0009897; C:external side of plasma membrane; IDA:BHF-UCL.
DR   GO; GO:0098982; C:GABA-ergic synapse; ISO:MGI.
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:0099072; P:regulation of postsynaptic membrane neurotransmitter receptor levels; ISO:MGI.
DR   GO; GO:0033081; P:regulation of T cell differentiation in thymus; IMP:BHF-UCL.
DR   InterPro; IPR008429; CLPTM1.
DR   PANTHER; PTHR21347; CLEFT LIP AND PALATE ASSOCIATED TRANSMEMBRANE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR21347:SF14; CLEFT LIP AND PALATE TRANSMEMBRANE PROTEIN 1; 1.
DR   Pfam; PF05602; CLPTM1; 1.
DR   Genevisible; Q8VBZ3; MM.
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
//