ID   CLPT1_HUMAN             Reviewed;         669 AA.
AC   O96005; B3KQH2; B4DDS3; B4E2X9; B7Z9X9; F5H8J3; Q53ET6; Q9BSS5;
DT   11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   27-MAR-2024, entry version 164.
DE   RecName: Full=Putative lipid scramblase CLPTM1 {ECO:0000305};
DE   AltName: Full=Cleft lip and palate transmembrane protein 1;
GN   Name=CLPTM1;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 1), CHROMOSOMAL
RP   TRANSLOCATION, TISSUE SPECIFICITY, AND POLYMORPHISM.
RC   TISSUE=Craniofacial;
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   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP   CYS-478.
RC   TISSUE=Thalamus, and Uterus;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA   Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA   Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA   Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA   Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA   Isogai T.;
RT   "Signal sequence and keyword trap in silico for selection of full-length
RT   human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT   libraries.";
RL   DNA Res. 12:117-126(2005).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
RA   Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL   Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15057824; DOI=10.1038/nature02399;
RA   Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA   Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA   Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA   Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA   Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA   Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA   Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA   Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA   Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA   McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA   Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA   Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA   She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA   Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA   Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA   Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA   Rubin E.M., Lucas S.M.;
RT   "The DNA sequence and biology of human chromosome 19.";
RL   Nature 428:529-535(2004).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Choriocarcinoma, and Melanoma;
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   [8]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-656 (ISOFORM 1).
RA   Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA   Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA   Phelan M., Farmer A.;
RT   "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL   Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN   [9]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-295.
RC   TISSUE=Platelet;
RX   PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA   Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT   "Elucidation of N-glycosylation sites on human platelet proteins: a
RT   glycoproteomic approach.";
RL   Mol. Cell. Proteomics 5:226-233(2006).
RN   [10]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-295.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [11]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [12]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP   METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [14]
RP   ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX   PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA   Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA   Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA   Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT   "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT   acetylation defects.";
RL   Hum. Mol. Genet. 24:1956-1976(2015).
RN   [15]
RP   FUNCTION.
RX   PubMed=29255114; DOI=10.1083/jcb.201706135;
RA   Liu Y.S., Guo X.Y., Hirata T., Rong Y., Motooka D., Kitajima T.,
RA   Murakami Y., Gao X.D., Nakamura S., Kinoshita T., Fujita M.;
RT   "N-Glycan-dependent protein folding and endoplasmic reticulum retention
RT   regulate GPI-anchor processing.";
RL   J. Cell Biol. 217:585-599(2018).
CC   -!- FUNCTION: Involved in GABAergic but not glutamatergic transmission.
CC       Binds and traps GABAA receptors in the endoplasmic reticulum (ER).
CC       Modulates postsynaptic GABAergic transmission, and therefore inhibitory
CC       neurotransmission, by reducing the plasma membrane expression of these
CC       receptors. Altered GABAergic signaling is one among many causes of
CC       cleft palate (By similarity). Might function as a lipid scramblase,
CC       translocating lipids in membranes from one leaflet to the other one (By
CC       similarity). Required for efficient glycosylphosphatidylinositol (GPI)
CC       inositol deacylation in the ER, which is a crucial step to switch GPI-
CC       anchored proteins (GPI-APs) from protein folding to transport states
CC       (PubMed:29255114). May play a role in T-cell development (By
CC       similarity). {ECO:0000250|UniProtKB:Q8VBZ3,
CC       ECO:0000250|UniProtKB:Q96KA5, ECO:0000269|PubMed:29255114}.
CC   -!- INTERACTION:
CC       O96005; Q8VCW4: Unc93b1; Xeno; NbExp=2; IntAct=EBI-2873194, EBI-6116986;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=O96005-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=O96005-3; Sequence=VSP_055525;
CC       Name=3;
CC         IsoId=O96005-4; Sequence=VSP_055526;
CC   -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9828125}.
CC   -!- POLYMORPHISM: A chromosomal translocation involving CLPTM1 is found in
CC       a family with cleft lip and palate. However, no etiologic link with the
CC       disease is characterized. Translocation t(2;19)(q11.2;q13.3).
CC       {ECO:0000269|PubMed:9828125}.
CC   -!- SIMILARITY: Belongs to the CLPTM1 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH04865.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC       Sequence=AAP35926.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR   EMBL; AF037338; AAC97420.1; -; Genomic_DNA.
DR   EMBL; AF037339; AAC98151.1; -; mRNA.
DR   EMBL; AK293314; BAG56834.1; -; mRNA.
DR   EMBL; AK304480; BAG65291.1; -; mRNA.
DR   EMBL; AK316094; BAH14465.1; -; mRNA.
DR   EMBL; AK074935; BAG52034.1; -; mRNA.
DR   EMBL; AK223553; BAD97273.1; -; mRNA.
DR   EMBL; AC011481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471126; EAW57314.1; -; Genomic_DNA.
DR   EMBL; BC004865; AAH04865.1; ALT_SEQ; mRNA.
DR   EMBL; BC012359; AAH12359.1; -; mRNA.
DR   EMBL; BT007262; AAP35926.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS12651.1; -. [O96005-1]
DR   CCDS; CCDS74394.1; -. [O96005-4]
DR   CCDS; CCDS74395.1; -. [O96005-3]
DR   RefSeq; NP_001269104.1; NM_001282175.1. [O96005-4]
DR   RefSeq; NP_001269105.1; NM_001282176.1. [O96005-3]
DR   RefSeq; NP_001285.1; NM_001294.3. [O96005-1]
DR   AlphaFoldDB; O96005; -.
DR   BioGRID; 107619; 170.
DR   IntAct; O96005; 35.
DR   MINT; O96005; -.
DR   STRING; 9606.ENSP00000336994; -.
DR   TCDB; 8.A.125.1.1; the cleft lip and palate transmembrane protein 1 (clptm1) family.
DR   GlyConnect; 1116; 5 N-Linked glycans (1 site).
DR   GlyCosmos; O96005; 6 sites, 5 glycans.
DR   GlyGen; O96005; 10 sites, 5 N-linked glycans (1 site), 2 O-linked glycans (3 sites).
DR   iPTMnet; O96005; -.
DR   MetOSite; O96005; -.
DR   PhosphoSitePlus; O96005; -.
DR   SwissPalm; O96005; -.
DR   BioMuta; CLPTM1; -.
DR   EPD; O96005; -.
DR   jPOST; O96005; -.
DR   MassIVE; O96005; -.
DR   MaxQB; O96005; -.
DR   PaxDb; 9606-ENSP00000336994; -.
DR   PeptideAtlas; O96005; -.
DR   ProteomicsDB; 27801; -.
DR   ProteomicsDB; 3887; -.
DR   ProteomicsDB; 51184; -. [O96005-1]
DR   Pumba; O96005; -.
DR   TopDownProteomics; O96005-1; -. [O96005-1]
DR   Antibodypedia; 31237; 190 antibodies from 29 providers.
DR   DNASU; 1209; -.
DR   Ensembl; ENST00000337392.10; ENSP00000336994.4; ENSG00000104853.16. [O96005-1]
DR   Ensembl; ENST00000541297.6; ENSP00000442011.1; ENSG00000104853.16. [O96005-4]
DR   Ensembl; ENST00000546079.5; ENSP00000443192.1; ENSG00000104853.16. [O96005-3]
DR   GeneID; 1209; -.
DR   KEGG; hsa:1209; -.
DR   MANE-Select; ENST00000337392.10; ENSP00000336994.4; NM_001294.4; NP_001285.1.
DR   UCSC; uc002pai.5; human. [O96005-1]
DR   AGR; HGNC:2087; -.
DR   CTD; 1209; -.
DR   DisGeNET; 1209; -.
DR   GeneCards; CLPTM1; -.
DR   HGNC; HGNC:2087; CLPTM1.
DR   HPA; ENSG00000104853; Low tissue specificity.
DR   MIM; 604783; gene.
DR   neXtProt; NX_O96005; -.
DR   OpenTargets; ENSG00000104853; -.
DR   PharmGKB; PA26613; -.
DR   VEuPathDB; HostDB:ENSG00000104853; -.
DR   eggNOG; KOG2489; Eukaryota.
DR   GeneTree; ENSGT00530000063461; -.
DR   HOGENOM; CLU_019907_3_1_1; -.
DR   InParanoid; O96005; -.
DR   OMA; TLWAHFY; -.
DR   OrthoDB; 31537at2759; -.
DR   PhylomeDB; O96005; -.
DR   TreeFam; TF318501; -.
DR   PathwayCommons; O96005; -.
DR   SignaLink; O96005; -.
DR   BioGRID-ORCS; 1209; 23 hits in 1156 CRISPR screens.
DR   ChiTaRS; CLPTM1; human.
DR   GeneWiki; Cleft_lip_and_palate_transmembrane_protein_1; -.
DR   GenomeRNAi; 1209; -.
DR   Pharos; O96005; Tbio.
DR   PRO; PR:O96005; -.
DR   Proteomes; UP000005640; Chromosome 19.
DR   RNAct; O96005; Protein.
DR   Bgee; ENSG00000104853; Expressed in right adrenal gland cortex and 198 other cell types or tissues.
DR   ExpressionAtlas; O96005; baseline and differential.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0009897; C:external side of plasma membrane; ISS:BHF-UCL.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR   GO; GO:0050811; F:GABA receptor binding; IEA:Ensembl.
DR   GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR   GO; GO:0033081; P:regulation of T cell differentiation in thymus; ISS: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; O96005; HS.
PE   1: Evidence at protein level;
KW   Acetylation; Alternative splicing; Chromosomal rearrangement;
KW   Developmental protein; Differentiation; Glycoprotein; Membrane;
KW   Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:25489052,
FT                   ECO:0007744|PubMed:22814378"
FT   CHAIN           2..669
FT                   /note="Putative lipid scramblase CLPTM1"
FT                   /id="PRO_0000245096"
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..669
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          1..50
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..669
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        19..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        622..654
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         2
FT                   /note="N-acetylalanine"
FT                   /evidence="ECO:0000269|PubMed:25489052,
FT                   ECO:0007744|PubMed:22814378"
FT   MOD_RES         601
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
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:0000269|PubMed:16263699,
FT                   ECO:0000269|PubMed:19159218"
FT   CARBOHYD        413
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..102
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055525"
FT   VAR_SEQ         1..24
FT                   /note="MAAAQEADGARSAVVAAGGGSSGQ -> MSRKAHITEK (in isoform
FT                   3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_055526"
FT   VARIANT         478
FT                   /note="Y -> C (in dbSNP:rs140564801)"
FT                   /evidence="ECO:0000269|PubMed:14702039"
FT                   /id="VAR_071064"
FT   CONFLICT        103
FT                   /note="M -> V (in Ref. 2; BAG65291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        175
FT                   /note="F -> S (in Ref. 2; BAG65291)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="W -> R (in Ref. 2; BAH14465)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        494
FT                   /note="S -> G (in Ref. 3; BAG52034)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        637
FT                   /note="A -> T (in Ref. 4; BAD97273)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   669 AA;  76097 MW;  769AB9D291917339 CRC64;
     MAAAQEADGA RSAVVAAGGG SSGQVTSNGS IGRDPPAETQ PQNPPAQPAP NAWQVIKGVL
     FRIFIIWAIS SWFRRGPAPQ DQAGPGGAPR 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 ETNPYLLALT
     IIVSIVHSVF EFLAFKNDIQ FWNSRQSLEG LSVRSVFFGV FQSFVVLLYI LDNETNFVVQ
     VSVFIGVLID LWKITKVMDV RLDREHRVAG IFPRLSFKDK STYIESSTKV YDDMAFRYLS
     WILFPLLGCY AVYSLLYLEH KGWYSWVLSM LYGFLLTFGF ITMTPQLFIN YKLKSVAHLP
     WRMLTYKALN TFIDDLFAFV IKMPVMYRIG CLRDDVVFFI YLYQRWIYRV DPTRVNEFGM
     SGEDPTAAAP VAEVPTAAGA LTPTPAPTTT TATREEASTS LPTKPTQGAS SASEPQEAPP
     KPAEDKKKD
//