TRAM1_HUMAN
ID TRAM1_HUMAN Reviewed; 374 AA.
AC Q15629; B4E0K2;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 179.
DE RecName: Full=Translocating chain-associated membrane protein 1 {ECO:0000303|PubMed:19121997};
DE Short=Protein TRAM1 {ECO:0000303|PubMed:19121997};
GN Name=TRAM1 {ECO:0000312|HGNC:HGNC:20568};
GN Synonyms=TRAM {ECO:0000303|PubMed:8616892};
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 [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, AND
RP GLYCOSYLATION.
RX PubMed=1315422; DOI=10.1038/357047a0;
RA Goerlich D., Hartmann E., Prehn S., Rapoport T.A.;
RT "A protein of the endoplasmic reticulum involved early in polypeptide
RT translocation.";
RL Nature 357:47-52(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
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 GENOMIC DNA].
RX PubMed=16421571; DOI=10.1038/nature04406;
RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M.,
RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L.,
RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S.,
RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A.,
RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III,
RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K.,
RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B.,
RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K.,
RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L.,
RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G.,
RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W.,
RA Platzer M., Shimizu N., Lander E.S.;
RT "DNA sequence and analysis of human chromosome 8.";
RL Nature 439:331-335(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Kidney;
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 [5]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=8616892; DOI=10.1016/s0092-8674(00)81115-0;
RA Do H., Falcone D., Lin J., Andrews D.W., Johnson A.E.;
RT "The cotranslational integration of membrane proteins into the phospholipid
RT bilayer is a multistep process.";
RL Cell 85:369-378(1996).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=9506517; DOI=10.1016/s0092-8674(00)81130-7;
RA Hegde R.S., Voigt S., Rapoport T.A., Lingappa V.R.;
RT "TRAM regulates the exposure of nascent secretory proteins to the cytosol
RT during translocation into the endoplasmic reticulum.";
RL Cell 92:621-631(1998).
RN [7]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=12475939; DOI=10.1091/mbc.e02-04-0198;
RA Meacock S.L., Lecomte F.J., Crawshaw S.G., High S.;
RT "Different transmembrane domains associate with distinct endoplasmic
RT reticulum components during membrane integration of a polytopic protein.";
RL Mol. Biol. Cell 13:4114-4129(2002).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP FUNCTION (MICROBIAL INFECTION), INTERACTION WITH SEC61B AND DERL1,
RP INTERACTION WITH HHV-5 PROTEINS US2 AND US11 (MICROBIAL INFECTION), AND
RP GLYCOSYLATION.
RX PubMed=19121997; DOI=10.1074/jbc.m807568200;
RA Oresic K., Ng C.L., Tortorella D.;
RT "TRAM1 participates in human cytomegalovirus US2- and US11-mediated
RT dislocation of an endoplasmic reticulum membrane glycoprotein.";
RL J. Biol. Chem. 284:5905-5914(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [13]
RP FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION BY ER STRESS.
RX PubMed=20430023; DOI=10.1016/j.yexcr.2010.04.010;
RA Ng C.L., Oresic K., Tortorella D.;
RT "TRAM1 is involved in disposal of ER membrane degradation substrates.";
RL Exp. Cell Res. 316:2113-2122(2010).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [15]
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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [17]
RP FUNCTION.
RX PubMed=32013668; DOI=10.1080/19336950.2020.1724759;
RA Klein M.C., Lerner M., Nguyen D., Pfeffer S., Dudek J., Foerster F.,
RA Helms V., Lang S., Zimmermann R.;
RT "TRAM1 protein may support ER protein import by modulating the phospholipid
RT bilayer near the lateral gate of the Sec61-channel.";
RL Channels 14:28-44(2020).
CC -!- FUNCTION: Involved in the translocation of nascent protein chains into
CC or through the endoplasmic reticulum (ER) membrane by facilitating the
CC proper chain positioning at the SEC61 channel (PubMed:1315422,
CC PubMed:8616892, PubMed:9506517, PubMed:12475939, PubMed:32013668).
CC Regulates the exposure of nascent secretory protein chain to the
CC cytosol during translocation into the ER (PubMed:9506517). May affect
CC the phospholipid bilayer in the vicinity of the lateral gate of the
CC SEC61 channel, thereby facilitating ER protein transport
CC (PubMed:32013668). Intimately associates with transmembrane (TM) domain
CC of nascent membrane proteins during the entire integration process into
CC the ER membrane (PubMed:8616892). Associates with the second TM domain
CC of G-protein-coupled receptor opsin/OPSD nascent chain in the ER
CC membrane, which may facilitate its integration into the membrane
CC (PubMed:12475939). Under conditions of ER stress, participates in the
CC disposal of misfolded ER membrane proteins during the unfolded protein
CC response (UPR), an integrated stress response (ISR) pathway, by
CC selectively retrotranslocating misfolded ER-membrane proteins from the
CC ER into the cytosol where they are ubiquitinated and degraded by the
CC proteasome (PubMed:20430023). {ECO:0000269|PubMed:12475939,
CC ECO:0000269|PubMed:1315422, ECO:0000269|PubMed:20430023,
CC ECO:0000269|PubMed:32013668, ECO:0000269|PubMed:8616892,
CC ECO:0000269|PubMed:9506517, ECO:0000303|PubMed:32013668}.
CC -!- FUNCTION: (Microbial infection) In case of cytomegalovirus infection,
CC participates in US2- and US11-mediated ER-to-cytosol retrotranslocation
CC and subsequent degradation of major histocompatibility complex (MHC)
CC class I heavy chains, thereby decreasing the immune detection by
CC cytotoxic T-cells. {ECO:0000269|PubMed:19121997}.
CC -!- SUBUNIT: Interacts with SEC61B (PubMed:19121997). May interact with
CC Derlin-1/DERL1 (PubMed:19121997). {ECO:0000269|PubMed:19121997}.
CC -!- SUBUNIT: (Microbial infection) Interacts with human
CC cytomegalovirus/HHV-5 proteins US2 and US11.
CC {ECO:0000269|PubMed:19121997}.
CC -!- INTERACTION:
CC Q15629; P51572: BCAP31; NbExp=5; IntAct=EBI-1788852, EBI-77683;
CC Q15629; Q02747: GUCA2A; NbExp=3; IntAct=EBI-1788852, EBI-12244272;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:12475939, ECO:0000269|PubMed:1315422,
CC ECO:0000269|PubMed:20430023, ECO:0000269|PubMed:8616892,
CC ECO:0000269|PubMed:9506517}; Multi-pass membrane protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q15629-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q15629-2; Sequence=VSP_056213;
CC -!- INDUCTION: Up-regulated upon endoplasmic reticulum stress.
CC {ECO:0000269|PubMed:20430023}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:1315422,
CC ECO:0000269|PubMed:19121997}.
CC -!- SIMILARITY: Belongs to the TRAM family. {ECO:0000305}.
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DR EMBL; X63679; CAA45218.1; -; mRNA.
DR EMBL; AK303411; BAG64464.1; -; mRNA.
DR EMBL; AC022731; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC120194; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000687; AAH00687.1; -; mRNA.
DR EMBL; BC037738; AAH37738.1; -; mRNA.
DR CCDS; CCDS6207.1; -. [Q15629-1]
DR PIR; S30034; S30034.
DR RefSeq; NP_001304733.1; NM_001317804.1. [Q15629-2]
DR RefSeq; NP_001304734.1; NM_001317805.1.
DR RefSeq; NP_055109.1; NM_014294.5. [Q15629-1]
DR AlphaFoldDB; Q15629; -.
DR BioGRID; 117032; 62.
DR DIP; DIP-45978N; -.
DR IntAct; Q15629; 30.
DR MINT; Q15629; -.
DR STRING; 9606.ENSP00000262213; -.
DR TCDB; 9.B.311.2.1; the 6-7 tms tram-lag (tram-lag) family.
DR GlyConnect; 1838; 1 N-Linked glycan (1 site).
DR GlyGen; Q15629; 2 sites, 1 N-linked glycan (1 site).
DR iPTMnet; Q15629; -.
DR PhosphoSitePlus; Q15629; -.
DR SwissPalm; Q15629; -.
DR BioMuta; TRAM1; -.
DR DMDM; 18202507; -.
DR EPD; Q15629; -.
DR jPOST; Q15629; -.
DR MassIVE; Q15629; -.
DR MaxQB; Q15629; -.
DR PaxDb; Q15629; -.
DR PeptideAtlas; Q15629; -.
DR PRIDE; Q15629; -.
DR ProteomicsDB; 5680; -.
DR ProteomicsDB; 60664; -. [Q15629-1]
DR TopDownProteomics; Q15629-1; -. [Q15629-1]
DR Antibodypedia; 12213; 152 antibodies from 28 providers.
DR DNASU; 23471; -.
DR Ensembl; ENST00000262213.7; ENSP00000262213.2; ENSG00000067167.8. [Q15629-1]
DR GeneID; 23471; -.
DR KEGG; hsa:23471; -.
DR MANE-Select; ENST00000262213.7; ENSP00000262213.2; NM_014294.6; NP_055109.1.
DR CTD; 23471; -.
DR DisGeNET; 23471; -.
DR GeneCards; TRAM1; -.
DR HGNC; HGNC:20568; TRAM1.
DR HPA; ENSG00000067167; Low tissue specificity.
DR MIM; 605190; gene.
DR neXtProt; NX_Q15629; -.
DR OpenTargets; ENSG00000067167; -.
DR PharmGKB; PA134955644; -.
DR VEuPathDB; HostDB:ENSG00000067167; -.
DR eggNOG; KOG1608; Eukaryota.
DR GeneTree; ENSGT00510000046470; -.
DR HOGENOM; CLU_062830_0_0_1; -.
DR InParanoid; Q15629; -.
DR OMA; YFHHGIK; -.
DR PhylomeDB; Q15629; -.
DR TreeFam; TF314319; -.
DR PathwayCommons; Q15629; -.
DR Reactome; R-HSA-1799339; SRP-dependent cotranslational protein targeting to membrane.
DR SignaLink; Q15629; -.
DR BioGRID-ORCS; 23471; 17 hits in 1077 CRISPR screens.
DR ChiTaRS; TRAM1; human.
DR GenomeRNAi; 23471; -.
DR Pharos; Q15629; Tbio.
DR PRO; PR:Q15629; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q15629; protein.
DR Bgee; ENSG00000067167; Expressed in choroid plexus epithelium and 214 other tissues.
DR ExpressionAtlas; Q15629; baseline and differential.
DR Genevisible; Q15629; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:ParkinsonsUK-UCL.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; TAS:ProtInc.
DR GO; GO:0038023; F:signaling receptor activity; TAS:ProtInc.
DR GO; GO:0006613; P:cotranslational protein targeting to membrane; IDA:UniProtKB.
DR GO; GO:0045048; P:protein insertion into ER membrane; IDA:UniProtKB.
DR GO; GO:0006986; P:response to unfolded protein; IMP:UniProtKB.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IEA:InterPro.
DR InterPro; IPR006634; TLC-dom.
DR InterPro; IPR013599; TRAM1.
DR InterPro; IPR016447; Translocation_assoc_membrane.
DR PANTHER; PTHR12371; PTHR12371; 1.
DR Pfam; PF08390; TRAM1; 1.
DR Pfam; PF03798; TRAM_LAG1_CLN8; 1.
DR PIRSF; PIRSF005449; Translocation_assoc_membrane; 1.
DR SMART; SM00724; TLC; 1.
DR PROSITE; PS50922; TLC; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein;
KW Host-virus interaction; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Translocation; Transmembrane; Transmembrane helix;
KW Transport; Unfolded protein response.
FT CHAIN 1..374
FT /note="Translocating chain-associated membrane protein 1"
FT /id="PRO_0000185530"
FT TOPO_DOM 1..29
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 51..76
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 77..97
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 98..121
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 122..142
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 143..159
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 160..180
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 181..192
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 214..217
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 239..251
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 252..272
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 273..297
FT /note="Lumenal"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 319..374
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q91V04"
FT DOMAIN 117..326
FT /note="TLC"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00205"
FT REGION 334..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 365
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT CARBOHYD 56
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..31
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056213"
SQ SEQUENCE 374 AA; 43072 MW; 9232ADA33DE20076 CRC64;
MAIRKKSTKS PPVLSHEFVL QNHADIVSCV AMVFLLGLMF EITAKASIIF VTLQYNVTLP
ATEEQATESV SLYYYGIKDL ATVFFYMLVA IIIHAVIQEY MLDKINRRMH FSKTKHSKFN
ESGQLSAFYL FACVWGTFIL ISENYISDPT ILWRAYPHNL MTFQMKFFYI SQLAYWLHAF
PELYFQKTKK EDIPRQLVYI GLYLFHIAGA YLLNLNHLGL VLLVLHYFVE FLFHISRLFY
FSNEKYQKGF SLWAVLFVLG RLLTLILSVL TVGFGLARAE NQKLDFSTGN FNVLAVRIAV
LASICVTQAF MMWKFINFQL RRWREHSAFQ APAVKKKPTV TKGRSSKKGT ENGVNGTLTS
NVADSPRNKK EKSS
