TX264_HUMAN
ID TX264_HUMAN Reviewed; 313 AA.
AC Q9Y6I9; B3KN87; Q9UKD7;
DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Testis-expressed protein 264 {ECO:0000305};
DE AltName: Full=Putative secreted protein Zsig11 {ECO:0000303|Ref.1};
GN Name=TEX264 {ECO:0000303|PubMed:31006537, ECO:0000303|PubMed:31006538,
GN ECO:0000312|HGNC:HGNC:30247}; Synonyms=ZSIG11 {ECO:0000303|Ref.1};
GN ORFNames=UNQ337/PRO536;
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].
RA Sheppard P., Sexson S., Jelinek L., Whitmore T., Grant F., O'Hara P.J.;
RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 212-313.
RC TISSUE=Brain;
RA Deng Y.C., Yao L.B., Su C.Z., Lui X.P., Nie X.Y., Wang J.C., Zhang X.G.,
RA Yang M., Ji S.P., Li F.Y., Han J., Han Y.H., He P.;
RT "New sequences cloned from adult brain cDNA library.";
RL Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION BY 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 [8]
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-244, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-239 AND SER-244, AND
RP IDENTIFICATION BY 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 [11]
RP INTERACTION WITH MAP1LC3A; MAP1LC3B; GABARAP AND GABARAPL1, SUBCELLULAR
RP LOCATION, TOPOLOGY, FUNCTION, DOMAIN, AND MUTAGENESIS OF PHE-273 AND
RP LEU-276.
RX PubMed=31006538; DOI=10.1016/j.molcel.2019.03.033;
RA Chino H., Hatta T., Natsume T., Mizushima N.;
RT "Intrinsically disordered protein TEX264 mediates ER-phagy.";
RL Mol. Cell 0:0-0(2019).
RN [12]
RP INTERACTION WITH MAP1LC3A; MAP1LC3B AND GABARAPL1, SUBCELLULAR LOCATION,
RP TOPOLOGY, FUNCTION, DOMAIN, AND MUTAGENESIS OF PHE-273.
RX PubMed=31006537; DOI=10.1016/j.molcel.2019.03.034;
RA An H., Ordureau A., Paulo J.A., Shoemaker C.J., Denic V., Harper J.W.;
RT "TEX264 is an endoplasmic reticulum-resident ATG8-interacting protein
RT critical for ER remodeling during nutrient stress.";
RL Mol. Cell 0:0-0(2019).
RN [13]
RP FUNCTION, INTERACTION WITH VCP, AND SUBCELLULAR LOCATION.
RX PubMed=32152270; DOI=10.1038/s41467-020-15000-w;
RA Fielden J., Wiseman K., Torrecilla I., Li S., Hume S., Chiang S.C.,
RA Ruggiano A., Narayan Singh A., Freire R., Hassanieh S., Domingo E.,
RA Vendrell I., Fischer R., Kessler B.M., Maughan T.S., El-Khamisy S.F.,
RA Ramadan K.;
RT "TEX264 coordinates p97- and SPRTN-mediated resolution of topoisomerase 1-
RT DNA adducts.";
RL Nat. Commun. 11:1274-1274(2020).
CC -!- FUNCTION: Major reticulophagy (also called ER-phagy) receptor that acts
CC independently of other candidate reticulophagy receptors to remodel
CC subdomains of the endoplasmic reticulum into autophagosomes upon
CC nutrient stress, which then fuse with lysosomes for endoplasmic
CC reticulum turnover (PubMed:31006538, PubMed:31006537). The ATG8-
CC containing isolation membrane (IM) cradles a tubular segment of TEX264-
CC positive ER near a three-way junction, allowing the formation of a
CC synapse of 2 juxtaposed membranes with trans interaction between the
CC TEX264 and ATG8 proteins (PubMed:31006537). Expansion of the IM would
CC extend the capture of ER, possibly through a 'zipper-like' process
CC involving continued trans TEX264-ATG8 interactions, until poorly
CC understood mechanisms lead to the fission of relevant membranes and,
CC ultimately, autophagosomal membrane closure (PubMed:31006537). Also
CC involved in the repair of covalent DNA-protein cross-links (DPCs)
CC during DNA synthesis: acts by bridging VCP/p97 to covalent DNA-protein
CC cross-links (DPCs) and initiating resolution of DPCs by SPRTN
CC (PubMed:32152270). {ECO:0000269|PubMed:31006537,
CC ECO:0000269|PubMed:31006538, ECO:0000269|PubMed:32152270}.
CC -!- SUBUNIT: Interacts (via the LIR motif) with ATG8 family proteins
CC MAP1LC3A, MAP1LC3B, GABARAP and GABARAPL1 (PubMed:31006537,
CC PubMed:31006538). Interacts with VCP/p97; bridging VCP/p97 to covalent
CC DNA-protein cross-links (DPCs) (PubMed:32152270). Interacts with TOP1
CC (when sumoylated) (PubMed:32152270). {ECO:0000269|PubMed:31006537,
CC ECO:0000269|PubMed:31006538, ECO:0000269|PubMed:32152270}.
CC -!- INTERACTION:
CC Q9Y6I9; Q86Y34: ADGRG3; NbExp=3; IntAct=EBI-10329860, EBI-17979264;
CC Q9Y6I9; Q3SXY8: ARL13B; NbExp=3; IntAct=EBI-10329860, EBI-11343438;
CC Q9Y6I9; Q9HA82: CERS4; NbExp=3; IntAct=EBI-10329860, EBI-2622997;
CC Q9Y6I9; P57739: CLDN2; NbExp=3; IntAct=EBI-10329860, EBI-751440;
CC Q9Y6I9; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-10329860, EBI-6165897;
CC Q9Y6I9; O75208: COQ9; NbExp=3; IntAct=EBI-10329860, EBI-724524;
CC Q9Y6I9; Q96BA8: CREB3L1; NbExp=3; IntAct=EBI-10329860, EBI-6942903;
CC Q9Y6I9; P54849: EMP1; NbExp=3; IntAct=EBI-10329860, EBI-4319440;
CC Q9Y6I9; Q5JX71: FAM209A; NbExp=3; IntAct=EBI-10329860, EBI-18304435;
CC Q9Y6I9; O15552: FFAR2; NbExp=3; IntAct=EBI-10329860, EBI-2833872;
CC Q9Y6I9; O14843: FFAR3; NbExp=3; IntAct=EBI-10329860, EBI-17762181;
CC Q9Y6I9; P60520: GABARAPL2; NbExp=3; IntAct=EBI-10329860, EBI-720116;
CC Q9Y6I9; P08034: GJB1; NbExp=3; IntAct=EBI-10329860, EBI-17565645;
CC Q9Y6I9; Q8TDT2: GPR152; NbExp=3; IntAct=EBI-10329860, EBI-13345167;
CC Q9Y6I9; O15529: GPR42; NbExp=3; IntAct=EBI-10329860, EBI-18076404;
CC Q9Y6I9; Q7Z7J7: LHFPL4; NbExp=3; IntAct=EBI-10329860, EBI-18016128;
CC Q9Y6I9; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-10329860, EBI-2820517;
CC Q9Y6I9; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-10329860, EBI-11956541;
CC Q9Y6I9; Q96HJ5: MS4A3; NbExp=4; IntAct=EBI-10329860, EBI-12806656;
CC Q9Y6I9; P35372-10: OPRM1; NbExp=3; IntAct=EBI-10329860, EBI-12807478;
CC Q9Y6I9; Q12908: SLC10A2; NbExp=3; IntAct=EBI-10329860, EBI-18114847;
CC Q9Y6I9; O95436-2: SLC34A2; NbExp=3; IntAct=EBI-10329860, EBI-12811757;
CC Q9Y6I9; Q9BZL3: SMIM3; NbExp=3; IntAct=EBI-10329860, EBI-741850;
CC Q9Y6I9; Q96CE8: TM4SF18; NbExp=3; IntAct=EBI-10329860, EBI-13351685;
CC Q9Y6I9; Q9BSE2: TMEM79; NbExp=8; IntAct=EBI-10329860, EBI-8649725;
CC Q9Y6I9; O95859: TSPAN12; NbExp=3; IntAct=EBI-10329860, EBI-2466403;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}; Single-pass
CC type III membrane protein {ECO:0000269|PubMed:31006537,
CC ECO:0000269|PubMed:31006538}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}. Cytoplasm,
CC cytosol {ECO:0000269|PubMed:32152270}. Nucleus
CC {ECO:0000269|PubMed:32152270}. Chromosome
CC {ECO:0000269|PubMed:32152270}. Note=Is trafficked from tubular ER to
CC growing autophagosomes via its cytosolic LIR motif (PubMed:31006537).
CC Also found in the cytosol, nucleus and chromatin (PubMed:32152270). In
CC response to formation of covalent DNA-protein cross-links (DPCs),
CC localizes to the nuclear periphery, and associates with DNA replication
CC forks (PubMed:32152270). {ECO:0000269|PubMed:31006537,
CC ECO:0000269|PubMed:32152270}.
CC -!- DOMAIN: The LIR motif in the cytosol-facing C-terminal region is
CC involved in the interaction with ATG8 proteins.
CC {ECO:0000269|PubMed:31006537, ECO:0000269|PubMed:31006538}.
CC -!- DOMAIN: The disordered region is required for autophagosome binding and
CC reticulophagy, probably via bridging the long distance between
CC endoplasmic reticulum and autophagosome membranes, because ribosomes
CC exist on endoplasmic reticulum membranes that attach to autophagic
CC membranes. {ECO:0000269|PubMed:31006538}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD52584.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF072733; AAD22397.1; -; mRNA.
DR EMBL; AY358972; AAQ89331.1; -; mRNA.
DR EMBL; AK023997; BAG51249.1; -; mRNA.
DR EMBL; CH471055; EAW65146.1; -; Genomic_DNA.
DR EMBL; BC008742; AAH08742.1; -; mRNA.
DR EMBL; AF172327; AAD52584.1; ALT_INIT; mRNA.
DR CCDS; CCDS2833.1; -.
DR RefSeq; NP_001123356.1; NM_001129884.2.
DR RefSeq; NP_001230654.1; NM_001243725.1.
DR RefSeq; NP_001230655.1; NM_001243726.1.
DR RefSeq; NP_001230656.1; NM_001243727.2.
DR RefSeq; NP_001265124.1; NM_001278195.1.
DR RefSeq; NP_057010.1; NM_015926.5.
DR RefSeq; XP_006713258.1; XM_006713195.3.
DR RefSeq; XP_006713260.1; XM_006713197.3.
DR RefSeq; XP_011532107.1; XM_011533805.2.
DR PDB; 7VED; X-ray; 2.02 A; A/B=271-281.
DR PDBsum; 7VED; -.
DR AlphaFoldDB; Q9Y6I9; -.
DR BioGRID; 119503; 189.
DR IntAct; Q9Y6I9; 55.
DR MINT; Q9Y6I9; -.
DR STRING; 9606.ENSP00000396628; -.
DR ChEMBL; CHEMBL4295994; -.
DR GlyGen; Q9Y6I9; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y6I9; -.
DR PhosphoSitePlus; Q9Y6I9; -.
DR SwissPalm; Q9Y6I9; -.
DR BioMuta; TEX264; -.
DR DMDM; 22002027; -.
DR EPD; Q9Y6I9; -.
DR jPOST; Q9Y6I9; -.
DR MassIVE; Q9Y6I9; -.
DR MaxQB; Q9Y6I9; -.
DR PaxDb; Q9Y6I9; -.
DR PeptideAtlas; Q9Y6I9; -.
DR PRIDE; Q9Y6I9; -.
DR ProteomicsDB; 86698; -.
DR TopDownProteomics; Q9Y6I9; -.
DR Antibodypedia; 2567; 89 antibodies from 18 providers.
DR DNASU; 51368; -.
DR Ensembl; ENST00000341333.10; ENSP00000340969.5; ENSG00000164081.13.
DR Ensembl; ENST00000395057.5; ENSP00000378497.1; ENSG00000164081.13.
DR Ensembl; ENST00000415259.5; ENSP00000396628.1; ENSG00000164081.13.
DR Ensembl; ENST00000416589.5; ENSP00000398802.1; ENSG00000164081.13.
DR Ensembl; ENST00000457573.5; ENSP00000408186.1; ENSG00000164081.13.
DR Ensembl; ENST00000611400.4; ENSP00000477946.1; ENSG00000164081.13.
DR GeneID; 51368; -.
DR KEGG; hsa:51368; -.
DR MANE-Select; ENST00000341333.10; ENSP00000340969.5; NM_015926.6; NP_057010.1.
DR UCSC; uc003dbk.6; human.
DR CTD; 51368; -.
DR GeneCards; TEX264; -.
DR HGNC; HGNC:30247; TEX264.
DR HPA; ENSG00000164081; Low tissue specificity.
DR neXtProt; NX_Q9Y6I9; -.
DR OpenTargets; ENSG00000164081; -.
DR PharmGKB; PA134875244; -.
DR VEuPathDB; HostDB:ENSG00000164081; -.
DR eggNOG; ENOG502S3D1; Eukaryota.
DR GeneTree; ENSGT00390000016901; -.
DR HOGENOM; CLU_077435_0_0_1; -.
DR InParanoid; Q9Y6I9; -.
DR OMA; QIKRFQK; -.
DR OrthoDB; 1561788at2759; -.
DR PhylomeDB; Q9Y6I9; -.
DR TreeFam; TF328465; -.
DR PathwayCommons; Q9Y6I9; -.
DR Reactome; R-HSA-114608; Platelet degranulation.
DR SignaLink; Q9Y6I9; -.
DR BioGRID-ORCS; 51368; 16 hits in 1081 CRISPR screens.
DR ChiTaRS; TEX264; human.
DR GenomeRNAi; 51368; -.
DR Pharos; Q9Y6I9; Tbio.
DR PRO; PR:Q9Y6I9; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y6I9; protein.
DR Bgee; ENSG00000164081; Expressed in left testis and 179 other tissues.
DR ExpressionAtlas; Q9Y6I9; baseline and differential.
DR Genevisible; Q9Y6I9; HS.
DR GO; GO:0000421; C:autophagosome membrane; IDA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; IDA:GO_Central.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031093; C:platelet alpha granule lumen; TAS:Reactome.
DR GO; GO:0005657; C:replication fork; IDA:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; IDA:MGI.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; IDA:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; IDA:MGI.
DR Gene3D; 3.20.80.10; -; 1.
DR InterPro; IPR011256; Reg_factor_effector_dom_sf.
DR SUPFAM; SSF55136; SSF55136; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Autophagy; Chromosome; Cytoplasm; Cytoplasmic vesicle;
KW DNA damage; DNA repair; Endoplasmic reticulum; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT CHAIN 1..313
FT /note="Testis-expressed protein 264"
FT /id="PRO_0000022601"
FT TOPO_DOM 1..6
FT /note="Lumenal"
FT /evidence="ECO:0000269|PubMed:31006538"
FT TRANSMEM 7..31
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 32..313
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:31006538"
FT REGION 193..313
FT /note="Disordered"
FT /evidence="ECO:0000305|PubMed:31006538"
FT MOTIF 273..276
FT /note="LIR motif"
FT /evidence="ECO:0000305|PubMed:31006538"
FT COMPBIAS 215..246
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 292
FT /note="G -> E (in dbSNP:rs11553574)"
FT /id="VAR_061718"
FT MUTAGEN 273
FT /note="F->A: Completely abolishes the interaction with
FT LC3B."
FT /evidence="ECO:0000269|PubMed:31006537,
FT ECO:0000269|PubMed:31006538"
FT MUTAGEN 276
FT /note="L->A: Completely abolishes the interaction with
FT LC3B."
FT /evidence="ECO:0000269|PubMed:31006538"
SQ SEQUENCE 313 AA; 34189 MW; 6159011A220F1C67 CRC64;
MSDLLLLGLI GGLTLLLLLT LLAFAGYSGL LAGVEVSAGS PPIRNVTVAY KFHMGLYGET
GRLFTESCSI SPKLRSIAVY YDNPHMVPPD KCRCAVGSIL SEGEESPSPE LIDLYQKFGF
KVFSFPAPSH VVTATFPYTT ILSIWLATRR VHPALDTYIK ERKLCAYPRL EIYQEDQIHF
MCPLARQGDF YVPEMKETEW KWRGLVEAID TQVDGTGADT MSDTSSVSLE VSPGSRETSA
ATLSPGASSR GWDDGDTRSE HSYSESGASG SSFEELDLEG EGPLGESRLD PGTEPLGTTK
WLWEPTAPEK GKE
