TX264_MOUSE
ID TX264_MOUSE Reviewed; 309 AA.
AC E9Q137; Q3TXY2; Q99LS5; Q9D7D9;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Testis-expressed protein 264 homolog {ECO:0000305};
GN Name=Tex264 {ECO:0000312|MGI:MGI:1096570};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J;
RC TISSUE=Tongue {ECO:0000312|EMBL:BAB26219.1}, and
RC Visual cortex {ECO:0000312|EMBL:BAE34782.1};
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II {ECO:0000312|EMBL:AAH02248.1}, and
RC FVB/N {ECO:0000312|EMBL:AAH06608.1};
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).
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. The ATG8-containing isolation membrane (IM) cradles
CC a tubular segment of TEX264-positive ER near a three-way junction,
CC allowing the formation of a synapse of 2 juxtaposed membranes with
CC trans interaction between the TEX264 and ATG8 proteins. Expansion of
CC the IM would extend the capture of ER, possibly through a 'zipper-like'
CC process involving continued trans TEX264-ATG8 interactions, until
CC poorly understood mechanisms lead to the fission of relevant membranes
CC and, ultimately, autophagosomal membrane closure. Also involved in the
CC repair of covalent DNA-protein cross-links (DPCs) during DNA synthesis:
CC acts by bridging VCP/p97 to covalent DNA-protein cross-links (DPCs) and
CC initiating resolution of DPCs by SPRTN. {ECO:0000250|UniProtKB:Q9Y6I9}.
CC -!- SUBUNIT: Interacts (via the LIR motif) with ATG8 family proteins
CC MAP1LC3A, MAP1LC3B, GABARAP and GABARAPL1. Interacts with VCP/p97;
CC bridging VCP/p97 to covalent DNA-protein cross-links (DPCs). Interacts
CC with TOP1 (when sumoylated). {ECO:0000250|UniProtKB:Q9Y6I9}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000250|UniProtKB:Q9Y6I9}; Single-pass type III membrane protein
CC {ECO:0000250|UniProtKB:Q9Y6I9}. Cytoplasmic vesicle, autophagosome
CC {ECO:0000250|UniProtKB:Q9Y6I9}. Cytoplasm, cytosol
CC {ECO:0000250|UniProtKB:Q9Y6I9}. Nucleus {ECO:0000250|UniProtKB:Q9Y6I9}.
CC Chromosome {ECO:0000250|UniProtKB:Q9Y6I9}. Note=Is trafficked from
CC tubular ER to growing autophagosomes via its cytosolic LIR motif. Also
CC found in the cytosol, nucleus and chromatin. In response to formation
CC of covalent DNA-protein cross-links (DPCs), localizes to the nuclear
CC periphery, and associates with DNA replication forks.
CC {ECO:0000250|UniProtKB:Q9Y6I9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=E9Q137-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9Q137-2; Sequence=VSP_060780;
CC -!- DOMAIN: The LIR motif in the cytosol-facing C-terminal region is
CC involved in the interaction with ATG8 proteins.
CC {ECO:0000250|UniProtKB:Q9Y6I9}.
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:0000250|UniProtKB:Q9Y6I9}.
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; AK009326; BAB26219.1; -; mRNA.
DR EMBL; AK159046; BAE34782.1; -; mRNA.
DR EMBL; AC125188; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC002248; AAH02248.1; -; mRNA.
DR EMBL; BC006608; AAH06608.1; -; mRNA.
DR CCDS; CCDS23483.1; -. [E9Q137-1]
DR RefSeq; NP_001075123.1; NM_001081654.2. [E9Q137-1]
DR RefSeq; NP_001273427.1; NM_001286498.1. [E9Q137-1]
DR RefSeq; NP_035703.2; NM_011573.3. [E9Q137-1]
DR AlphaFoldDB; E9Q137; -.
DR STRING; 10090.ENSMUSP00000132247; -.
DR PhosphoSitePlus; E9Q137; -.
DR EPD; E9Q137; -.
DR jPOST; E9Q137; -.
DR MaxQB; E9Q137; -.
DR PaxDb; E9Q137; -.
DR PeptideAtlas; E9Q137; -.
DR PRIDE; E9Q137; -.
DR ProteomicsDB; 342775; -. [E9Q137-1]
DR Antibodypedia; 2567; 89 antibodies from 18 providers.
DR Ensembl; ENSMUST00000046735; ENSMUSP00000044654; ENSMUSG00000040813. [E9Q137-1]
DR Ensembl; ENSMUST00000163441; ENSMUSP00000132247; ENSMUSG00000040813. [E9Q137-1]
DR Ensembl; ENSMUST00000169068; ENSMUSP00000133194; ENSMUSG00000040813. [E9Q137-1]
DR GeneID; 21767; -.
DR KEGG; mmu:21767; -.
DR UCSC; uc009rkk.2; mouse. [E9Q137-1]
DR CTD; 51368; -.
DR MGI; MGI:1096570; Tex264.
DR VEuPathDB; HostDB:ENSMUSG00000040813; -.
DR eggNOG; ENOG502S3D1; Eukaryota.
DR GeneTree; ENSGT00390000016901; -.
DR HOGENOM; CLU_077435_0_0_1; -.
DR InParanoid; E9Q137; -.
DR OMA; QIKRFQK; -.
DR OrthoDB; 1561788at2759; -.
DR PhylomeDB; E9Q137; -.
DR TreeFam; TF328465; -.
DR Reactome; R-MMU-114608; Platelet degranulation.
DR BioGRID-ORCS; 21767; 2 hits in 72 CRISPR screens.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; E9Q137; protein.
DR Bgee; ENSMUSG00000040813; Expressed in placenta labyrinth and 248 other tissues.
DR GO; GO:0000421; C:autophagosome membrane; IDA:MGI.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005657; C:replication fork; ISS:UniProtKB.
DR GO; GO:0038023; F:signaling receptor activity; ISO:MGI.
DR GO; GO:0106300; P:protein-DNA covalent cross-linking repair; ISS:UniProtKB.
DR GO; GO:0061709; P:reticulophagy; ISO:MGI.
DR Gene3D; 3.20.80.10; -; 1.
DR InterPro; IPR011256; Reg_factor_effector_dom_sf.
DR SUPFAM; SSF55136; SSF55136; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Autophagy; Chromosome; Cytoplasm;
KW Cytoplasmic vesicle; DNA damage; DNA repair; Endoplasmic reticulum;
KW Membrane; Nucleus; Phosphoprotein; Reference proteome; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..309
FT /note="Testis-expressed protein 264 homolog"
FT /id="PRO_0000451419"
FT TOPO_DOM 1..3
FT /note="Lumenal"
FT /evidence="ECO:0000305"
FT TRANSMEM 4..24
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 25..309
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 193..309
FT /note="Disordered"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6I9"
FT MOTIF 272..275
FT /note="LIR motif"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6I9"
FT COMPBIAS 209..245
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 238
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6I9"
FT MOD_RES 243
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6I9"
FT VAR_SEQ 162..199
FT /note="Missing (in isoform 2)"
FT /id="VSP_060780"
FT CONFLICT 56
FT /note="S -> V (in Ref. 1; BAB26219)"
FT /evidence="ECO:0000305"
FT CONFLICT 174
FT /note="H -> Q (in Ref. 3; AAH02248/AAH06608)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 309 AA; 33590 MW; 0CAA2F9C6D539244 CRC64;
MPDLLLLGLI GALTLLLLLT LLAFAGYSGL LTGVTVSAGS PPIRNITVAY KFHVGSYGDT
GHLFTESCSI SPKLRSIAVY YDNPHTVPPE KCRCAVGSIL SEGEESPSPE LIHLYQKFGF
KIFSFPAPSH VVIATFPYTT PISIWLAARR VHPALDTYIK ERKLCAHPRL EIYHQDKIHF
MCPLARQGDF YVPEVKETER KCRELAEATD TQTDGTGADT SDASSVSLDV RPGSRETSAT
TLSPGAGNRG WDDGDNRSEH SYSESGASGS SFEELDLEGE GPLGEPRLNP EAKLLGPPRE
LSTPERGEE
