ID RETR3_HUMAN Reviewed; 466 AA. AC Q86VR2; B3KR75; DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 136. DE RecName: Full=Reticulophagy regulator 3; GN Name=RETREG3 {ECO:0000312|HGNC:HGNC:27258}; Synonyms=FAM134C; 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 [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Brain, and Tongue; 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16625196; DOI=10.1038/nature04689; RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.; RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the RT human lineage."; RL Nature 440:1045-1049(2006). RN [3] 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Brain; 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-260; THR-283; RP SER-285; THR-307; THR-310; SER-313; SER-320; SER-360 AND THR-440, AND RP IDENTIFICATION BY 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 [6] 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=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-258; SER-260; THR-307; RP SER-313; SER-320 AND THR-440, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [8] RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE RP ANALYSIS] AT THR-10; SER-258 AND SER-260, CLEAVAGE OF INITIATOR METHIONINE RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE RP 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 [9] 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 [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-26; SER-258; SER-260 AND RP SER-320, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [11] 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 [12] RP FUNCTION. RX PubMed=23939472; DOI=10.1016/j.gene.2013.08.006; RA Wang J.L., Tong C.W., Chang W.T., Huang A.M.; RT "Novel genes FAM134C, C3orf10 and ENOX1 are regulated by NRF-1 and RT differentially regulate neurite outgrowth in neuroblastoma cells and RT hippocampal neurons."; RL Gene 529:7-15(2013). RN [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-10 AND SER-320, AND RP IDENTIFICATION BY 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-307; THR-310; SER-313 AND RP SER-320, AND 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 [15] RP INTERACTION WITH MAP1LC3A; MAP1LC3B; GABARAP AND GABARAPL1, AND DOMAIN. RX PubMed=26040720; DOI=10.1038/nature14498; RA Khaminets A., Heinrich T., Mari M., Grumati P., Huebner A.K., Akutsu M., RA Liebmann L., Stolz A., Nietzsche S., Koch N., Mauthe M., Katona I., RA Qualmann B., Weis J., Reggiori F., Kurth I., Huebner C.A., Dikic I.; RT "Regulation of endoplasmic reticulum turnover by selective autophagy."; RL Nature 522:354-358(2015). RN [16] RP FUNCTION, INTERACTION WITH MAP1LC3A; MAP1LC3B; MAP1LC3C; GABARAP; RP GABARAPL1; GABARAPL2 AND CANX, SUBCELLULAR LOCATION, AND MUTAGENESIS OF RP 447-PHE--LEU-450. RX PubMed=34338405; DOI=10.15252/embr.202052289; RA Reggio A., Buonomo V., Berkane R., Bhaskara R.M., Tellechea M., Peluso I., RA Polishchuk E., Di Lorenzo G., Cirillo C., Esposito M., Hussain A., RA Huebner A.K., Huebner C.A., Settembre C., Hummer G., Grumati P., Stolz A.; RT "Role of FAM134 paralogues in endoplasmic reticulum remodeling, ER-phagy, RT and Collagen quality control."; RL EMBO Rep. 22:e52289-e52289(2021). RN [17] RP FUNCTION, INTERACTION WITH RTN4, SUBCELLULAR LOCATION, INDUCTION, TOPOLOGY, RP AND MUTAGENESIS OF 445-ASP--LEU-450. RX PubMed=33826365; DOI=10.1091/mbc.e20-06-0409; RA Kumar D., Lak B., Suntio T., Vihinen H., Belevich I., Viita T., Xiaonan L., RA Vartiainen A., Vartiainen M., Varjosalo M., Jokitalo E.; RT "RTN4B interacting protein FAM134C promotes ER membrane curvature and has a RT functional role in autophagy."; RL Mol. Biol. Cell 32:1158-1170(2021). CC -!- FUNCTION: Endoplasmic reticulum (ER)-anchored autophagy regulator which CC exists in an inactive state under basal conditions but is activated CC following cellular stress (PubMed:34338405). When activated, induces ER CC fragmentation and mediates ER delivery into lysosomes through CC sequestration into autophagosomes via interaction with ATG8 family CC proteins (PubMed:34338405). Promotes ER membrane curvature and ER CC tubulation required for subsequent ER fragmentation and engulfment into CC autophagosomes (PubMed:33826365). Required for collagen quality control CC in a LIR motif-dependent manner (By similarity). Mediates NRF1-enhanced CC neurite outgrowth (PubMed:26040720). {ECO:0000250|UniProtKB:Q9CQV4, CC ECO:0000269|PubMed:26040720, ECO:0000269|PubMed:33826365, CC ECO:0000269|PubMed:34338405}. CC -!- SUBUNIT: Interacts with ATG8 family modifier proteins MAP1LC3A, CC MAP1LC3B, MAP1LC3C, GABARAP, GABARAPL1 and GABARAPL2 (PubMed:26040720, CC PubMed:34338405). Interacts with CANX (PubMed:34338405). Interacts with CC RTN4 isoform B (PubMed:33826365). {ECO:0000269|PubMed:26040720, CC ECO:0000269|PubMed:33826365, ECO:0000269|PubMed:34338405}. CC -!- INTERACTION: CC Q86VR2; O95870: ABHD16A; NbExp=7; IntAct=EBI-10192441, EBI-348517; CC Q86VR2; Q9ULC5: ACSL5; NbExp=5; IntAct=EBI-10192441, EBI-2876927; CC Q86VR2; Q9NRZ5: AGPAT4; NbExp=3; IntAct=EBI-10192441, EBI-1754287; CC Q86VR2; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-10192441, EBI-11522760; CC Q86VR2; Q86W74-2: ANKRD46; NbExp=3; IntAct=EBI-10192441, EBI-12109402; CC Q86VR2; Q15041: ARL6IP1; NbExp=7; IntAct=EBI-10192441, EBI-714543; CC Q86VR2; O15145: ARPC3; NbExp=5; IntAct=EBI-10192441, EBI-351829; CC Q86VR2; P27449: ATP6V0C; NbExp=3; IntAct=EBI-10192441, EBI-721179; CC Q86VR2; O15155: BET1; NbExp=3; IntAct=EBI-10192441, EBI-749204; CC Q86VR2; Q12981: BNIP1; NbExp=3; IntAct=EBI-10192441, EBI-4402847; CC Q86VR2; Q8WVX3-2: C4orf3; NbExp=3; IntAct=EBI-10192441, EBI-12003442; CC Q86VR2; Q9P0B6: CCDC167; NbExp=3; IntAct=EBI-10192441, EBI-9083477; CC Q86VR2; Q8NHW4: CCL4L2; NbExp=3; IntAct=EBI-10192441, EBI-10271156; CC Q86VR2; O14735: CDIPT; NbExp=3; IntAct=EBI-10192441, EBI-358858; CC Q86VR2; Q92903: CDS1; NbExp=3; IntAct=EBI-10192441, EBI-13295305; CC Q86VR2; Q96MX0: CMTM3; NbExp=3; IntAct=EBI-10192441, EBI-7247651; CC Q86VR2; Q96DZ9-2: CMTM5; NbExp=3; IntAct=EBI-10192441, EBI-11522780; CC Q86VR2; Q96FZ5: CMTM7; NbExp=5; IntAct=EBI-10192441, EBI-2807956; CC Q86VR2; Q8N6G5: CSGALNACT2; NbExp=3; IntAct=EBI-10192441, EBI-10267100; CC Q86VR2; O43169: CYB5B; NbExp=3; IntAct=EBI-10192441, EBI-1058710; CC Q86VR2; P78329: CYP4F2; NbExp=3; IntAct=EBI-10192441, EBI-1752413; CC Q86VR2; Q9BUN8: DERL1; NbExp=3; IntAct=EBI-10192441, EBI-398977; CC Q86VR2; Q8N5I4: DHRSX; NbExp=3; IntAct=EBI-10192441, EBI-3923585; CC Q86VR2; Q9UKR5: ERG28; NbExp=3; IntAct=EBI-10192441, EBI-711490; CC Q86VR2; Q96IV6: FAXDC2; NbExp=3; IntAct=EBI-10192441, EBI-12142299; CC Q86VR2; Q96LL3: FIMP; NbExp=3; IntAct=EBI-10192441, EBI-12887376; CC Q86VR2; Q14318: FKBP8; NbExp=3; IntAct=EBI-10192441, EBI-724839; CC Q86VR2; Q9BWH2: FUNDC2; NbExp=3; IntAct=EBI-10192441, EBI-714482; CC Q86VR2; Q9H0R8: GABARAPL1; NbExp=8; IntAct=EBI-10192441, EBI-746969; CC Q86VR2; P60520: GABARAPL2; NbExp=3; IntAct=EBI-10192441, EBI-720116; CC Q86VR2; Q96F15: GIMAP5; NbExp=5; IntAct=EBI-10192441, EBI-6166686; CC Q86VR2; O14653: GOSR2; NbExp=3; IntAct=EBI-10192441, EBI-4401517; CC Q86VR2; P30519: HMOX2; NbExp=3; IntAct=EBI-10192441, EBI-712096; CC Q86VR2; Q9BUP3-3: HTATIP2; NbExp=3; IntAct=EBI-10192441, EBI-12937691; CC Q86VR2; Q01628: IFITM3; NbExp=3; IntAct=EBI-10192441, EBI-7932862; CC Q86VR2; Q8N5M9: JAGN1; NbExp=3; IntAct=EBI-10192441, EBI-10266796; CC Q86VR2; Q68G75: LEMD1; NbExp=3; IntAct=EBI-10192441, EBI-12268900; CC Q86VR2; Q9UBY5: LPAR3; NbExp=5; IntAct=EBI-10192441, EBI-12033434; CC Q86VR2; Q7L5N7: LPCAT2; NbExp=3; IntAct=EBI-10192441, EBI-4280011; CC Q86VR2; O75427: LRCH4; NbExp=3; IntAct=EBI-10192441, EBI-718707; CC Q86VR2; Q969L2: MAL2; NbExp=3; IntAct=EBI-10192441, EBI-944295; CC Q86VR2; Q13021: MALL; NbExp=3; IntAct=EBI-10192441, EBI-750078; CC Q86VR2; Q9H492: MAP1LC3A; NbExp=9; IntAct=EBI-10192441, EBI-720768; CC Q86VR2; Q96EZ8: MCRS1; NbExp=3; IntAct=EBI-10192441, EBI-348259; CC Q86VR2; Q9GZY8-5: MFF; NbExp=3; IntAct=EBI-10192441, EBI-11956541; CC Q86VR2; Q70IA6: MOB2; NbExp=3; IntAct=EBI-10192441, EBI-2558739; CC Q86VR2; O75425: MOSPD3; NbExp=3; IntAct=EBI-10192441, EBI-12179105; CC Q86VR2; Q8IXM6: NRM; NbExp=3; IntAct=EBI-10192441, EBI-10262547; CC Q86VR2; Q96CV9: OPTN; NbExp=3; IntAct=EBI-10192441, EBI-748974; CC Q86VR2; Q53FV1: ORMDL2; NbExp=3; IntAct=EBI-10192441, EBI-11075081; CC Q86VR2; Q8N138: ORMDL3; NbExp=3; IntAct=EBI-10192441, EBI-721750; CC Q86VR2; Q9NUU6: OTULINL; NbExp=3; IntAct=EBI-10192441, EBI-6916492; CC Q86VR2; Q99640-2: PKMYT1; NbExp=3; IntAct=EBI-10192441, EBI-12257782; CC Q86VR2; Q04941: PLP2; NbExp=3; IntAct=EBI-10192441, EBI-608347; CC Q86VR2; Q8IY26: PLPP6; NbExp=3; IntAct=EBI-10192441, EBI-11721828; CC Q86VR2; P54315: PNLIPRP1; NbExp=3; IntAct=EBI-10192441, EBI-8652812; CC Q86VR2; O60831: PRAF2; NbExp=3; IntAct=EBI-10192441, EBI-2506064; CC Q86VR2; Q9UI14: RABAC1; NbExp=3; IntAct=EBI-10192441, EBI-712367; CC Q86VR2; Q96HR9-2: REEP6; NbExp=3; IntAct=EBI-10192441, EBI-14065960; CC Q86VR2; Q96GQ5: RUSF1; NbExp=3; IntAct=EBI-10192441, EBI-8636004; CC Q86VR2; O00767: SCD; NbExp=3; IntAct=EBI-10192441, EBI-2684237; CC Q86VR2; Q96IW7: SEC22A; NbExp=5; IntAct=EBI-10192441, EBI-8652744; CC Q86VR2; Q9HC62: SENP2; NbExp=3; IntAct=EBI-10192441, EBI-714881; CC Q86VR2; Q8N6R1: SERP2; NbExp=3; IntAct=EBI-10192441, EBI-749270; CC Q86VR2; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-10192441, EBI-2854842; CC Q86VR2; Q9BWM7: SFXN3; NbExp=5; IntAct=EBI-10192441, EBI-1171999; CC Q86VR2; Q99726: SLC30A3; NbExp=3; IntAct=EBI-10192441, EBI-10294651; CC Q86VR2; Q13433-2: SLC39A6; NbExp=3; IntAct=EBI-10192441, EBI-12956703; CC Q86VR2; Q9NRQ5: SMCO4; NbExp=3; IntAct=EBI-10192441, EBI-8640191; CC Q86VR2; B2RUZ4: SMIM1; NbExp=3; IntAct=EBI-10192441, EBI-12188413; CC Q86VR2; Q9ULZ2: STAP1; NbExp=8; IntAct=EBI-10192441, EBI-6083058; CC Q86VR2; Q13190: STX5; NbExp=3; IntAct=EBI-10192441, EBI-714206; CC Q86VR2; O15400: STX7; NbExp=3; IntAct=EBI-10192441, EBI-3221827; CC Q86VR2; Q9UNK0: STX8; NbExp=5; IntAct=EBI-10192441, EBI-727240; CC Q86VR2; O43759-2: SYNGR1; NbExp=3; IntAct=EBI-10192441, EBI-12187159; CC Q86VR2; Q969Z0: TBRG4; NbExp=3; IntAct=EBI-10192441, EBI-702328; CC Q86VR2; Q15560: TCEA2; NbExp=3; IntAct=EBI-10192441, EBI-710310; CC Q86VR2; Q9NZ01: TECR; NbExp=3; IntAct=EBI-10192441, EBI-2877718; CC Q86VR2; Q9NV29: TMEM100; NbExp=3; IntAct=EBI-10192441, EBI-8644968; CC Q86VR2; P17152: TMEM11; NbExp=3; IntAct=EBI-10192441, EBI-723946; CC Q86VR2; A0PK00: TMEM120B; NbExp=3; IntAct=EBI-10192441, EBI-10171534; CC Q86VR2; Q5BJH2-2: TMEM128; NbExp=3; IntAct=EBI-10192441, EBI-10694905; CC Q86VR2; Q96HP8: TMEM176A; NbExp=3; IntAct=EBI-10192441, EBI-2800645; CC Q86VR2; Q96B42-2: TMEM18; NbExp=3; IntAct=EBI-10192441, EBI-17196383; CC Q86VR2; Q969S6: TMEM203; NbExp=3; IntAct=EBI-10192441, EBI-12274070; CC Q86VR2; A2RU14: TMEM218; NbExp=3; IntAct=EBI-10192441, EBI-10173151; CC Q86VR2; Q9H0R3: TMEM222; NbExp=3; IntAct=EBI-10192441, EBI-347385; CC Q86VR2; Q96Q45-2: TMEM237; NbExp=3; IntAct=EBI-10192441, EBI-10982110; CC Q86VR2; Q8WW34-2: TMEM239; NbExp=3; IntAct=EBI-10192441, EBI-11528917; CC Q86VR2; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-10192441, EBI-12887458; CC Q86VR2; Q8TBM7: TMEM254; NbExp=3; IntAct=EBI-10192441, EBI-11956809; CC Q86VR2; Q69YG0: TMEM42; NbExp=3; IntAct=EBI-10192441, EBI-12038591; CC Q86VR2; Q9H2L4: TMEM60; NbExp=3; IntAct=EBI-10192441, EBI-2852148; CC Q86VR2; Q6PI78: TMEM65; NbExp=3; IntAct=EBI-10192441, EBI-6656213; CC Q86VR2; Q6ZT21: TMPPE; NbExp=3; IntAct=EBI-10192441, EBI-11724433; CC Q86VR2; Q6ZUI0: TPRG1; NbExp=3; IntAct=EBI-10192441, EBI-17249488; CC Q86VR2; A0AVG3: TSNARE1; NbExp=3; IntAct=EBI-10192441, EBI-12003468; CC Q86VR2; Q5TGU0: TSPO2; NbExp=5; IntAct=EBI-10192441, EBI-12195249; CC Q86VR2; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-10192441, EBI-2819725; CC Q86VR2; P23763-3: VAMP1; NbExp=3; IntAct=EBI-10192441, EBI-12097582; CC Q86VR2; Q15836: VAMP3; NbExp=3; IntAct=EBI-10192441, EBI-722343; CC Q86VR2; O75379: VAMP4; NbExp=3; IntAct=EBI-10192441, EBI-744953; CC Q86VR2; O95183: VAMP5; NbExp=3; IntAct=EBI-10192441, EBI-10191195; CC Q86VR2; Q9P0L0: VAPA; NbExp=3; IntAct=EBI-10192441, EBI-1059156; CC Q86VR2; O95292: VAPB; NbExp=3; IntAct=EBI-10192441, EBI-1188298; CC Q86VR2; Q9Y548: YIPF1; NbExp=3; IntAct=EBI-10192441, EBI-7850136; CC Q86VR2; Q96EC8: YIPF6; NbExp=5; IntAct=EBI-10192441, EBI-751210; CC Q86VR2; P0DTD3: 9c; Xeno; NbExp=3; IntAct=EBI-10192441, EBI-25475917; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:33826365, ECO:0000269|PubMed:34338405}; Multi-pass CC membrane protein {ECO:0000255}. Note=Localizes preferentially to CC endoplasmic reticulum tubules and sheet edges. CC {ECO:0000269|PubMed:33826365}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q86VR2-1; Sequence=Displayed; CC Name=2; CC IsoId=Q86VR2-2; Sequence=VSP_056991; CC -!- INDUCTION: Induced by amino acid starvation but not by endoplasmic CC reticulum stress. {ECO:0000269|PubMed:33826365}. CC -!- DOMAIN: The LIR motif interacts with ATG8 family proteins. CC {ECO:0000269|PubMed:26040720}. CC -!- SIMILARITY: Belongs to the RETREG family. {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; AK091125; BAG52287.1; -; mRNA. DR EMBL; AK294791; BAG57914.1; -; mRNA. DR EMBL; AC067852; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471152; EAW60851.1; -; Genomic_DNA. DR EMBL; BC049370; AAH49370.1; -; mRNA. DR CCDS; CCDS11432.1; -. [Q86VR2-1] DR RefSeq; NP_835227.1; NM_178126.3. [Q86VR2-1] DR AlphaFoldDB; Q86VR2; -. DR BioGRID; 127817; 233. DR DIP; DIP-61578N; -. DR IntAct; Q86VR2; 159. DR MINT; Q86VR2; -. DR STRING; 9606.ENSP00000309432; -. DR iPTMnet; Q86VR2; -. DR PhosphoSitePlus; Q86VR2; -. DR SwissPalm; Q86VR2; -. DR BioMuta; RETREG3; -. DR DMDM; 74727607; -. DR EPD; Q86VR2; -. DR jPOST; Q86VR2; -. DR MassIVE; Q86VR2; -. DR MaxQB; Q86VR2; -. DR PaxDb; 9606-ENSP00000309432; -. DR PeptideAtlas; Q86VR2; -. DR ProteomicsDB; 3584; -. DR ProteomicsDB; 70060; -. [Q86VR2-1] DR Pumba; Q86VR2; -. DR Antibodypedia; 3087; 80 antibodies from 17 providers. DR DNASU; 162427; -. DR Ensembl; ENST00000309428.10; ENSP00000309432.4; ENSG00000141699.11. [Q86VR2-1] DR GeneID; 162427; -. DR KEGG; hsa:162427; -. DR MANE-Select; ENST00000309428.10; ENSP00000309432.4; NM_178126.4; NP_835227.1. DR UCSC; uc060fkv.1; human. [Q86VR2-1] DR AGR; HGNC:27258; -. DR CTD; 162427; -. DR DisGeNET; 162427; -. DR GeneCards; RETREG3; -. DR HGNC; HGNC:27258; RETREG3. DR HPA; ENSG00000141699; Low tissue specificity. DR MIM; 616498; gene. DR neXtProt; NX_Q86VR2; -. DR OpenTargets; ENSG00000141699; -. DR PharmGKB; PA162386207; -. DR VEuPathDB; HostDB:ENSG00000141699; -. DR eggNOG; ENOG502QPTN; Eukaryota. DR GeneTree; ENSGT00940000161349; -. DR HOGENOM; CLU_036265_0_0_1; -. DR InParanoid; Q86VR2; -. DR OMA; HRVFQHV; -. DR OrthoDB; 5400903at2759; -. DR PhylomeDB; Q86VR2; -. DR TreeFam; TF329111; -. DR PathwayCommons; Q86VR2; -. DR SignaLink; Q86VR2; -. DR SIGNOR; Q86VR2; -. DR BioGRID-ORCS; 162427; 28 hits in 1179 CRISPR screens. DR ChiTaRS; FAM134C; human. DR GeneWiki; FAM134C; -. DR GenomeRNAi; 162427; -. DR Pharos; Q86VR2; Tdark. DR PRO; PR:Q86VR2; -. DR Proteomes; UP000005640; Chromosome 17. DR RNAct; Q86VR2; Protein. DR Bgee; ENSG00000141699; Expressed in parotid gland and 211 other cell types or tissues. DR ExpressionAtlas; Q86VR2; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0071782; C:endoplasmic reticulum tubular network; IDA:UniProtKB. DR GO; GO:0032991; C:protein-containing complex; IDA:MGI. DR GO; GO:0140506; F:endoplasmic reticulum-autophagosome adaptor activity; IEA:Ensembl. DR GO; GO:0030574; P:collagen catabolic process; IEA:Ensembl. DR GO; GO:0071786; P:endoplasmic reticulum tubular network organization; IMP:UniProtKB. DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:UniProtKB. DR GO; GO:0061709; P:reticulophagy; IMP:UniProtKB. DR CDD; cd22562; RETR3_RHD; 1. DR InterPro; IPR043384; RETREG1/3. DR PANTHER; PTHR28659; RETICULOPHAGY REGULATOR 3; 1. DR PANTHER; PTHR28659:SF1; RETICULOPHAGY REGULATOR 3; 1. DR Genevisible; Q86VR2; HS. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Autophagy; Endoplasmic reticulum; KW Membrane; Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378" FT CHAIN 2..466 FT /note="Reticulophagy regulator 3" FT /id="PRO_0000288469" FT TOPO_DOM 2..80 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:33826365" FT TRANSMEM 81..101 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 102..163 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:33826365" FT TRANSMEM 164..184 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 185..186 FT /note="Cytoplasmic" FT /evidence="ECO:0000305|PubMed:33826365" FT TRANSMEM 187..207 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 208..381 FT /note="Lumenal" FT /evidence="ECO:0000305|PubMed:33826365" FT TRANSMEM 382..402 FT /note="Helical" FT /evidence="ECO:0000255" FT TOPO_DOM 403..466 FT /note="Cytoplasmic" FT /evidence="ECO:0000269|PubMed:33826365" FT REGION 1..28 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 284..374 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 412..466 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 445..450 FT /note="LIR motif" FT /evidence="ECO:0000305|PubMed:26040720" FT COMPBIAS 292..310 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 314..328 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 2 FT /note="N-acetylalanine" FT /evidence="ECO:0007744|PubMed:19413330, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:22814378" FT MOD_RES 10 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 26 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 258 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 260 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692" FT MOD_RES 283 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 285 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 288 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CQV4" FT MOD_RES 293 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CQV4" FT MOD_RES 303 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9CQV4" FT MOD_RES 307 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569" FT MOD_RES 310 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:24275569" FT MOD_RES 313 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:24275569" FT MOD_RES 320 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT MOD_RES 360 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 440 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332" FT VAR_SEQ 1..195 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_056991" FT MUTAGEN 445..450 FT /note="DDFELL->AAAAAA: Reduced formation of FT autophagosomes." FT /evidence="ECO:0000269|PubMed:33826365" FT MUTAGEN 447..450 FT /note="FELL->AELA: Abolishes interaction with ATG8 family FT proteins, induction of ER fragmentation and ER FT degradation." FT /evidence="ECO:0000269|PubMed:34338405" SQ SEQUENCE 466 AA; 51396 MW; F9D468353C13A14B CRC64; MAEAEGVPTT PGPASGSTFR GRRDVSGSWE RDQQVEAAQR ALVEVLGPYE PLLSRVQAAL VWERPARSAL WCLGLNAAFW FFALTSLRLV FLLAFGLMII VCIDQWKNKI WPEIKVPRPD ALDNESWGFV HPRLLSVPEL CHHVAEVWVS GTIFIRNVLL FKKQNPGKFC LLSCGILTFL AVLGRYVPGL LLSYLMLVTV MMWPLAVYHR LWDRAYVRLK PALQRLDFSV RGYMMSKQRE RQLRRRALHP ERAMDNHSDS EEELAAFCPQ LDDSTVAREL AITDSEHSDA EVSCTDNGTF NLSRGQTPLT EGSEDLDGHS DPEESFARDL PDFPSINMDP AGLDDEDDTS IGMPSLMYRS PPGAEEPQAP PASRDEAALP ELLLGALPVG SNLTSNLASL VSQGMIQLAL SGASQPGPSG APAQRATRGF LRSPSSDLDT DAEGDDFELL DQSELSQLDP ASSRSH //