ID RETR2_HUMAN Reviewed; 543 AA. AC Q8NC44; Q6P1P5; Q9H0K7; DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot. DT 18-MAY-2010, sequence version 3. DT 10-JUN-2026, entry version 157. DE RecName: Full=Reticulophagy regulator 2 {ECO:0000312|HGNC:HGNC:28450}; GN Name=RETREG2 {ECO:0000312|HGNC:HGNC:28450}; GN Synonyms=C2orf17, FAM134A, MAG2 {ECO:0000312|HGNC:HGNC:28450}; 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], AND VARIANT GLN-419. 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=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 262-543, AND VARIANT GLN-419. 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 431-543. RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [5] RP SEQUENCE REVISION. RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-311 AND SER-385, AND 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 [7] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-279; SER-281 AND SER-283, RP VARIANT [LARGE SCALE ANALYSIS] GLN-419, AND IDENTIFICATION BY MASS RP 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 [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=18318008; DOI=10.1002/pmic.200700884; RA Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., RA Zou H., Gu J.; RT "Large-scale phosphoproteome analysis of human liver tissue by enrichment RT and fractionation of phosphopeptides with strong anion exchange RT chromatography."; RL Proteomics 8:1346-1361(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-344 AND SER-347, AND RP IDENTIFICATION BY 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, AND IDENTIFICATION BY RP 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 [13] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-385, 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-291; SER-311; SER-347 AND RP SER-385, 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 492-PHE--LEU-495. 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 INTERACTION WITH GABARAPL1 AND MAP1LC3B. RX PubMed=34854256; DOI=10.1002/2211-5463.13340; RA Zhao J., Li Z., Li J.; RT "The crystal structure of the FAM134B-GABARAP complex provides mechanistic RT insights into the selective binding of FAM134 to the GABARAP subfamily."; RL FEBS Open Bio 12:320-331(2022). 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). Required for collagen quality control in a CC LIR motif-independent manner (By similarity). CC {ECO:0000250|UniProtKB:Q6NS82, 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, PubMed:34854256). Shows higher affinity for GABARAPL1 CC than for MAP1LC3B (PubMed:34854256). Interacts with CANX CC (PubMed:34338405). {ECO:0000269|PubMed:26040720, CC ECO:0000269|PubMed:34338405, ECO:0000269|PubMed:34854256}. CC -!- INTERACTION: CC Q8NC44; Q9GZQ8: MAP1LC3B; NbExp=2; IntAct=EBI-712899, EBI-373144; CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane CC {ECO:0000269|PubMed:34338405}; Multi-pass membrane protein CC {ECO:0000255}. CC -!- DOMAIN: The LIR motif interacts with ATG8 family proteins. CC {ECO:0000269|PubMed:26040720, ECO:0000269|PubMed:34338405}. 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; AK074983; BAC11332.1; -; mRNA. DR EMBL; AC068946; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC064950; AAH64950.1; -; mRNA. DR EMBL; AL136758; CAB66692.2; -; mRNA. DR CCDS; CCDS2434.1; -. DR RefSeq; NP_077269.3; NM_024293.5. DR PDB; 6EWC; X-ray; 3.20 A; C/G=400-408. DR PDBsum; 6EWC; -. DR AlphaFoldDB; Q8NC44; -. DR SMR; Q8NC44; -. DR BioGRID; 122558; 54. DR DIP; DIP-56781N; -. DR FunCoup; Q8NC44; 1830. DR IntAct; Q8NC44; 45. DR MINT; Q8NC44; -. DR NDEx; MUSIC2-C5172-RETREG2; Osteosarcoma (U2OS) cell map - Endoplasmic reticulum (98 proteins). DR STRING; 9606.ENSP00000395249; -. DR iPTMnet; Q8NC44; -. DR PhosphoSitePlus; Q8NC44; -. DR BioMuta; RETREG2; -. DR DMDM; 296439357; -. DR jPOST; Q8NC44; -. DR MassIVE; Q8NC44; -. DR PaxDb; 9606-ENSP00000395249; -. DR PeptideAtlas; Q8NC44; -. DR ProteomicsDB; 72849; -. DR Pumba; Q8NC44; -. DR Antibodypedia; 2502; 42 antibodies from 15 providers. DR DNASU; 79137; -. DR Ensembl; ENST00000430297.7; ENSP00000395249.2; ENSG00000144567.12. DR GeneID; 79137; -. DR KEGG; hsa:79137; -. DR MANE-Select; ENST00000430297.7; ENSP00000395249.2; NM_024293.6; NP_077269.3. DR UCSC; uc002vjw.5; human. DR AGR; HGNC:28450; -. DR ClinPGx; PA162386165; -. DR CTD; 79137; -. DR DisGeNET; 79137; -. DR GeneCards; RETREG2; -. DR HGNC; HGNC:28450; RETREG2. DR HPA; ENSG00000144567; Low tissue specificity. DR MIM; 621473; gene. DR OpenTargets; ENSG00000144567; -. DR VEuPathDB; HostDB:ENSG00000144567; -. DR eggNOG; ENOG502QPTN; Eukaryota. DR GeneTree; ENSGT00940000162511; -. DR HOGENOM; CLU_036265_2_1_1; -. DR InParanoid; Q8NC44; -. DR OMA; EKWKPRF; -. DR OrthoDB; 10029527at2759; -. DR PAN-GO; Q8NC44; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q8NC44; -. DR PathwayCommons; Q8NC44; -. DR SignaLink; Q8NC44; -. DR Agora; ENSG00000144567; -. DR BioGRID-ORCS; 79137; 8 hits in 1155 CRISPR screens. DR ChiTaRS; FAM134A; human. DR GenomeRNAi; 79137; -. DR Pharos; Q8NC44; Tdark. DR PRO; PR:Q8NC44; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8NC44; protein. DR Bgee; ENSG00000144567; Expressed in sperm and 198 other cell types or tissues. DR ExpressionAtlas; Q8NC44; baseline and differential. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0140506; F:endoplasmic reticulum-autophagosome adaptor activity; IEA:Ensembl. DR CDD; cd22561; RETR2_RHD; 1. DR InterPro; IPR052114; ER_autophagy_membrane_reg. DR InterPro; IPR055257; RETR2_RHD. DR InterPro; IPR057282; RETREG1-3-like_RHD. DR PANTHER; PTHR20952; ADP-RIBOSYLATION-LIKE FACTOR 6-INTERACTING PROTEIN; 1. DR PANTHER; PTHR20952:SF4; RETICULOPHAGY REGULATOR 2; 1. DR Pfam; PF24456; RHD_RETREG1-3; 1. PE 1: Evidence at protein level; KW 3D-structure; Autophagy; Endoplasmic reticulum; Membrane; Phosphoprotein; KW Proteomics identification; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1..543 FT /note="Reticulophagy regulator 2" FT /id="PRO_0000089346" FT TRANSMEM 12..32 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 100..120 FT /note="Helical" FT /evidence="ECO:0000255" FT TRANSMEM 204..224 FT /note="Helical" FT /evidence="ECO:0000255" FT REGION 254..287 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 336..394 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 411..486 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 504..543 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOTIF 490..495 FT /note="LIR motif" FT /evidence="ECO:0000305|PubMed:26040720" FT COMPBIAS 254..265 FT /note="Basic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 275..285 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 461..480 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 512..524 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 279 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 281 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 283 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 291 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 311 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:24275569" FT MOD_RES 334 FT /note="Phosphothreonine" FT /evidence="ECO:0000250|UniProtKB:Q6NS82" FT MOD_RES 337 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q6NS82" FT MOD_RES 344 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 347 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:24275569" FT MOD_RES 385 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:18088087, ECO:0007744|PubMed:18318008, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569" FT VARIANT 374 FT /note="R -> H (in dbSNP:rs3210652)" FT /id="VAR_033720" FT VARIANT 419 FT /note="P -> Q (in dbSNP:rs3731900)" FT /evidence="ECO:0000269|PubMed:14702039, FT ECO:0000269|PubMed:15489334, ECO:0007744|PubMed:18669648" FT /id="VAR_022835" FT MUTAGEN 492..495 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" FT CONFLICT 338 FT /note="E -> G (in Ref. 1; BAC11332)" FT /evidence="ECO:0000305" FT HELIX 401..403 FT /evidence="ECO:0007829|PDB:6EWC" SQ SEQUENCE 543 AA; 57830 MW; 03DD659722BA9E5B CRC64; MASGGGGGNT GAGGGPGMGL SLGLGLGLSL GMSEATSEAE EEAATAEAVG RLATTLWLRL RGWEAVLAAA QRLLVWEKPL HSLVTAAALN GLFWLLSSSS LRPFFLLSVS LLAYFLLDLW QPRFLPDVSA SSPEEPHSDS EGAGSGARPH LLSVPELCRY LAESWLTFQI HLQELLQYKR QNPAQFCVRV CSGCAVLAVL GHYVPGIMIS YIVLLSILLW PLVVYHELIQ RMYTRLEPLL MQLDYSMKAE ANALHHKHDK RKRQGKNAPP GGDEPLAETE SESEAELAGF SPVVDVKKTA LALAITDSEL SDEEASILES GGFSVSRATT PQLTDVSEDL DQQSLPSEPE ETLSRDLGEG EEGELAPPED LLGRPQALSR QALDSEEEEE DVAAKETLLR LSSPLHFVNT HFNGAGSPPD GVKCSPGGPV ETLSPETVSG GLTALPGTLS PPLCLVGSDP APSPSILPPV PQDSPQPLPA PEEEEALTTE DFELLDQGEL EQLNAELGLE PETPPKPPDA PPLGPDIHSL VQSDQEAQAV AEP //