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RETR2_MOUSE
ID   RETR2_MOUSE             Reviewed;         541 AA.
AC   Q6NS82; Q3TA48; Q3TMF7; Q8BSD3; Q8CHY1; Q8R0Q3;
DT   05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2005, sequence version 2.
DT   03-AUG-2022, entry version 127.
DE   RecName: Full=Reticulophagy regulator 2;
GN   Name=Retreg2; Synonyms=Fam134a;
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] (ISOFORMS 1 AND 3).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Cerebellum, Embryo, Lung, and Spleen;
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 MRNA] (ISOFORMS 2 AND 3).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, Kidney, and Salivary gland;
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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-274; SER-276 AND SER-278, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA   Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT   "Large-scale phosphorylation analysis of mouse liver.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA   Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA   Thibault P.;
RT   "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL   Immunity 30:143-154(2009).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=19838196; DOI=10.1038/ng.464;
RA   Kurth I., Pamminger T., Hennings J.C., Soehendra D., Huebner A.K.,
RA   Rotthier A., Baets J., Senderek J., Topaloglu H., Farrell S.A.,
RA   Nuernberg G., Nurnberg P., De Jonghe P., Gal A., Kaether C., Timmerman V.,
RA   Huebner C.A.;
RT   "Mutations in FAM134B, encoding a newly identified Golgi protein, cause
RT   severe sensory and autonomic neuropathy.";
RL   Nat. Genet. 41:1179-1181(2009).
RN   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-274; SER-276; SER-278;
RP   THR-329; SER-332; SER-339 AND SER-342, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brain, Brown adipose tissue, Kidney, Liver, Lung, Spleen, and
RC   Testis;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- SUBUNIT: Interacts with ATG8 family modifier proteins MAP1LC3A,
CC       MAP1LC3B, GABARAP and GABARAPL1. {ECO:0000250|UniProtKB:Q8NC44}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q6NS82-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6NS82-2; Sequence=VSP_014550, VSP_014551;
CC       Name=3;
CC         IsoId=Q6NS82-3; Sequence=VSP_014551;
CC   -!- TISSUE SPECIFICITY: Mainly expressed in the central nervous system and
CC       in parenchymatous organs including liver, lung and kidney.
CC       {ECO:0000269|PubMed:19838196}.
CC   -!- DOMAIN: The LIR motif interacts with ATG8 family proteins.
CC       {ECO:0000250|UniProtKB:Q8NC44}.
CC   -!- SIMILARITY: Belongs to the RETREG family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC28789.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AK034667; BAC28789.1; ALT_FRAME; mRNA.
DR   EMBL; AK160400; BAE35769.1; -; mRNA.
DR   EMBL; AK165957; BAE38485.1; -; mRNA.
DR   EMBL; AK172093; BAE42822.1; -; mRNA.
DR   EMBL; BC026519; AAH26519.1; -; mRNA.
DR   EMBL; BC038286; AAH38286.1; -; mRNA.
DR   EMBL; BC070406; AAH70406.1; -; mRNA.
DR   CCDS; CCDS35621.1; -. [Q6NS82-1]
DR   CCDS; CCDS78621.1; -. [Q6NS82-3]
DR   RefSeq; NP_001292160.1; NM_001305231.1. [Q6NS82-3]
DR   RefSeq; NP_001292161.1; NM_001305232.1.
DR   RefSeq; NP_739561.2; NM_170755.2. [Q6NS82-1]
DR   AlphaFoldDB; Q6NS82; -.
DR   BioGRID; 230611; 8.
DR   IntAct; Q6NS82; 7.
DR   STRING; 10090.ENSMUSP00000095300; -.
DR   iPTMnet; Q6NS82; -.
DR   PhosphoSitePlus; Q6NS82; -.
DR   EPD; Q6NS82; -.
DR   jPOST; Q6NS82; -.
DR   MaxQB; Q6NS82; -.
DR   PaxDb; Q6NS82; -.
DR   PeptideAtlas; Q6NS82; -.
DR   PRIDE; Q6NS82; -.
DR   ProteomicsDB; 255234; -. [Q6NS82-1]
DR   ProteomicsDB; 255235; -. [Q6NS82-2]
DR   ProteomicsDB; 255236; -. [Q6NS82-3]
DR   Antibodypedia; 2502; 43 antibodies from 16 providers.
DR   DNASU; 227298; -.
DR   Ensembl; ENSMUST00000097694; ENSMUSP00000095300; ENSMUSG00000049339. [Q6NS82-1]
DR   Ensembl; ENSMUST00000190240; ENSMUSP00000139410; ENSMUSG00000049339. [Q6NS82-3]
DR   GeneID; 227298; -.
DR   KEGG; mmu:227298; -.
DR   UCSC; uc007bnt.1; mouse. [Q6NS82-1]
DR   UCSC; uc007bnu.1; mouse. [Q6NS82-3]
DR   CTD; 79137; -.
DR   MGI; MGI:2388278; Retreg2.
DR   VEuPathDB; HostDB:ENSMUSG00000049339; -.
DR   eggNOG; ENOG502QPTN; Eukaryota.
DR   GeneTree; ENSGT00940000162511; -.
DR   HOGENOM; CLU_036265_2_1_1; -.
DR   InParanoid; Q6NS82; -.
DR   OMA; TSPLHFV; -.
DR   OrthoDB; 901531at2759; -.
DR   PhylomeDB; Q6NS82; -.
DR   TreeFam; TF329111; -.
DR   BioGRID-ORCS; 227298; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Fam134a; mouse.
DR   PRO; PR:Q6NS82; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q6NS82; protein.
DR   Bgee; ENSMUSG00000049339; Expressed in perirhinal cortex and 254 other tissues.
DR   ExpressionAtlas; Q6NS82; baseline and differential.
DR   Genevisible; Q6NS82; MM.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0140506; F:endoplasmic reticulum-autophagosome adaptor activity; IMP:MGI.
DR   GO; GO:0030574; P:collagen catabolic process; IMP:MGI.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; IMP:MGI.
DR   GO; GO:0061709; P:reticulophagy; IDA:MGI.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Phosphoprotein; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..541
FT                   /note="Reticulophagy regulator 2"
FT                   /id="PRO_0000089347"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        199..219
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          249..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          331..369
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..541
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           485..490
FT                   /note="LIR motif"
FT                   /evidence="ECO:0000250|UniProtKB:Q9H6L5"
FT   COMPBIAS        434..448
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        506..520
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         274
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         276
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17242355,
FT                   ECO:0007744|PubMed:21183079"
FT   MOD_RES         286
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC44"
FT   MOD_RES         306
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC44"
FT   MOD_RES         329
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   VAR_SEQ         1..226
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_014550"
FT   VAR_SEQ         431..467
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_014551"
FT   CONFLICT        139
FT                   /note="G -> R (in Ref. 1; BAC28789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        515
FT                   /note="V -> L (in Ref. 1; BAC28789)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        525
FT                   /note="S -> C (in Ref. 1; BAE38485)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   541 AA;  57542 MW;  88C99862C92BAF10 CRC64;
     MASSGGGNTG AGGTSGLGLG LGLSLGMGEA TGDAEEEAAA AEAVGRLATS LWLRLRGWEA
     VLAAAQRLLV WEKPLHSLVT AATLNGLFWL LSSSSLRPFF LLSISLLTYF LLDLWHPRFL
     PDVSAPPPEE PHSDSEGAGS GAQPHLLSVP ELCRYLAESW LTFQIHLQEL LQYKRQNPAQ
     FCARGCAACA VLAVLGHYVP GVMISYIVLL SILLWPLVVY HELIQRMYTR LEPLLMQLDY
     SMKAEADALH HKHDKRKRQG KSAPPAGDEP LAETESESEA ELAGFSPVVD VKKTALALAI
     TDSELSDEEA SILESGGFSV SRATTPQLTD VSEDLDQQSL PSEPEEALNR ELGEGEETEL
     ASPEDLLSAP PALSKQALDT EEEGAADKEA LLQLSSPLHF VNTHFNGAGS PQDGVKCPPG
     APVKTLSPEA VSGDLMAPSS TLSPQLCLAE SGPVTPLSPS VLPSLPQDSP QPLAAPEEEE
     ALTTEDFELL DQGELEQLNA ELGLGPEMPP KPPDVLPPPP LGADSHSLVQ SDQEAHAEVE
     P
 
 
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