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RETR2_RAT
ID   RETR2_RAT               Reviewed;         541 AA.
AC   Q3MHU5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 2.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Reticulophagy regulator 2;
GN   Name=Retreg2; Synonyms=Fam134a;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RX   PubMed=15057822; DOI=10.1038/nature02426;
RA   Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA   Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA   Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA   Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA   Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA   Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA   Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA   Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA   Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA   Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA   Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA   Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA   Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA   Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA   Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA   Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA   Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA   Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA   Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA   Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA   Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA   Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA   Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA   Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA   Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA   Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA   Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA   Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA   Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA   Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA   Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA   Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA   Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA   Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA   Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA   Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA   Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA   Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA   Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA   Mockrin S., Collins F.S.;
RT   "Genome sequence of the Brown Norway rat yields insights into mammalian
RT   evolution.";
RL   Nature 428:493-521(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-541.
RC   TISSUE=Testis;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-274; SER-339 AND SER-342, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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   -!- DOMAIN: The LIR motif interacts with ATG8 family proteins.
CC       {ECO:0000250|UniProtKB:Q8NC44}.
CC   -!- SIMILARITY: Belongs to the RETREG family. {ECO:0000305}.
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DR   EMBL; AABR03068044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC104673; AAI04674.1; -; mRNA.
DR   RefSeq; NP_001094230.1; NM_001100760.1.
DR   AlphaFoldDB; Q3MHU5; -.
DR   STRING; 10116.ENSRNOP00000054145; -.
DR   iPTMnet; Q3MHU5; -.
DR   PhosphoSitePlus; Q3MHU5; -.
DR   jPOST; Q3MHU5; -.
DR   PaxDb; Q3MHU5; -.
DR   PRIDE; Q3MHU5; -.
DR   GeneID; 363252; -.
DR   KEGG; rno:363252; -.
DR   UCSC; RGD:1306844; rat.
DR   CTD; 79137; -.
DR   RGD; 1306844; Retreg2.
DR   VEuPathDB; HostDB:ENSRNOG00000018586; -.
DR   eggNOG; ENOG502QPTN; Eukaryota.
DR   InParanoid; Q3MHU5; -.
DR   OMA; TSPLHFV; -.
DR   OrthoDB; 901531at2759; -.
DR   PhylomeDB; Q3MHU5; -.
DR   TreeFam; TF329111; -.
DR   PRO; PR:Q3MHU5; -.
DR   Proteomes; UP000002494; Chromosome 9.
DR   Bgee; ENSRNOG00000018586; Expressed in frontal cortex and 19 other tissues.
DR   ExpressionAtlas; Q3MHU5; baseline and differential.
DR   Genevisible; Q3MHU5; RN.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISO:RGD.
DR   GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR   GO; GO:0140506; F:endoplasmic reticulum-autophagosome adaptor activity; ISO:RGD.
DR   GO; GO:0030574; P:collagen catabolic process; ISO:RGD.
DR   GO; GO:0007029; P:endoplasmic reticulum organization; ISO:RGD.
DR   GO; GO:0061709; P:reticulophagy; ISO:RGD.
PE   1: Evidence at protein level;
KW   Membrane; Phosphoprotein; Reference proteome; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..541
FT                   /note="Reticulophagy regulator 2"
FT                   /id="PRO_0000288464"
FT   TRANSMEM        75..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..115
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..389
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          403..440
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          459..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          496..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        506..524
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         274
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         276
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC44"
FT   MOD_RES         278
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8NC44"
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:0000250|UniProtKB:Q6NS82"
FT   MOD_RES         332
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q6NS82"
FT   MOD_RES         339
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         342
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
SQ   SEQUENCE   541 AA;  57659 MW;  DE2C518FA4E616B9 CRC64;
     MASSGGGNTG AGGTSGLGLG LGLGLCMGEA TGDAEEEAAA AEAVGRLATS LWLRLRGWEA
     VLAAAQRLLV WEKPLHSLVT AATLNGLFWL LSSSSLRPFF LLSISLLTYF LLDLWHPRFL
     PDVSAPPPEE PHSDSEGAGS GAQPHLLSVP ELCRYLAESW LTFQIHLQEL LQYKRQNPAQ
     FCARVCSGCA VLAVLGHYVP GIMISYIVLL SILLWPLVVY HELIQRMYTR LEPLLMQLDY
     SMKAEADALH HKHDKRKRQG KNAPPAGDEP LAETESESEA ELAGFSPVVD VKKTALALAI
     TDSELSDEEA SILESGGFSV SRATTPQLTD VSEDLDQQSL PSEPEEALSR ELGDGEETEL
     APPEDLLSAP PALSKQALDT EEEGAADKET LLQLSSPLHF VNTHFNGAGS PQEGVKCPPG
     GPVETLSPEA VSGDLMAPSS TLSPQLCLAE SGPVTLLSPS VLPSLPQDSP QALTAPEEEE
     ALTTEDFELL DQGELEQLNA ELGLGPEMPP KPPDVLPPPP LGPDSHSLVQ SDQEAHAVVE
     P
 
 
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