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DRAM2_MOUSE
ID   DRAM2_MOUSE             Reviewed;         267 AA.
AC   Q9CR48; Q9D520;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=DNA damage-regulated autophagy modulator protein 2;
DE   AltName: Full=Transmembrane protein 77;
GN   Name=Dram2; Synonyms=Tmem77;
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].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryo, Mammary gland, Spleen, Testis, and Tongue;
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   SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX   PubMed=25983245; DOI=10.1016/j.ajhg.2015.04.006;
RG   UK Inherited Retinal Disease Consortium;
RA   El-Asrag M.E., Sergouniotis P.I., McKibbin M., Plagnol V., Sheridan E.,
RA   Waseem N., Abdelhamed Z., McKeefry D., Van Schil K., Poulter J.A.,
RA   Johnson C.A., Carr I.M., Leroy B.P., De Baere E., Inglehearn C.F.,
RA   Webster A.R., Toomes C., Ali M.;
RT   "Biallelic mutations in the autophagy regulator DRAM2 cause retinal
RT   dystrophy with early macular involvement.";
RL   Am. J. Hum. Genet. 96:948-954(2015).
CC   -!- FUNCTION: Plays a role in the initiation of autophagy. In the retina,
CC       might be involved in the process of photoreceptor cells renewal and
CC       recycling to preserve visual function. Induces apoptotic cell death
CC       when coexpressed with DRAM1. {ECO:0000250|UniProtKB:Q6UX65}.
CC   -!- SUBCELLULAR LOCATION: Lysosome membrane {ECO:0000250|UniProtKB:Q6UX65};
CC       Multi-pass membrane protein {ECO:0000250|UniProtKB:Q6UX65}.
CC       Photoreceptor inner segment {ECO:0000269|PubMed:25983245}. Apical cell
CC       membrane {ECO:0000269|PubMed:25983245}. Note=Localized to photoreceptor
CC       inner segments and to the apical surface of retinal pigment epithelial
CC       cells. {ECO:0000269|PubMed:25983245}.
CC   -!- TISSUE SPECIFICITY: Expressed in the retina.
CC       {ECO:0000269|PubMed:25983245}.
CC   -!- SIMILARITY: Belongs to the DRAM/TMEM150 family. {ECO:0000305}.
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DR   EMBL; AK009940; BAB26598.1; -; mRNA.
DR   EMBL; AK012044; BAB27990.1; -; mRNA.
DR   EMBL; AK015888; BAB30020.1; -; mRNA.
DR   EMBL; AK052824; BAC35162.1; -; mRNA.
DR   EMBL; AK172455; BAE43014.1; -; mRNA.
DR   CCDS; CCDS17725.1; -.
DR   RefSeq; NP_001273915.1; NM_001286986.1.
DR   RefSeq; NP_001273916.1; NM_001286987.1.
DR   RefSeq; NP_080289.1; NM_026013.3.
DR   AlphaFoldDB; Q9CR48; -.
DR   STRING; 10090.ENSMUSP00000063510; -.
DR   iPTMnet; Q9CR48; -.
DR   PhosphoSitePlus; Q9CR48; -.
DR   jPOST; Q9CR48; -.
DR   MaxQB; Q9CR48; -.
DR   PaxDb; Q9CR48; -.
DR   PeptideAtlas; Q9CR48; -.
DR   PRIDE; Q9CR48; -.
DR   ProteomicsDB; 279484; -.
DR   Antibodypedia; 20104; 78 antibodies from 19 providers.
DR   DNASU; 67171; -.
DR   Ensembl; ENSMUST00000067630; ENSMUSP00000063510; ENSMUSG00000027900.
DR   Ensembl; ENSMUST00000121034; ENSMUSP00000112680; ENSMUSG00000027900.
DR   GeneID; 67171; -.
DR   KEGG; mmu:67171; -.
DR   UCSC; uc008qwd.2; mouse.
DR   CTD; 128338; -.
DR   MGI; MGI:1914421; Dram2.
DR   VEuPathDB; HostDB:ENSMUSG00000027900; -.
DR   eggNOG; KOG4320; Eukaryota.
DR   GeneTree; ENSGT01030000234578; -.
DR   HOGENOM; CLU_059992_2_2_1; -.
DR   InParanoid; Q9CR48; -.
DR   OMA; IYMLVQT; -.
DR   OrthoDB; 1199230at2759; -.
DR   PhylomeDB; Q9CR48; -.
DR   TreeFam; TF314508; -.
DR   BioGRID-ORCS; 67171; 2 hits in 72 CRISPR screens.
DR   ChiTaRS; Dram2; mouse.
DR   PRO; PR:Q9CR48; -.
DR   Proteomes; UP000000589; Chromosome 3.
DR   RNAct; Q9CR48; protein.
DR   Bgee; ENSMUSG00000027900; Expressed in intercostal muscle and 256 other tissues.
DR   ExpressionAtlas; Q9CR48; baseline and differential.
DR   Genevisible; Q9CR48; MM.
DR   GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR   GO; GO:0005794; C:Golgi apparatus; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR   GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR   GO; GO:0001917; C:photoreceptor inner segment; IDA:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR   GO; GO:0006914; P:autophagy; IEA:UniProtKB-KW.
DR   GO; GO:0045494; P:photoreceptor cell maintenance; IMP:UniProtKB.
DR   GO; GO:0010506; P:regulation of autophagy; ISO:MGI.
DR   GO; GO:0007601; P:visual perception; ISS:UniProtKB.
DR   InterPro; IPR032990; DRAM2.
DR   InterPro; IPR019402; Frag1/DRAM/Sfk1.
DR   PANTHER; PTHR21324:SF10; PTHR21324:SF10; 1.
DR   Pfam; PF10277; Frag1; 1.
PE   2: Evidence at transcript level;
KW   Apoptosis; Autophagy; Cell membrane; Lysosome; Membrane;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..267
FT                   /note="DNA damage-regulated autophagy modulator protein 2"
FT                   /id="PRO_0000254103"
FT   TRANSMEM        8..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        53..73
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        87..107
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        118..138
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        203..223
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        253
FT                   /note="P -> L (in Ref. 1; BAB30020)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   267 AA;  30228 MW;  228214D5AFF36783 CRC64;
     MWWFQQGLSF LPSALVIWTF ATFIFSYITA ITLHHVDPAL PYISDTGTIP PERCLFGVML
     NIAAVLGIAT MYVRYKQVHA LNPEENLIIK LNKAGLVLGI LSCLGLSLVA NFQKSTLFIV
     HVCGAVLAFS MGSFYMFVQT ILSYQMQPKI HSKQVFWVRL LLVIWCGVSA LSMMTCSSIL
     YSSDFGPDVV QKLHWNPEDK GYVLHLVTTA AEWSMSFSFF GFFLTYIRDF QKITLRVEAN
     LHGLTLYDTV PCPVNNERTP LLSRDFQ
 
 
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