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TIM21_MOUSE
ID   TIM21_MOUSE             Reviewed;         244 AA.
AC   Q8CCM6; Q3THX0; Q8CE44; Q9CYU8; Q9CZS4;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-APR-2020, sequence version 2.
DT   03-AUG-2022, entry version 117.
DE   RecName: Full=Mitochondrial import inner membrane translocase subunit Tim21;
DE   AltName: Full=TIM21-like protein, mitochondrial;
DE   Flags: Precursor;
GN   Name=Timm21; Synonyms=Tim21;
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 2).
RC   STRAIN=C57BL/6J; TISSUE=Embryo, Olfactory bulb, and Skin;
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] (ISOFORM 1).
RC   STRAIN=C57BL/6J; TISSUE=Eye, and 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   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Liver, Spleen, and 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   -!- FUNCTION: Participates in the translocation of transit peptide-
CC       containing proteins across the mitochondrial inner membrane. Also
CC       required for assembly of mitochondrial respiratory chain complex I and
CC       complex IV as component of the MITRAC (mitochondrial translation
CC       regulation assembly intermediate of cytochrome c oxidase complex)
CC       complex. Probably shuttles between the presequence translocase and
CC       respiratory-chain assembly intermediates in a process that promotes
CC       incorporation of early nuclear-encoded subunits into these complexes.
CC       {ECO:0000250|UniProtKB:Q9BVV7}.
CC   -!- SUBUNIT: Component of the TIM23 complex. Component of the MITRAC
CC       (mitochondrial translation regulation assembly intermediate of
CC       cytochrome c oxidase complex) complex, the core components of this
CC       complex being COA3/MITRAC12 and COX14. Interacts with COA3 AND MT-
CC       CO1/COX1. {ECO:0000250|UniProtKB:Q9BVV7}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion membrane {ECO:0000305}; Single-pass
CC       membrane protein {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8CCM6-2; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8CCM6-3; Sequence=VSP_060547, VSP_060548;
CC   -!- SIMILARITY: Belongs to the TIM21 family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC27885.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; AK012203; BAB28097.1; -; mRNA.
DR   EMBL; AK013281; BAB28768.1; -; mRNA.
DR   EMBL; AK029037; BAC26258.1; -; mRNA.
DR   EMBL; AK032468; BAC27885.1; ALT_SEQ; mRNA.
DR   EMBL; AK168105; BAE40076.1; -; mRNA.
DR   EMBL; BC034297; AAH34297.1; -; mRNA.
DR   CCDS; CCDS29386.1; -. [Q8CCM6-2]
DR   RefSeq; NP_080245.1; NM_025969.4. [Q8CCM6-2]
DR   RefSeq; XP_011245396.1; XM_011247094.2.
DR   AlphaFoldDB; Q8CCM6; -.
DR   SMR; Q8CCM6; -.
DR   STRING; 10090.ENSMUSP00000025547; -.
DR   PhosphoSitePlus; Q8CCM6; -.
DR   EPD; Q8CCM6; -.
DR   jPOST; Q8CCM6; -.
DR   MaxQB; Q8CCM6; -.
DR   PaxDb; Q8CCM6; -.
DR   PeptideAtlas; Q8CCM6; -.
DR   PRIDE; Q8CCM6; -.
DR   ProteomicsDB; 259390; -. [Q8CCM6-2]
DR   ProteomicsDB; 259391; -. [Q8CCM6-2]
DR   ProteomicsDB; 259392; -. [Q8CCM6-3]
DR   Antibodypedia; 2242; 49 antibodies from 18 providers.
DR   DNASU; 67105; -.
DR   Ensembl; ENSMUST00000025547; ENSMUSP00000025547; ENSMUSG00000024645. [Q8CCM6-2]
DR   GeneID; 67105; -.
DR   KEGG; mmu:67105; -.
DR   CTD; 29090; -.
DR   MGI; MGI:1920595; Timm21.
DR   VEuPathDB; HostDB:ENSMUSG00000024645; -.
DR   eggNOG; KOG4836; Eukaryota.
DR   GeneTree; ENSGT00390000011552; -.
DR   HOGENOM; CLU_099476_0_0_1; -.
DR   InParanoid; Q8CCM6; -.
DR   OMA; FRYVFVE; -.
DR   OrthoDB; 1232375at2759; -.
DR   PhylomeDB; Q8CCM6; -.
DR   TreeFam; TF315067; -.
DR   BioGRID-ORCS; 67105; 2 hits in 72 CRISPR screens.
DR   PRO; PR:Q8CCM6; -.
DR   Proteomes; UP000000589; Chromosome 18.
DR   RNAct; Q8CCM6; protein.
DR   Bgee; ENSMUSG00000024645; Expressed in epiblast (generic) and 64 other tissues.
DR   Genevisible; Q8CCM6; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0005744; C:TIM23 mitochondrial import inner membrane translocase complex; ISS:UniProtKB.
DR   GO; GO:0033617; P:mitochondrial cytochrome c oxidase assembly; ISS:UniProtKB.
DR   GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; ISS:UniProtKB.
DR   GO; GO:0030150; P:protein import into mitochondrial matrix; ISS:UniProtKB.
DR   Gene3D; 3.10.450.320; -; 1.
DR   InterPro; IPR013261; Tim21.
DR   InterPro; IPR038552; Tim21_IMS_sf.
DR   PANTHER; PTHR13032; PTHR13032; 1.
DR   Pfam; PF08294; TIM21; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Membrane; Mitochondrion; Protein transport;
KW   Reference proteome; Transit peptide; Translocation; Transmembrane;
KW   Transmembrane helix; Transport.
FT   TRANSIT         1..18
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..244
FT                   /note="Mitochondrial import inner membrane translocase
FT                   subunit Tim21"
FT                   /id="PRO_0000043229"
FT   TRANSMEM        107..127
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          65..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        68..86
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         121..131
FT                   /note="GLLYAIFKELF -> YRPSKHMNAFT (in isoform 2)"
FT                   /id="VSP_060547"
FT   VAR_SEQ         132..244
FT                   /note="Missing (in isoform 2)"
FT                   /id="VSP_060548"
FT   CONFLICT        71
FT                   /note="R -> Q (in Ref. 1; BAB28768)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   244 AA;  27911 MW;  C8648D3401FB5914 CRC64;
     MICAFLRVVQ HAEKLHGSLG RQLLPHFVFT KACFKTQPLR WGLREQKITV QPRTVLRFTQ
     KTFWTQGPDP RKAKEDSTKQ VSIRRNQREE TGVSMSQKVR EAGRDVSYLI VVLFGVGLTG
     GLLYAIFKEL FFSSSPNIIY GKALGKCRTH PEVIGVFGEP LKGYGEMSRR GRRQHVRFSE
     YVNNGLKRIR VKFYIEGSEP GKQGTVHAEV EENPGSGQFE FRYIFVEVTP TRSIIVEDNR
     SEQS
 
 
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