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T120B_MOUSE
ID   T120B_MOUSE             Reviewed;         339 AA.
AC   Q3TA38; Q14BK6; Q8R243;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 105.
DE   RecName: Full=Transmembrane protein 120B {ECO:0000305};
GN   Name=Tmem120b {ECO:0000303|PubMed:26024229, ECO:0000303|PubMed:32084332,
GN   ECO:0000312|MGI:MGI:3603158};
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] (ISOFORM 1).
RC   STRAIN=C57BL/6J, and NOD; TISSUE=Inner ear, 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 1 AND 2).
RC   TISSUE=Mammary tumor;
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   FUNCTION, SUBCELLULAR LOCATION, INDUCTION, AND TISSUE SPECIFICITY.
RX   PubMed=26024229; DOI=10.1371/journal.pone.0127712;
RA   Batrakou D.G., de Las Heras J.I., Czapiewski R., Mouras R., Schirmer E.C.;
RT   "TMEM120A and B: nuclear envelope transmembrane proteins important for
RT   adipocyte differentiation.";
RL   PLoS ONE 10:E0127712-E0127712(2015).
RN   [4]
RP   FUNCTION.
RX   PubMed=32084332; DOI=10.1016/j.cell.2020.01.033;
RA   Beaulieu-Laroche L., Christin M., Donoghue A., Agosti F., Yousefpour N.,
RA   Petitjean H., Davidova A., Stanton C., Khan U., Dietz C., Faure E.,
RA   Fatima T., MacPherson A., Mouchbahani-Constance S., Bisson D.G.,
RA   Haglund L., Ouellet J.A., Stone L.S., Samson J., Smith M.J., Ask K.,
RA   Ribeiro-da-Silva A., Blunck R., Poole K., Bourinet E., Sharif-Naeini R.;
RT   "TACAN is an ion channel involved in sensing mechanical pain.";
RL   Cell 0:0-0(2020).
CC   -!- FUNCTION: Necessary for efficient adipogenesis (PubMed:26024229). Does
CC       not show ion channel activity (PubMed:32084332).
CC       {ECO:0000269|PubMed:26024229, ECO:0000269|PubMed:32084332}.
CC   -!- SUBUNIT: Heterooligomer with TMEM120A. {ECO:0000269|PubMed:26024229}.
CC   -!- SUBCELLULAR LOCATION: Nucleus inner membrane
CC       {ECO:0000269|PubMed:26024229}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q3TA38-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3TA38-2; Sequence=VSP_029233;
CC   -!- TISSUE SPECIFICITY: Expressed in inguinal and subcutaneous white
CC       adipose tissue and in brown adipose tissue.
CC       {ECO:0000269|PubMed:26024229}.
CC   -!- INDUCTION: Up-regulated during adipocyte differentiation.
CC       {ECO:0000269|PubMed:26024229}.
CC   -!- SIMILARITY: Belongs to the TMEM120 family. {ECO:0000305}.
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DR   EMBL; AK158123; BAE34369.1; -; mRNA.
DR   EMBL; AK172110; BAE42832.1; -; mRNA.
DR   EMBL; BC022593; AAH22593.2; -; mRNA.
DR   EMBL; BC115785; AAI15786.1; -; mRNA.
DR   EMBL; BC118014; AAI18015.1; -; mRNA.
DR   CCDS; CCDS39262.1; -. [Q3TA38-1]
DR   RefSeq; NP_001034812.1; NM_001039723.2. [Q3TA38-1]
DR   AlphaFoldDB; Q3TA38; -.
DR   SMR; Q3TA38; -.
DR   STRING; 10090.ENSMUSP00000068551; -.
DR   iPTMnet; Q3TA38; -.
DR   PhosphoSitePlus; Q3TA38; -.
DR   SwissPalm; Q3TA38; -.
DR   MaxQB; Q3TA38; -.
DR   PaxDb; Q3TA38; -.
DR   PRIDE; Q3TA38; -.
DR   ProteomicsDB; 254514; -. [Q3TA38-1]
DR   ProteomicsDB; 254515; -. [Q3TA38-2]
DR   Antibodypedia; 2742; 42 antibodies from 14 providers.
DR   Ensembl; ENSMUST00000067505; ENSMUSP00000068551; ENSMUSG00000054434. [Q3TA38-1]
DR   Ensembl; ENSMUST00000111619; ENSMUSP00000107246; ENSMUSG00000054434. [Q3TA38-2]
DR   GeneID; 330189; -.
DR   KEGG; mmu:330189; -.
DR   UCSC; uc008znc.1; mouse. [Q3TA38-1]
DR   UCSC; uc012edc.1; mouse. [Q3TA38-2]
DR   CTD; 144404; -.
DR   MGI; MGI:3603158; Tmem120b.
DR   VEuPathDB; HostDB:ENSMUSG00000054434; -.
DR   eggNOG; KOG4758; Eukaryota.
DR   GeneTree; ENSGT00390000007848; -.
DR   HOGENOM; CLU_048749_1_1_1; -.
DR   InParanoid; Q3TA38; -.
DR   OMA; YGFQAYN; -.
DR   OrthoDB; 916768at2759; -.
DR   PhylomeDB; Q3TA38; -.
DR   TreeFam; TF313552; -.
DR   BioGRID-ORCS; 330189; 0 hits in 72 CRISPR screens.
DR   ChiTaRS; Tmem120b; mouse.
DR   PRO; PR:Q3TA38; -.
DR   Proteomes; UP000000589; Chromosome 5.
DR   RNAct; Q3TA38; protein.
DR   Bgee; ENSMUSG00000054434; Expressed in brown adipose tissue and 218 other tissues.
DR   ExpressionAtlas; Q3TA38; baseline and differential.
DR   Genevisible; Q3TA38; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IBA:GO_Central.
DR   GO; GO:0005637; C:nuclear inner membrane; IDA:UniProtKB.
DR   GO; GO:0045444; P:fat cell differentiation; IMP:UniProtKB.
DR   GO; GO:0051291; P:protein heterooligomerization; IDA:UniProtKB.
DR   InterPro; IPR012926; TACAN/TMEM120B.
DR   PANTHER; PTHR21433; PTHR21433; 1.
DR   Pfam; PF07851; TMPIT; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Coiled coil; Membrane; Nucleus; Reference proteome;
KW   Transmembrane; Transmembrane helix.
FT   CHAIN           1..339
FT                   /note="Transmembrane protein 120B"
FT                   /id="PRO_0000309530"
FT   TRANSMEM        102..124
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        132..152
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        159..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        187..207
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        270..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        302..322
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   COILED          1..67
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         64..102
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_029233"
FT   CONFLICT        211
FT                   /note="I -> T (in Ref. 2; AAI15786)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   339 AA;  40407 MW;  56FA0CF4045EDD76 CRC64;
     MSGQLERCER EWHELEGEFQ ELQETHRIYK QKLEELTSLQ TLCSTSISKQ KRHLKDLKHT
     LQRYKRHSSH EEAALIQQMT ANIKERQNVF FDMEAYLPKK NGLYLNLVLG NVSVTLLSNQ
     AKFAYKDEYE KFKLYLTIIL LLGAVACRFV LHYRVTDEVF NFLLVWYYCT LTIRESILIS
     NGSRIKGWWV SHHYVSTFLS GVMLTWPNGL IYQKFRNQFL AFSIFQSCVQ FLQYYYQRGC
     LYRLRALGER NHLDLTVEGF QSWMWRGLTF LLPFLFCGHF WQLYNAVTLF ELSTHEECKE
     WQVFVLALTF LILFLGNFLT TLKVVHAKLH KNRNKTKQP
 
 
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