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TM237_MOUSE
ID   TM237_MOUSE             Reviewed;         427 AA.
AC   Q3V0J1; B2RVK7; Q3TIS2;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 104.
DE   RecName: Full=Transmembrane protein 237;
DE   AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 4 protein homolog;
GN   Name=Tmem237; Synonyms=Als2cr4;
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; TISSUE=Placenta, and Testis;
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 GENOMIC DNA].
RC   STRAIN=C57BL/6J;
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   [4]
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   [5]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=22152675; DOI=10.1016/j.ajhg.2011.11.005;
RA   Huang L., Szymanska K., Jensen V.L., Janecke A.R., Innes A.M., Davis E.E.,
RA   Frosk P., Li C., Willer J.R., Chodirker B.N., Greenberg C.R., McLeod D.R.,
RA   Bernier F.P., Chudley A.E., Muller T., Shboul M., Logan C.V., Loucks C.M.,
RA   Beaulieu C.L., Bowie R.V., Bell S.M., Adkins J., Zuniga F.I., Ross K.D.,
RA   Wang J., Ban M.R., Becker C., Nurnberg P., Douglas S., Craft C.M.,
RA   Akimenko M.A., Hegele R.A., Ober C., Utermann G., Bolz H.J., Bulman D.E.,
RA   Katsanis N., Blacque O.E., Doherty D., Parboosingh J.S., Leroux M.R.,
RA   Johnson C.A., Boycott K.M.;
RT   "TMEM237 is mutated in individuals with a Joubert syndrome related disorder
RT   and expands the role of the TMEM family at the ciliary transition zone.";
RL   Am. J. Hum. Genet. 89:713-730(2011).
CC   -!- FUNCTION: Component of the transition zone in primary cilia. Required
CC       for ciliogenesis. {ECO:0000269|PubMed:22152675}.
CC   -!- SUBUNIT: Part of the tectonic-like complex (also named B9 complex).
CC       Interacts with TMEM107. {ECO:0000250|UniProtKB:Q96Q45}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}. Cell projection, cilium
CC       {ECO:0000269|PubMed:22152675}. Note=Localizes at the proximal region of
CC       primary cilia were observed, consistent with localization to the
CC       transition zone.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q3V0J1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q3V0J1-2; Sequence=VSP_042384, VSP_042386;
CC       Name=3;
CC         IsoId=Q3V0J1-3; Sequence=VSP_042385, VSP_042386;
CC   -!- SIMILARITY: Belongs to the TMEM237 family. {ECO:0000305}.
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DR   EMBL; AK133112; BAE21513.1; -; mRNA.
DR   EMBL; AK167733; BAE39774.1; -; mRNA.
DR   EMBL; AC133162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC147243; AAI47244.1; -; mRNA.
DR   EMBL; BC147244; AAI47245.1; -; mRNA.
DR   CCDS; CCDS14983.1; -. [Q3V0J1-2]
DR   CCDS; CCDS14984.1; -. [Q3V0J1-3]
DR   CCDS; CCDS87834.1; -. [Q3V0J1-1]
DR   RefSeq; NP_001028621.1; NM_001033449.1. [Q3V0J1-2]
DR   RefSeq; NP_001032901.1; NM_001037812.2. [Q3V0J1-3]
DR   AlphaFoldDB; Q3V0J1; -.
DR   IntAct; Q3V0J1; 1.
DR   STRING; 10090.ENSMUSP00000092522; -.
DR   iPTMnet; Q3V0J1; -.
DR   PhosphoSitePlus; Q3V0J1; -.
DR   EPD; Q3V0J1; -.
DR   MaxQB; Q3V0J1; -.
DR   PeptideAtlas; Q3V0J1; -.
DR   PRIDE; Q3V0J1; -.
DR   ProteomicsDB; 260690; -. [Q3V0J1-1]
DR   ProteomicsDB; 260691; -. [Q3V0J1-2]
DR   ProteomicsDB; 260692; -. [Q3V0J1-3]
DR   Antibodypedia; 47646; 103 antibodies from 22 providers.
DR   Ensembl; ENSMUST00000087475; ENSMUSP00000084745; ENSMUSG00000038079. [Q3V0J1-3]
DR   Ensembl; ENSMUST00000094917; ENSMUSP00000092522; ENSMUSG00000038079. [Q3V0J1-2]
DR   Ensembl; ENSMUST00000186794; ENSMUSP00000139823; ENSMUSG00000038079. [Q3V0J1-1]
DR   GeneID; 381259; -.
DR   KEGG; mmu:381259; -.
DR   UCSC; uc007bdd.1; mouse. [Q3V0J1-3]
DR   UCSC; uc007bde.1; mouse. [Q3V0J1-2]
DR   UCSC; uc007bdf.1; mouse. [Q3V0J1-1]
DR   CTD; 65062; -.
DR   MGI; MGI:2138365; Tmem237.
DR   VEuPathDB; HostDB:ENSMUSG00000038079; -.
DR   eggNOG; ENOG502QTW0; Eukaryota.
DR   GeneTree; ENSGT00390000005159; -.
DR   HOGENOM; CLU_061097_0_0_1; -.
DR   InParanoid; Q3V0J1; -.
DR   OMA; THCACAR; -.
DR   OrthoDB; 1428687at2759; -.
DR   PhylomeDB; Q3V0J1; -.
DR   TreeFam; TF329703; -.
DR   BioGRID-ORCS; 381259; 0 hits in 72 CRISPR screens.
DR   ChiTaRS; Tmem237; mouse.
DR   PRO; PR:Q3V0J1; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q3V0J1; protein.
DR   Bgee; ENSMUSG00000038079; Expressed in choroid plexus epithelium and 228 other tissues.
DR   ExpressionAtlas; Q3V0J1; baseline and differential.
DR   Genevisible; Q3V0J1; MM.
DR   GO; GO:0035869; C:ciliary transition zone; IDA:UniProtKB.
DR   GO; GO:0120199; C:cone photoreceptor outer segment; IDA:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0032391; C:photoreceptor connecting cilium; IDA:MGI.
DR   GO; GO:0120200; C:rod photoreceptor outer segment; IDA:MGI.
DR   GO; GO:0060271; P:cilium assembly; IMP:UniProtKB.
DR   GO; GO:0030111; P:regulation of Wnt signaling pathway; IMP:UniProtKB.
DR   InterPro; IPR029409; TMEM237.
DR   PANTHER; PTHR28388; PTHR28388; 1.
DR   Pfam; PF15383; TMEM237; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell projection; Cilium;
KW   Cilium biogenesis/degradation; Membrane; Phosphoprotein;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..427
FT                   /note="Transmembrane protein 237"
FT                   /id="PRO_0000076170"
FT   TRANSMEM        252..272
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        290..310
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        325..345
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        375..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          1..172
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..57
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        79..116
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        135..157
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         25
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96Q45"
FT   MOD_RES         72
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q96Q45"
FT   VAR_SEQ         1..14
FT                   /note="MRDDSGPPLEEDQA -> MTSRETVGEPPPLLGTPADAE (in isoform
FT                   2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042384"
FT   VAR_SEQ         1..14
FT                   /note="MRDDSGPPLEEDQA -> MGKKQVVSEPQ (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_042385"
FT   VAR_SEQ         29..49
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072"
FT                   /id="VSP_042386"
SQ   SEQUENCE   427 AA;  47343 MW;  A8612DBBCE7FA7E1 CRC64;
     MRDDSGPPLE EDQARPPRAL PPVPSAIQVC SSFVENNSRM DQQDDLVGED DIPLSHPKKK
     KSRTKSSLAT ASSEGHAEPV VNRRAEGSEP PAAELKEHPE APAPRRQKKI RPPPELETSL
     TERPSSPSLL RNENGIDAEP REEAVIPKPR RKAKKTQPAE PQYASELGVE DEDILTDEQS
     TLEHHSRFTA PTGVSQPVGK VFVEKSRRFQ AADRSELIKT TENIDVSMDV KPSWTTRDVA
     LSVHRAFRMV GLFSHGFLAG CAVWNTVVIY VLAGDQLSNV SNLLQQYKPL AYPFQSLLYL
     LLALSTVSAF DRTDFAKISV AIRNFLALEP TALASFLYFT ALILSLSQQM TSDRIHLYEP
     SVNGSLWAAE AEEPILVPWI IVNLVVALLV GLSWLFLSYR PGMDLSEELM FFSDVDEHPE
     TGTKASP
 
 
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