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MUC20_MOUSE
ID   MUC20_MOUSE             Reviewed;         656 AA.
AC   Q8BUE7; Q76I84; Q8R0X0;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 116.
DE   RecName: Full=Mucin-20;
DE            Short=MUC-20;
DE   Flags: Precursor;
GN   Name=Muc20;
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 [MRNA], AND TISSUE SPECIFICITY.
RC   TISSUE=Kidney;
RX   PubMed=14565953; DOI=10.1074/jbc.m304558200;
RA   Higuchi T., Orita T., Nakanishi S., Katsuya K., Watanabe H., Yamasaki Y.,
RA   Waga I., Nanayama T., Yamamoto Y., Munger W., Sun H.-W., Falk R.J.,
RA   Jennette J.C., Alcorta D.A., Li H., Yamamoto T., Saito Y., Nakamura M.;
RT   "Molecular cloning, genomic structure, and expression analysis of MUC20, a
RT   novel mucin protein, up-regulated in injured kidney.";
RL   J. Biol. Chem. 279:1968-1979(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Kidney;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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   [4]
RP   INTERACTION WITH MET.
RX   PubMed=15314156; DOI=10.1128/mcb.24.17.7456-7468.2004;
RA   Higuchi T., Orita T., Katsuya K., Yamasaki Y., Akiyama K., Li H.,
RA   Yamamoto T., Saito Y., Nakamura M.;
RT   "MUC20 suppresses the hepatocyte growth factor-induced Grb2-Ras pathway by
RT   binding to a multifunctional docking site of met.";
RL   Mol. Cell. Biol. 24:7456-7468(2004).
CC   -!- FUNCTION: May regulate MET signaling cascade. Seems to decrease
CC       hepatocyte growth factor (HGF)-induced transient MAPK activation.
CC       Blocks GRB2 recruitment to MET thus suppressing the GRB2-RAS pathway.
CC       Inhibits HGF-induced proliferation of MMP1 and MMP9 expression (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with MET; oligomerization increases affinity for
CC       MET. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. Apical cell membrane
CC       {ECO:0000250}. Basolateral cell membrane {ECO:0000250}. Cell
CC       projection, microvillus membrane {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in kidney. Up-regulated in renal
CC       tissues during renal injury. {ECO:0000269|PubMed:14565953}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH26367.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC   -!- WEB RESOURCE: Name=Mucin database;
CC       URL="http://www.medkem.gu.se/mucinbiology/databases/";
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DR   EMBL; AB098732; BAD06719.1; -; mRNA.
DR   EMBL; AK085640; BAC39492.1; -; mRNA.
DR   EMBL; AK165477; BAE38212.1; -; mRNA.
DR   EMBL; BC026367; AAH26367.1; ALT_INIT; mRNA.
DR   CCDS; CCDS49830.1; -.
DR   RefSeq; NP_001139346.1; NM_001145874.1.
DR   RefSeq; NP_666183.2; NM_146071.2.
DR   AlphaFoldDB; Q8BUE7; -.
DR   BioGRID; 230247; 1.
DR   STRING; 10090.ENSMUSP00000110769; -.
DR   GlyGen; Q8BUE7; 2 sites.
DR   iPTMnet; Q8BUE7; -.
DR   PhosphoSitePlus; Q8BUE7; -.
DR   PaxDb; Q8BUE7; -.
DR   PRIDE; Q8BUE7; -.
DR   ProteomicsDB; 287524; -.
DR   Antibodypedia; 35139; 211 antibodies from 24 providers.
DR   DNASU; 224116; -.
DR   Ensembl; ENSMUST00000041123; ENSMUSP00000041221; ENSMUSG00000035638.
DR   GeneID; 224116; -.
DR   KEGG; mmu:224116; -.
DR   UCSC; uc007yzi.2; mouse.
DR   CTD; 200958; -.
DR   MGI; MGI:2385039; Muc20.
DR   VEuPathDB; HostDB:ENSMUSG00000035638; -.
DR   eggNOG; ENOG502SVUK; Eukaryota.
DR   GeneTree; ENSGT00730000111453; -.
DR   HOGENOM; CLU_026298_0_0_1; -.
DR   InParanoid; Q8BUE7; -.
DR   OrthoDB; 878577at2759; -.
DR   PhylomeDB; Q8BUE7; -.
DR   Reactome; R-MMU-8851805; MET activates RAS signaling.
DR   Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR   Reactome; R-MMU-977068; Termination of O-glycan biosynthesis.
DR   BioGRID-ORCS; 224116; 0 hits in 72 CRISPR screens.
DR   PRO; PR:Q8BUE7; -.
DR   Proteomes; UP000000589; Chromosome 16.
DR   RNAct; Q8BUE7; protein.
DR   Bgee; ENSMUSG00000035638; Expressed in lumbar subsegment of spinal cord and 50 other tissues.
DR   ExpressionAtlas; Q8BUE7; baseline and differential.
DR   Genevisible; Q8BUE7; MM.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0009925; C:basal plasma membrane; ISO:MGI.
DR   GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0031528; C:microvillus membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005741; C:mitochondrial outer membrane; ISS:UniProtKB.
DR   GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR   GO; GO:0048012; P:hepatocyte growth factor receptor signaling pathway; IDA:MGI.
DR   GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR   GO; GO:0043410; P:positive regulation of MAPK cascade; IPI:MGI.
DR   InterPro; IPR034551; MUC20.
DR   PANTHER; PTHR37358; PTHR37358; 2.
PE   1: Evidence at protein level;
KW   Cell membrane; Cell projection; Glycoprotein; Membrane; Reference proteome;
KW   Repeat; Secreted; Signal.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000255"
FT   CHAIN           22..656
FT                   /note="Mucin-20"
FT                   /id="PRO_0000317470"
FT   REPEAT          180..188
FT                   /note="1"
FT   REPEAT          189..197
FT                   /note="2"
FT   REPEAT          198..206
FT                   /note="3"
FT   REPEAT          210..218
FT                   /note="4"
FT   REPEAT          219..227
FT                   /note="5"
FT   REGION          85..125
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          159..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          180..227
FT                   /note="Approximate repeats"
FT   REGION          329..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..603
FT                   /note="Involved in oligomerization"
FT                   /evidence="ECO:0000250"
FT   REGION          560..592
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          604..656
FT                   /note="Interaction with MET"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        366
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        570
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        99
FT                   /note="T -> A (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        199
FT                   /note="T -> I (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        215
FT                   /note="P -> L (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        219
FT                   /note="T -> A (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="T -> K (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        273
FT                   /note="A -> T (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        293
FT                   /note="S -> P (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        297
FT                   /note="V -> I (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        329
FT                   /note="Y -> H (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        374
FT                   /note="N -> T (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        391
FT                   /note="A -> V (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        509
FT                   /note="A -> T (in Ref. 1; BAD06719)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   656 AA;  68720 MW;  5A0BECDE6F3297DA CRC64;
     MGSVWGLAVP LLVFCWKVGV SVSSPGLDIS RSVPLVTTNN MEVSTFTQRD RPSSERAFQT
     TNLIQYVPLD TQTLSTESAS NALSATSISS EVNSRDTQTT SFVTKTRKTH TTTPAASSLE
     AQTTSPNLST LNIQITSPIA SSLDAQTIFP VSLSLSTQTT SPAPSFLDTQ TTSPEPSSLT
     TSPAPSSLIT SPTPSSLTTS PAPSFLDTQT TSPAPSSLTT SPAPSSLDTQ TISPIELTLK
     TQTISTVTET RTVSIRIPSD LTVMHTIPTE TLAPSNSPRT GMSTVQTGTV WDSIEAVFDT
     LCTDDSSEEA RKITVDLLTL AHTSTEVEYL SSESSSSSDS SAGVLSSSRV LGPDSATPAK
     GLVAFNITHI KLSNCITEIE TTITISGAPG ASLSPTEATA ALFTSEILTL PPPTEAKPIF
     PETTSLSGIL STAGTPALAT TLEGTVSTSA ITESETAVAQ TLTSVGTSVT VRRNPLENTS
     TLSIETQSHT EVLGTITVPM VAGSTMGEAA SFVSFTALDS SSLSVVVTTE SSATSETLTT
     GNTTNSSFLT ESHPPFSIYS TTASTSKNPN ITLTKTTASP KPPTHPTTSA STAWIRKTTK
     HDPGEDGGFL LVRLTVASPK DLTEHNAREK LMNQLRRELH ARMPLVHMSF LSIRRG
 
 
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