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MUC15_MOUSE
ID   MUC15_MOUSE             Reviewed;         331 AA.
AC   Q8C6Z1; Q3UQC4; Q6XYQ9; Q7TMH6; Q8CE82;
DT   19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=Mucin-15;
DE            Short=MUC-15;
DE   Flags: Precursor;
GN   Name=Muc15;
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].
RC   TISSUE=Lactating mammary gland;
RA   Bierie B., Cui K., Miyoshi K., Tang W., Hennighausen L.;
RT   "Cloning and characterization of two mouse MUC15 splice forms.";
RL   Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Mammary gland, 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 195-331.
RC   STRAIN=C57BL/6J; 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).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}.
CC   -!- PTM: Highly glycosylated (N- and O-linked carbohydrates).
CC       {ECO:0000250}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAO45176.1; Type=Frameshift; Evidence={ECO:0000305};
CC       Sequence=AAO45177.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AY198336; AAO45176.1; ALT_FRAME; mRNA.
DR   EMBL; AY198337; AAO45177.1; ALT_FRAME; mRNA.
DR   EMBL; AK028832; BAC26143.1; -; mRNA.
DR   EMBL; AK052840; BAC35171.1; -; mRNA.
DR   EMBL; AK142590; BAE25118.1; -; mRNA.
DR   EMBL; BC055469; AAH55469.1; -; mRNA.
DR   CCDS; CCDS16513.1; -.
DR   RefSeq; NP_001277715.1; NM_001290786.1.
DR   RefSeq; NP_766567.1; NM_172979.3.
DR   AlphaFoldDB; Q8C6Z1; -.
DR   STRING; 10090.ENSMUSP00000106645; -.
DR   GlyGen; Q8C6Z1; 12 sites.
DR   iPTMnet; Q8C6Z1; -.
DR   PhosphoSitePlus; Q8C6Z1; -.
DR   PaxDb; Q8C6Z1; -.
DR   PRIDE; Q8C6Z1; -.
DR   ProteomicsDB; 287520; -.
DR   Antibodypedia; 12684; 143 antibodies from 28 providers.
DR   DNASU; 269328; -.
DR   Ensembl; ENSMUST00000090332; ENSMUSP00000087805; ENSMUSG00000050808.
DR   Ensembl; ENSMUST00000111016; ENSMUSP00000106645; ENSMUSG00000050808.
DR   GeneID; 269328; -.
DR   KEGG; mmu:269328; -.
DR   UCSC; uc008lmz.2; mouse.
DR   CTD; 143662; -.
DR   MGI; MGI:2442110; Muc15.
DR   VEuPathDB; HostDB:ENSMUSG00000050808; -.
DR   eggNOG; ENOG502S7P0; Eukaryota.
DR   GeneTree; ENSGT00390000001698; -.
DR   HOGENOM; CLU_054055_0_0_1; -.
DR   InParanoid; Q8C6Z1; -.
DR   OMA; PDEWLTT; -.
DR   OrthoDB; 1169762at2759; -.
DR   PhylomeDB; Q8C6Z1; -.
DR   TreeFam; TF338656; -.
DR   Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR   Reactome; R-MMU-977068; Termination of O-glycan biosynthesis.
DR   BioGRID-ORCS; 269328; 1 hit in 71 CRISPR screens.
DR   PRO; PR:Q8C6Z1; -.
DR   Proteomes; UP000000589; Chromosome 2.
DR   RNAct; Q8C6Z1; protein.
DR   Bgee; ENSMUSG00000050808; Expressed in epithelium of cochlear duct and 61 other tissues.
DR   ExpressionAtlas; Q8C6Z1; baseline and differential.
DR   Genevisible; Q8C6Z1; MM.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   InterPro; IPR031371; Mucin-15.
DR   PANTHER; PTHR45427; PTHR45427; 1.
DR   Pfam; PF15672; Mucin15; 1.
PE   2: Evidence at transcript level;
KW   Glycoprotein; Membrane; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..331
FT                   /note="Mucin-15"
FT                   /id="PRO_0000019289"
FT   TOPO_DOM        23..233
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        255..331
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          124..186
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          302..331
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        124..163
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        164..178
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        30
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        44
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        54
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        75
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        84
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        145
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        152
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        215
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        222
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        308
FT                   /note="M -> L (in Ref. 3; AAH55469)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        327
FT                   /note="L -> F (in Ref. 3; AAH55469)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   331 AA;  36383 MW;  A53CC7F6265591D0 CRC64;
     MLTLAKIALI SSLFISLPFA RPQKQNPRRN VTQHTIEDVK IMRNNSIHLE RSINVTSENG
     SDISNLMVTT PSPLNLSTTF RTTNSTRTWL MTSSSESSRP SSTYSVPPLV QGFVSKLPLN
     SSTADANPLQ VSEHSNSTNS PSPENFTWSL DNDTMNSPED ISTTVRPFPP PPKTTPVTPF
     TAEPTEWLPT NNDNFAGFTP YQEKTTLQPT LKFTNNSKLF PNTSDTPKEN KNTGIVFGAI
     LGAILGASLL SLVGYLLCGQ RKTDSFSHRR LYDDRNEPVL RLDNAPEPYD VNFGNSSYYN
     PAVSDSSMPE GGESLQDGIP MDAIPPLRPS I
 
 
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