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CRUM3_MOUSE
ID   CRUM3_MOUSE             Reviewed;         113 AA.
AC   Q8QZT4; Q3TJV6;
DT   07-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 132.
DE   RecName: Full=Protein crumbs homolog 3;
DE   Flags: Precursor;
GN   Name=Crb3;
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; TISSUE=Embryo;
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   STRAIN=FVB/N; TISSUE=Kidney, and Placenta;
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   INTERACTION WITH PATJ AND PALS1.
RX   PubMed=12527193; DOI=10.1016/s0378111902010843;
RA   Makarova O., Roh M.H., Liu C.-J., Laurinec S., Margolis B.;
RT   "Mammalian Crumbs3 is a small transmembrane protein linked to protein
RT   associated with Lin-7 (Pals1).";
RL   Gene 302:21-29(2003).
RN   [4]
RP   TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX   PubMed=17920587; DOI=10.1016/j.yexcr.2007.08.025;
RA   Gosens I., Sessa A., den Hollander A.I., Letteboer S.J.F., Belloni V.,
RA   Arends M.L., Le Bivic A., Cremers F.P.M., Broccoli V., Roepman R.;
RT   "FERM protein EPB41L5 is a novel member of the mammalian CRB-MPP5 polarity
RT   complex.";
RL   Exp. Cell Res. 313:3959-3970(2007).
RN   [5]
RP   FUNCTION.
RX   PubMed=21145499; DOI=10.1016/j.devcel.2010.11.012;
RA   Varelas X., Samavarchi-Tehrani P., Narimatsu M., Weiss A., Cockburn K.,
RA   Larsen B.G., Rossant J., Wrana J.L.;
RT   "The Crumbs complex couples cell density sensing to Hippo-dependent control
RT   of the TGF-beta-SMAD pathway.";
RL   Dev. Cell 19:831-844(2010).
RN   [6]
RP   TISSUE SPECIFICITY.
RX   PubMed=26404741; DOI=10.1038/srep14504;
RA   Paniagua A.E., Herranz-Martin S., Jimeno D., Jimeno A.M., Lopez-Benito S.,
RA   Carlos Arevalo J., Velasco A., Aijon J., Lillo C.;
RT   "CRB2 completes a fully expressed Crumbs complex in the Retinal Pigment
RT   Epithelium.";
RL   Sci. Rep. 5:14504-14504(2015).
CC   -!- FUNCTION: Involved in the establishment of cell polarity in mammalian
CC       epithelial cells (By similarity). Regulates the morphogenesis of tight
CC       junctions (PubMed:21145499). Involved in promoting phosphorylation and
CC       cytoplasmic retention of transcriptional coactivators YAP1 and
CC       WWTR1/TAZ which leads to suppression of TGFB1-dependent transcription
CC       of target genes such as CCN2/CTGF, SERPINE1/PAI1, SNAI1/SNAIL1 and
CC       SMAD7 (PubMed:21145499). {ECO:0000250|UniProtKB:Q9BUF7,
CC       ECO:0000269|PubMed:21145499}.
CC   -!- SUBUNIT: Component of a complex composed of CRB3, PALS1 and PATJ (By
CC       similarity). Interacts (via C-terminus) with PALS1 (via PDZ domain)
CC       (PubMed:12527193). Interacts with PARD6A (By similarity). Interacts
CC       (via intracellular domain) with EPB41L5 (By similarity).
CC       {ECO:0000250|UniProtKB:A0A5F4BST2, ECO:0000250|UniProtKB:Q9BUF7,
CC       ECO:0000269|PubMed:12527193}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000250|UniProtKB:Q9BUF7}; Single-pass type I membrane protein
CC       {ECO:0000255}. Cell junction, tight junction
CC       {ECO:0000250|UniProtKB:Q9BUF7}. Note=Localizes primarily to the apical
CC       membrane with a small fraction in the upper part of tight junctions of
CC       epithelial cells. {ECO:0000250|UniProtKB:Q9BUF7}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q8QZT4-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8QZT4-2; Sequence=VSP_013990;
CC   -!- TISSUE SPECIFICITY: Expressed in the apical renal tubules (at protein
CC       level) (PubMed:17920587). Expressed in the retinal pigment epithelium
CC       (PubMed:26404741). {ECO:0000269|PubMed:17920587,
CC       ECO:0000269|PubMed:26404741}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in the branchial arches, optic vesicle
CC       and mesonephric tubules of the kidney at 10.5 dpc (PubMed:17920587).
CC       Expressed in the internal endodermal layer and in the nascent bronchial
CC       tips of the lung at 11.5 dpc (PubMed:17920587).
CC       {ECO:0000269|PubMed:17920587}.
CC   -!- DOMAIN: The PDZ-binding motif is involved in the interactions with
CC       PARD6A and PALS1. {ECO:0000250|UniProtKB:Q9BUF7}.
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DR   EMBL; AK077528; BAC36847.1; -; mRNA.
DR   EMBL; AK167279; BAE39389.1; -; mRNA.
DR   EMBL; BC024462; AAH24462.1; -; mRNA.
DR   EMBL; CK030526; -; NOT_ANNOTATED_CDS; mRNA.
DR   CCDS; CCDS28924.1; -. [Q8QZT4-1]
DR   CCDS; CCDS84327.1; -. [Q8QZT4-2]
DR   RefSeq; NP_001334337.1; NM_001347408.1. [Q8QZT4-2]
DR   RefSeq; NP_808306.1; NM_177638.4. [Q8QZT4-1]
DR   RefSeq; XP_006524228.1; XM_006524165.3.
DR   RefSeq; XP_006524230.1; XM_006524167.3.
DR   AlphaFoldDB; Q8QZT4; -.
DR   SMR; Q8QZT4; -.
DR   CORUM; Q8QZT4; -.
DR   STRING; 10090.ENSMUSP00000094902; -.
DR   GlyGen; Q8QZT4; 1 site.
DR   PhosphoSitePlus; Q8QZT4; -.
DR   MaxQB; Q8QZT4; -.
DR   PaxDb; Q8QZT4; -.
DR   PRIDE; Q8QZT4; -.
DR   ProteomicsDB; 285314; -. [Q8QZT4-1]
DR   ProteomicsDB; 285315; -. [Q8QZT4-2]
DR   Antibodypedia; 3003; 101 antibodies from 16 providers.
DR   DNASU; 224912; -.
DR   Ensembl; ENSMUST00000071826; ENSMUSP00000071729; ENSMUSG00000044279. [Q8QZT4-1]
DR   Ensembl; ENSMUST00000097299; ENSMUSP00000094902; ENSMUSG00000044279. [Q8QZT4-1]
DR   Ensembl; ENSMUST00000163763; ENSMUSP00000132502; ENSMUSG00000044279. [Q8QZT4-1]
DR   Ensembl; ENSMUST00000169543; ENSMUSP00000125760; ENSMUSG00000044279. [Q8QZT4-2]
DR   GeneID; 224912; -.
DR   KEGG; mmu:224912; -.
DR   UCSC; uc008ddw.1; mouse. [Q8QZT4-1]
DR   CTD; 92359; -.
DR   MGI; MGI:2670904; Crb3.
DR   VEuPathDB; HostDB:ENSMUSG00000044279; -.
DR   eggNOG; ENOG502S74B; Eukaryota.
DR   GeneTree; ENSGT00950000183101; -.
DR   HOGENOM; CLU_2120342_0_0_1; -.
DR   InParanoid; Q8QZT4; -.
DR   OMA; WGQVWGQ; -.
DR   OrthoDB; 1551105at2759; -.
DR   PhylomeDB; Q8QZT4; -.
DR   TreeFam; TF338371; -.
DR   BioGRID-ORCS; 224912; 2 hits in 39 CRISPR screens.
DR   ChiTaRS; Crb3; mouse.
DR   PRO; PR:Q8QZT4; -.
DR   Proteomes; UP000000589; Chromosome 17.
DR   RNAct; Q8QZT4; protein.
DR   Bgee; ENSMUSG00000044279; Expressed in cleaving embryo and 164 other tissues.
DR   ExpressionAtlas; Q8QZT4; baseline and differential.
DR   Genevisible; Q8QZT4; MM.
DR   GO; GO:0045177; C:apical part of cell; IDA:MGI.
DR   GO; GO:0016324; C:apical plasma membrane; ISA:MGI.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0030054; C:cell junction; ISO:MGI.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR   GO; GO:0035003; C:subapical complex; IDA:MGI.
DR   GO; GO:0019904; F:protein domain specific binding; ISO:MGI.
DR   GO; GO:0017124; F:SH3 domain binding; ISO:MGI.
DR   GO; GO:0045216; P:cell-cell junction organization; ISA:MGI.
DR   GO; GO:0045198; P:establishment of epithelial cell apical/basal polarity; ISA:MGI.
DR   GO; GO:1901890; P:positive regulation of cell junction assembly; IMP:UniProtKB.
DR   GO; GO:0072659; P:protein localization to plasma membrane; ISO:MGI.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell junction; Cell membrane; Glycoprotein; Membrane;
KW   Reference proteome; Signal; Tight junction; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..113
FT                   /note="Protein crumbs homolog 3"
FT                   /id="PRO_0000021006"
FT   TOPO_DOM        25..49
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        50..70
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        71..113
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   REGION          23..44
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          77..113
FT                   /note="Interaction with EPB41L5"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUF7"
FT   REGION          80..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           110..113
FT                   /note="PDZ-binding"
FT   COMPBIAS        24..42
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        31
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         94..113
FT                   /note="VGARAPPPPNLKLPPEERLI -> FSHAAAEARAPQDSKEPVRGCLPI (in
FT                   isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_013990"
SQ   SEQUENCE   113 AA;  11921 MW;  1C94A072057F1E3E CRC64;
     MATPGLGVLL AFGLPMLPSG WSLTAPDPFT NSTTQPPGDE SNGGLSSGAI VAITVVFSIL
     GVLLIAVGLF LLMRKLREKR QTEGTYRPSS EEQVGARAPP PPNLKLPPEE RLI
 
 
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