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CRUM3_CANLF
ID   CRUM3_CANLF             Reviewed;         123 AA.
AC   A0A5F4BST2;
DT   02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT   11-DEC-2019, sequence version 1.
DT   03-AUG-2022, entry version 11.
DE   RecName: Full=Protein crumbs homolog 3 {ECO:0000305};
DE   Flags: Precursor;
GN   Name=CRB3 {ECO:0000250|UniProtKB:Q9BUF7};
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615 {ECO:0000312|Proteomes:UP000002254};
RN   [1] {ECO:0000312|Proteomes:UP000002254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer {ECO:0000312|Proteomes:UP000002254};
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
RN   [2] {ECO:0000305}
RP   IDENTIFICATION IN A COMPLEX WITH PALS1 AND PATJ, AND SUBCELLULAR LOCATION.
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   [3] {ECO:0000305}
RP   SUBCELLULAR LOCATION.
RX   PubMed=12771187; DOI=10.1242/jcs.00500;
RA   Roh M.H., Fan S., Liu C.-J., Margolis B.;
RT   "The Crumbs3-Pals1 complex participates in the establishment of polarity in
RT   mammalian epithelial cells.";
RL   J. Cell Sci. 116:2895-2906(2003).
CC   -!- FUNCTION: Involved in the establishment of cell polarity in mammalian
CC       epithelial cells (By similarity). Regulates the morphogenesis of tight
CC       junctions (By similarity). 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 (By similarity). {ECO:0000250|UniProtKB:Q8QZT4,
CC       ECO:0000250|UniProtKB:Q9BUF7}.
CC   -!- SUBUNIT: Component of a complex composed of CRB3, PALS1 and PATJ
CC       (PubMed:12527193). Interacts (via C-terminus) with PALS1 (via PDZ
CC       domain) (By similarity). Interacts with PARD6A (By similarity).
CC       Interacts (via intracellular domain) with EPB41L5 (By similarity).
CC       {ECO:0000250|UniProtKB:Q9BUF7, ECO:0000269|PubMed:12527193}.
CC   -!- SUBCELLULAR LOCATION: Apical cell membrane
CC       {ECO:0000269|PubMed:12527193, ECO:0000269|PubMed:12771187}; Single-pass
CC       type I membrane protein {ECO:0000255}. Cell junction, tight junction
CC       {ECO:0000269|PubMed:12527193}. 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   -!- 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; AAEX03012494; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_005633034.1; XM_005632977.2.
DR   RefSeq; XP_013977398.1; XM_014121923.1.
DR   RefSeq; XP_013977399.1; XM_014121924.1.
DR   AlphaFoldDB; A0A5F4BST2; -.
DR   SMR; A0A5F4BST2; -.
DR   STRING; 9615.ENSCAFP00000044539; -.
DR   Ensembl; ENSCAFT00030038046; ENSCAFP00030033190; ENSCAFG00030020725.
DR   Ensembl; ENSCAFT00040045568; ENSCAFP00040039782; ENSCAFG00040024468.
DR   Ensembl; ENSCAFT00845019111; ENSCAFP00845014929; ENSCAFG00845010829.
DR   GeneID; 100855851; -.
DR   KEGG; cfa:100855851; -.
DR   CTD; 92359; -.
DR   VEuPathDB; HostDB:ENSCAFG00845010829; -.
DR   GeneTree; ENSGT00950000183101; -.
DR   Proteomes; UP000002254; Chromosome 20.
DR   Bgee; ENSCAFG00000049307; Expressed in jejunum and 36 other tissues.
DR   GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0035003; C:subapical complex; IEA:Ensembl.
DR   GO; GO:0017124; F:SH3 domain binding; IEA:Ensembl.
DR   GO; GO:1901890; P:positive regulation of cell junction assembly; IEA:Ensembl.
DR   GO; GO:0072659; P:protein localization to plasma membrane; IEA:Ensembl.
PE   1: Evidence at protein level;
KW   Cell junction; Cell membrane; Glycoprotein; Membrane; Reference proteome;
KW   Signal; Tight junction; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000255"
FT   CHAIN           27..123
FT                   /note="Protein crumbs homolog 3"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000451439"
FT   TOPO_DOM        27..59
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        60..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        81..120
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   REGION          87..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOTIF           119..123
FT                   /note="PDZ-binding"
FT                   /evidence="ECO:0000305"
FT   CARBOHYD        36
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BUF7"
SQ   SEQUENCE   123 AA;  12989 MW;  CCF89668EC0C1AB2 CRC64;
     MASPGLGLLL ALGLPLLPAR WGRAWGQTLD PHVNENGTIT PSAPGSGSNG ALSQEAITAI
     IVVFSLLAAV LLAVGLVLLL RKLREKRQTQ GTYRPSSEEQ FNHAAEARAP QDSKETVRGC
     LPI
 
 
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