PAR3L_MOUSE
ID PAR3L_MOUSE Reviewed; 1203 AA.
AC Q9CSB4; Q5SV53;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 2.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Partitioning defective 3 homolog B;
DE AltName: Full=Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 19 protein homolog;
DE AltName: Full=PAR3-beta;
DE AltName: Full=Partitioning defective 3-like protein;
DE Short=PAR3-L protein;
GN Name=Pard3b; Synonyms=Als2cr19, Par3l;
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 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-213 (ISOFORM 2).
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746 AND SER-749, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-346; SER-352; SER-635;
RP SER-710; SER-728; SER-730; SER-746; SER-749; THR-810 AND SER-1088, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [5]
RP STRUCTURE BY NMR OF 478-591.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of PDZ domain in protein XP_110852.";
RL Submitted (NOV-2004) to the PDB data bank.
CC -!- FUNCTION: Putative adapter protein involved in asymmetrical cell
CC division and cell polarization processes. May play a role in the
CC formation of epithelial tight junctions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with PARD6B. Interacts with INSC/inscuteable (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q9CSB4; Q9WTK7: Stk11; NbExp=2; IntAct=EBI-16107395, EBI-8627450;
CC -!- SUBCELLULAR LOCATION: Endomembrane system {ECO:0000250}. Cell junction
CC {ECO:0000250}. Cell junction, tight junction {ECO:0000250}.
CC Note=Partially localized along the cell-cell contact region.
CC Colocalizes with TJP1 to epithelial tight junctions (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9CSB4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9CSB4-2; Sequence=VSP_022017;
CC -!- MISCELLANEOUS: [Isoform 2]: Sequence incomplete. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the PAR3 family. {ECO:0000305}.
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DR EMBL; AL645727; CAI24504.1; -; Genomic_DNA.
DR EMBL; AL662815; CAI24504.1; JOINED; Genomic_DNA.
DR EMBL; AL645669; CAI24504.1; JOINED; Genomic_DNA.
DR EMBL; AL645544; CAI24504.1; JOINED; Genomic_DNA.
DR EMBL; AL662920; CAI24504.1; JOINED; Genomic_DNA.
DR EMBL; AL645669; CAI24824.1; -; Genomic_DNA.
DR EMBL; AL662920; CAI24824.1; JOINED; Genomic_DNA.
DR EMBL; AL662815; CAI24824.1; JOINED; Genomic_DNA.
DR EMBL; AL645727; CAI24824.1; JOINED; Genomic_DNA.
DR EMBL; AL645544; CAI24824.1; JOINED; Genomic_DNA.
DR EMBL; AL645544; CAI25199.1; -; Genomic_DNA.
DR EMBL; AL645669; CAI25199.1; JOINED; Genomic_DNA.
DR EMBL; AL645727; CAI25199.1; JOINED; Genomic_DNA.
DR EMBL; AL662815; CAI25199.1; JOINED; Genomic_DNA.
DR EMBL; AL662920; CAI25199.1; JOINED; Genomic_DNA.
DR EMBL; AL662815; CAI25349.1; -; Genomic_DNA.
DR EMBL; AL645544; CAI25349.1; JOINED; Genomic_DNA.
DR EMBL; AL645669; CAI25349.1; JOINED; Genomic_DNA.
DR EMBL; AL645727; CAI25349.1; JOINED; Genomic_DNA.
DR EMBL; AL662920; CAI25349.1; JOINED; Genomic_DNA.
DR EMBL; AL662920; CAI26112.1; -; Genomic_DNA.
DR EMBL; AL645544; CAI26112.1; JOINED; Genomic_DNA.
DR EMBL; AL645669; CAI26112.1; JOINED; Genomic_DNA.
DR EMBL; AL645727; CAI26112.1; JOINED; Genomic_DNA.
DR EMBL; AL662815; CAI26112.1; JOINED; Genomic_DNA.
DR EMBL; AK013352; BAB28805.1; -; mRNA.
DR CCDS; CCDS48276.1; -. [Q9CSB4-1]
DR RefSeq; NP_001074519.2; NM_001081050.2. [Q9CSB4-1]
DR PDB; 1WG6; NMR; -; A=478-591.
DR PDBsum; 1WG6; -.
DR AlphaFoldDB; Q9CSB4; -.
DR SMR; Q9CSB4; -.
DR BioGRID; 215587; 2.
DR DIP; DIP-60855N; -.
DR IntAct; Q9CSB4; 1.
DR STRING; 10090.ENSMUSP00000074837; -.
DR iPTMnet; Q9CSB4; -.
DR PhosphoSitePlus; Q9CSB4; -.
DR jPOST; Q9CSB4; -.
DR MaxQB; Q9CSB4; -.
DR PaxDb; Q9CSB4; -.
DR PRIDE; Q9CSB4; -.
DR ProteomicsDB; 287953; -. [Q9CSB4-1]
DR ProteomicsDB; 287954; -. [Q9CSB4-2]
DR Antibodypedia; 34169; 40 antibodies from 18 providers.
DR DNASU; 72823; -.
DR Ensembl; ENSMUST00000075374; ENSMUSP00000074837; ENSMUSG00000052062. [Q9CSB4-1]
DR GeneID; 72823; -.
DR KEGG; mmu:72823; -.
DR UCSC; uc007bfe.2; mouse. [Q9CSB4-1]
DR CTD; 117583; -.
DR MGI; MGI:1919301; Pard3b.
DR VEuPathDB; HostDB:ENSMUSG00000052062; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00950000183214; -.
DR InParanoid; Q9CSB4; -.
DR OMA; MVPPYEE; -.
DR OrthoDB; 908238at2759; -.
DR PhylomeDB; Q9CSB4; -.
DR TreeFam; TF323729; -.
DR BioGRID-ORCS; 72823; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Pard3b; mouse.
DR EvolutionaryTrace; Q9CSB4; -.
DR PRO; PR:Q9CSB4; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q9CSB4; protein.
DR Bgee; ENSMUSG00000052062; Expressed in rostral migratory stream and 192 other tissues.
DR ExpressionAtlas; Q9CSB4; baseline and differential.
DR Genevisible; Q9CSB4; MM.
DR GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR GO; GO:0043296; C:apical junction complex; IBA:GO_Central.
DR GO; GO:0016324; C:apical plasma membrane; IBA:GO_Central.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005938; C:cell cortex; IBA:GO_Central.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0012505; C:endomembrane system; IEA:UniProtKB-SubCell.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0035091; F:phosphatidylinositol binding; IBA:GO_Central.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0030010; P:establishment of cell polarity; IBA:GO_Central.
DR GO; GO:0051660; P:establishment of centrosome localization; IBA:GO_Central.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IBA:GO_Central.
DR GO; GO:0008104; P:protein localization; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 3.
DR InterPro; IPR021922; Par3/HAL_N.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF12053; Par3_HAL_N_term; 1.
DR Pfam; PF00595; PDZ; 2.
DR SMART; SM00228; PDZ; 3.
DR SUPFAM; SSF50156; SSF50156; 3.
DR PROSITE; PS50106; PDZ; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell cycle; Cell division;
KW Cell junction; Membrane; Phosphoprotein; Reference proteome; Repeat;
KW Tight junction.
FT CHAIN 1..1203
FT /note="Partitioning defective 3 homolog B"
FT /id="PRO_0000185073"
FT DOMAIN 201..289
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 383..468
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 496..585
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 79..104
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..162
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 718..743
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 787..927
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 968..994
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1050..1203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 787..803
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 804..823
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 836..851
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 852..927
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1138..1165
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1184..1203
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW8"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 352
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW8"
FT MOD_RES 635
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 710
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 728
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 730
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 749
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 801
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW8"
FT MOD_RES 810
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1088
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1182
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8TEW8"
FT VAR_SEQ 169..213
FT /note="DSTQNVENKEAMNGEQAGLLSLHRPKDELSDMTRAVEISGEGDPL -> RTL
FT IGNSSSGEFSALFWLLWALHSCAWINTHSKHITENKIKTFKD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_022017"
FT STRAND 482..484
FT /evidence="ECO:0007829|PDB:1WG6"
FT STRAND 493..500
FT /evidence="ECO:0007829|PDB:1WG6"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:1WG6"
FT TURN 505..507
FT /evidence="ECO:0007829|PDB:1WG6"
FT STRAND 512..518
FT /evidence="ECO:0007829|PDB:1WG6"
FT TURN 519..522
FT /evidence="ECO:0007829|PDB:1WG6"
FT STRAND 523..531
FT /evidence="ECO:0007829|PDB:1WG6"
FT STRAND 534..537
FT /evidence="ECO:0007829|PDB:1WG6"
FT HELIX 539..542
FT /evidence="ECO:0007829|PDB:1WG6"
FT STRAND 549..553
FT /evidence="ECO:0007829|PDB:1WG6"
FT STRAND 556..558
FT /evidence="ECO:0007829|PDB:1WG6"
FT HELIX 563..580
FT /evidence="ECO:0007829|PDB:1WG6"
FT STRAND 583..590
FT /evidence="ECO:0007829|PDB:1WG6"
SQ SEQUENCE 1203 AA; 132780 MW; 7A9D63ED45BD3109 CRC64;
MKVTVCFGRT GIVVPCKDGQ LRVRELTQQA LQRYLKTRDQ DPGYWVKIHH LEYTDGGILD
PDDVLADVVE DKDKLIAVFD EQEPLQKTES PGGNPADRQS PDAFETEVAA QLAAFKPVGG
EIVVTPSALK LGTPLLVRRS SDPAPGPHAD AQPSTASLSG QSLKPVVLDS TQNVENKEAM
NGEQAGLLSL HRPKDELSDM TRAVEISGEG DPLGIHVVPF FSSLSGRILG LFIRGIEENS
RCKQEGLFQE NECIVKINNV ELLDKTFAQA QDVFRQAMKS PSVILHVLLP QNREQYEKSV
IGPLNIFGNN DGASRTKAAP PARGKPGLKA VHLTRASSPE GEEPASPQQS KSPRVPRLGR
KPSSPSLSPL MGFGSKKNAK KIKIDLKKGP EGLGFTVVTR DSSIHGPGPI FVKNILPKGA
AVKDGRLQSG DRILEVNGRD VTGRTQEELV AMLRSTKQGE TVSLVIARQE GSFLPRELKG
EPDCYALSLE SSEQLTLEIP LNDSGSAGLG VSLKGNKSRE TGTDLGIFIK SIIHGGAAFK
DGRLRMNDQL IAVNGETLLG KSNHEAMETL RRSMSMEGNI RGMIQLVILR RPERPLEELS
ECGALSRPGF ENCQEALSTS RRNDSSILYP FGTYSPQDKR KDLLLPSDGW AENEVPPSPP
PHPALEWGLE DFSHSSGVDS TGYFPDQHVN FRTVTPVRQP ELINLKASKS MDLVPDEGKV
QSLADRRSDS PGKDFGPTLG LKKSSSLESL QTAVAEVRKN DLPFHRPRPH MVRGRGCNES
FRAAIDKSYD GPEEADADGL SDKSSRSGHT ALNCESAPQG NPELDNVENK AKNIKKTKEK
EKKKGKGKLK VKEKKLKEEH EDAERKMKRK GFGAMLRFGK KKDDKVGKAE QKGAQKSGHP
EEEELERMKE ERERIGAKHQ ELREKQARGL VDYATAVTGP VHDMDDDEMD PNYARVNHFR
EPCASANVFR SPSPLRAGPL AYPRDGRPLS PDHLEGLYAK VNKPYHPPAL ADSGRPMAGT
TDRIQKLRKE YYQARREGFL LYEDENTRAR PSDHDLRWVS GKGPDGSTHN LRFEGMERQY
ASLPRGGSAD PVDYLTASPR GRYNDRELPY YPGPHPVHAP RGSYPRPPDL RATDLRYPQY
YPPPPAHQHK GPFRQDVPPS PPQHQRVPVY QEMGRAGPRG SSPDQYPYRN QDPRQKNPMT
AAV
