JAC1_CAEEL
ID JAC1_CAEEL Reviewed; 1254 AA.
AC Q9U308; Q2HQL5;
DT 12-DEC-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 03-AUG-2022, entry version 152.
DE RecName: Full=Juxtamembrane domain-associated catenin;
DE AltName: Full=p120 catenin homolog;
GN Name=jac-1; ORFNames=Y105C5B.21;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
RN [2]
RP IDENTIFICATION.
RX PubMed=11560894; DOI=10.1093/genetics/159.1.159;
RA Natarajan L., Witwer N.E., Eisenmann D.M.;
RT "The divergent Caenorhabditis elegans beta-catenin proteins BAR-1, WRM-1
RT and HMP-2 make distinct protein interactions but retain functional
RT redundancy in vivo.";
RL Genetics 159:159-172(2001).
RN [3]
RP IDENTIFICATION, FUNCTION, INTERACTION WITH HMR-1, SUBCELLULAR LOCATION,
RP ALTERNATIVE SPLICING, TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=12847081; DOI=10.1083/jcb.200212136;
RA Pettitt J., Cox E.A., Broadbent I.D., Flett A., Hardin J.;
RT "The Caenorhabditis elegans p120 catenin homologue, JAC-1, modulates
RT cadherin-catenin function during epidermal morphogenesis.";
RL J. Cell Biol. 162:15-22(2003).
RN [4]
RP FUNCTION, ASSOCIATION WITH THE CATENIN-CADHERIN COMPLEX, INTERACTION WITH
RP PICC-1 AND HMR-1, SUBCELLULAR LOCATION, AND DISRUPTION PHENOTYPE.
RX PubMed=25938815; DOI=10.1038/ncb3168;
RA Klompstra D., Anderson D.C., Yeh J.Y., Zilberman Y., Nance J.;
RT "An instructive role for C. elegans E-cadherin in translating cell contact
RT cues into cortical polarity.";
RL Nat. Cell Biol. 17:726-735(2015).
CC -!- FUNCTION: May act as a positive modulator of hmr-1 function during
CC epidermal morphogenesis (PubMed:12847081). Required for proper
CC localization of other junctional components, such as pac-1
CC (PubMed:25938815). {ECO:0000269|PubMed:12847081,
CC ECO:0000269|PubMed:25938815}.
CC -!- SUBUNIT: Associated with the catenin-cadherin complex consisting of
CC hmr-1, hmp-1 and hmp-2 (PubMed:25938815). Interacts with hmr-1
CC (PubMed:12847081, PubMed:25938815). Interacts with picc-1
CC (PubMed:25938815). {ECO:0000269|PubMed:12847081,
CC ECO:0000269|PubMed:25938815}.
CC -!- INTERACTION:
CC Q9U308; Q967F4: hmr-1; NbExp=3; IntAct=EBI-2917356, EBI-2528888;
CC Q9U308; H2KYP0: picc-1; NbExp=3; IntAct=EBI-2917356, EBI-315998;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:12847081, ECO:0000269|PubMed:25938815}. Nucleus
CC {ECO:0000269|PubMed:25938815}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a;
CC IsoId=Q9U308-1; Sequence=Displayed;
CC Name=b;
CC IsoId=Q9U308-2; Sequence=VSP_021980;
CC -!- TISSUE SPECIFICITY: Epidermal cells. {ECO:0000269|PubMed:12847081}.
CC -!- DEVELOPMENTAL STAGE: Expressed in the early epidermis.
CC {ECO:0000269|PubMed:12847081}.
CC -!- DISRUPTION PHENOTYPE: Embryos are viable, but display a partial loss of
CC junctional component, pac-1, from adherens junctions.
CC {ECO:0000269|PubMed:25938815}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR EMBL; AL110479; CAJ76966.1; -; Genomic_DNA.
DR EMBL; AL110479; CAB60320.2; -; Genomic_DNA.
DR RefSeq; NP_001041007.1; NM_001047542.1. [Q9U308-1]
DR RefSeq; NP_001041008.1; NM_001047543.2. [Q9U308-2]
DR AlphaFoldDB; Q9U308; -.
DR SMR; Q9U308; -.
DR BioGRID; 43529; 23.
DR DIP; DIP-61637N; -.
DR IntAct; Q9U308; 21.
DR STRING; 6239.Y105C5B.21a; -.
DR iPTMnet; Q9U308; -.
DR EPD; Q9U308; -.
DR PaxDb; Q9U308; -.
DR PeptideAtlas; Q9U308; -.
DR PRIDE; Q9U308; -.
DR EnsemblMetazoa; Y105C5B.21a.1; Y105C5B.21a.1; WBGene00002175. [Q9U308-1]
DR EnsemblMetazoa; Y105C5B.21b.1; Y105C5B.21b.1; WBGene00002175. [Q9U308-2]
DR GeneID; 178451; -.
DR KEGG; cel:CELE_Y105C5B.21; -.
DR UCSC; Y105C5B.21b.1; c. elegans. [Q9U308-1]
DR CTD; 178451; -.
DR WormBase; Y105C5B.21a; CE32231; WBGene00002175; jac-1. [Q9U308-1]
DR WormBase; Y105C5B.21b; CE39806; WBGene00002175; jac-1. [Q9U308-2]
DR eggNOG; KOG1048; Eukaryota.
DR GeneTree; ENSGT00940000166712; -.
DR InParanoid; Q9U308; -.
DR Reactome; R-CEL-351906; Apoptotic cleavage of cell adhesion proteins.
DR Reactome; R-CEL-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-CEL-6798695; Neutrophil degranulation.
DR Reactome; R-CEL-6809371; Formation of the cornified envelope.
DR SignaLink; Q9U308; -.
DR PRO; PR:Q9U308; -.
DR Proteomes; UP000001940; Chromosome IV.
DR Bgee; WBGene00002175; Expressed in pharyngeal muscle cell (C elegans) and 3 other tissues.
DR ExpressionAtlas; Q9U308; baseline and differential.
DR GO; GO:0005912; C:adherens junction; IDA:WormBase.
DR GO; GO:0016342; C:catenin complex; IDA:WormBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; IPI:WormBase.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0010172; P:embryonic body morphogenesis; IGI:WormBase.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; IGI:WormBase.
DR GO; GO:0032880; P:regulation of protein localization; IGI:WormBase.
DR CDD; cd00063; FN3; 4.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 4.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR028446; JAC-1.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR PANTHER; PTHR10372:SF27; PTHR10372:SF27; 1.
DR Pfam; PF00514; Arm; 3.
DR Pfam; PF00041; fn3; 3.
DR SMART; SM00185; ARM; 5.
DR SMART; SM00060; FN3; 4.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49265; SSF49265; 2.
DR PROSITE; PS50176; ARM_REPEAT; 2.
DR PROSITE; PS50853; FN3; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..1254
FT /note="Juxtamembrane domain-associated catenin"
FT /id="PRO_0000268649"
FT DOMAIN 207..302
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 315..411
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 428..518
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 530..624
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 733..775
FT /note="ARM 1"
FT REPEAT 777..820
FT /note="ARM 2"
FT REPEAT 874..922
FT /note="ARM 3"
FT REPEAT 969..1012
FT /note="ARM 4"
FT REPEAT 1016..1058
FT /note="ARM 5"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 662..685
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 920..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1159..1254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..956
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1161..1222
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..170
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_021980"
SQ SEQUENCE 1254 AA; 138358 MW; 2EEE70F6E72C8607 CRC64;
MISSGWMQEM EPIPEEGTEA DGSEWGAMSD TAKRTMRKKE VYTSEQINTL VSTVPKEAVP
QEWLVENQVV DPEMATSYLT ESLAGPTSAR GSSYSYSYES HYDNPPEEEY EHFTNDDGVH
QMQKVTRVTK VTTTRSVRQV PVQSPYSNID FDSSGLPTPS PVIDRDPSLE MMARMGGASD
HDSEDRSAPP PAPASRFLHE DSGIPSAPGV PDVVDAGIGE VTVVWSAPLQ SNGGEVRGYQ
IEMREFPDGE WESMGVDHLL KDTTCRVTNL TSHEVQFRVS AYGRTGFGPA SNPSLPVKIP
ISETDLATSA GAPLAPGRPT VIAVDGQGVL LEWTPPVADV HSSPPQGYQV EYRVYGSRDW
IVANEQLVQE NVFTVESLRP NGVYEFRVRG KNQDGLGHPS MSSGGVAIRP AAPQRHVPAR
KVSESVQPPG QPQMVEVGDD VVKLEWAPSV QNARYIVEYR EVGDPEWHTA NYDPIVQNGI
QVEGLHRNST YEFCVISIVD NIASQPSETS DIIHLRPTCN TSALRPAPNI LEAPEFLEVD
GDKITICWLP AQSQLPVMGY DVEFRDLQQD DRWYKVNDQP VFACKMTVGD LIMDHDYQFR
VLAHNASGCS QPSPPSDFVH IEPSTNRFSS DTMESPHLGH HDVVKYVEAE RFGAVPLLQE
EMVRESPPLP ERDDSPPPLR RANNNVQWRD PSLKEVIEYL SSADKDKQLN ASGYLQHLTY
TDNQIKEETR EYGGIPKLIA LLRSDTPRIQ KNACACLKNL SFGKENDANK LAVMEADGVR
LIAEVLRTTH DASVKEEAAA ALWNLSSADM LKPVILESAT EILSQQVIAP VLAVGTSDPT
RHFGSTLFKN STGVLRNVSA ASQQARRRLR DIPNLIEALV HFLTHAIQKS QVDSPTVENA
VCLLRNLSYR IQEVVDPNYD PAAAHSSSSK NMKHVASPKP EKKKKDKEKK KDKNPKNIVT
GPSVLWQPHV VKLYLKLLQD SSNIETLEAS AGAIQNLAAC QFPPSAEVRA AVRVEKGLPV
LVELIRLPED FVVCAVATAL RNLAIDPRNR ELIGKYALRD FLDKLPEPGS PRRSAISDQT
IGAVLGILFE IVRSSAAYTK DVHELKGTDK LRALSRSYPT YSHRVCKYAS QVLYVMWQHK
ELHDGFKRSG LKEADFYSGT ARRGDSSTLA RPISSQGRER PSMHQLDETL SSGGGYGTME
SNNRAGTLRP ASATSQTIQR RYDQVPRDGP VYSSVQKPSP RGGGGGGNID DSWV
