PICC1_CAEEL
ID PICC1_CAEEL Reviewed; 535 AA.
AC H2KYP0; Q8IA85;
DT 11-NOV-2015, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 1.
DT 03-AUG-2022, entry version 55.
DE RecName: Full=PAC-1 interacting and coiled-coil domain-containing protein 1 {ECO:0000303|PubMed:25938815};
GN Name=picc-1 {ECO:0000312|WormBase:F29G9.2a};
GN ORFNames=F29G9.2 {ECO:0000312|WormBase:F29G9.2a};
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239 {ECO:0000312|Proteomes:UP000001940};
RN [1] {ECO:0000312|Proteomes:UP000001940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Bristol N2 {ECO:0000312|Proteomes:UP000001940};
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] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PAC-1 AND JAC-1, SUBCELLULAR LOCATION,
RP DEVELOPMENTAL STAGE, 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: Linker protein which helps to recruit the Rho GTPase-
CC activating protein, pac-1, to adherens junctions.
CC {ECO:0000269|PubMed:25938815}.
CC -!- SUBUNIT: Interacts with pac-1 and jac-1. {ECO:0000269|PubMed:25938815}.
CC -!- INTERACTION:
CC H2KYP0; Q9U308: jac-1; NbExp=3; IntAct=EBI-315998, EBI-2917356;
CC H2KYP0; P34288: pac-1; NbExp=4; IntAct=EBI-315998, EBI-2918318;
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:25938815}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=a {ECO:0000312|WormBase:F29G9.2a};
CC IsoId=H2KYP0-1; Sequence=Displayed;
CC Name=b {ECO:0000312|WormBase:F29G9.2b};
CC IsoId=H2KYP0-2; Sequence=VSP_057978;
CC -!- DEVELOPMENTAL STAGE: Expressed in four-cell stage embryos.
CC {ECO:0000269|PubMed:25938815}.
CC -!- DISRUPTION PHENOTYPE: Mutants are 97% viable. However, the Rho GTPase-
CC activating protein, pac-1, does not localize to adherens junctions.
CC {ECO:0000269|PubMed:25938815}.
CC -!- SIMILARITY: Belongs to the CCDC85 family. {ECO:0000305}.
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DR EMBL; BX284605; CCD64130.1; -; Genomic_DNA.
DR EMBL; BX284605; CCD64131.1; -; Genomic_DNA.
DR PIR; T31802; T31802.
DR RefSeq; NP_504560.1; NM_072159.6. [H2KYP0-1]
DR RefSeq; NP_872141.1; NM_182341.4.
DR AlphaFoldDB; H2KYP0; -.
DR SMR; H2KYP0; -.
DR DIP; DIP-61636N; -.
DR IntAct; H2KYP0; 9.
DR MINT; H2KYP0; -.
DR STRING; 6239.F29G9.2a; -.
DR EPD; H2KYP0; -.
DR PaxDb; H2KYP0; -.
DR EnsemblMetazoa; F29G9.2a.1; F29G9.2a.1; WBGene00017931. [H2KYP0-1]
DR EnsemblMetazoa; F29G9.2b.1; F29G9.2b.1; WBGene00017931. [H2KYP0-2]
DR GeneID; 3564810; -.
DR KEGG; cel:CELE_F29G9.2; -.
DR UCSC; F29G9.2a; c. elegans.
DR CTD; 3564810; -.
DR WormBase; F29G9.2a; CE27374; WBGene00017931; picc-1. [H2KYP0-1]
DR WormBase; F29G9.2b; CE09796; WBGene00017931; picc-1. [H2KYP0-2]
DR eggNOG; KOG3819; Eukaryota.
DR GeneTree; ENSGT00940000170945; -.
DR InParanoid; H2KYP0; -.
DR OMA; RIKHLEM; -.
DR OrthoDB; 809807at2759; -.
DR SignaLink; H2KYP0; -.
DR PRO; PR:H2KYP0; -.
DR Proteomes; UP000001940; Chromosome V.
DR Bgee; WBGene00017931; Expressed in embryo and 4 other tissues.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR InterPro; IPR019359; CCDC85.
DR PANTHER; PTHR13546; PTHR13546; 1.
DR Pfam; PF10226; CCDC85; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Coiled coil; Reference proteome.
FT CHAIN 1..535
FT /note="PAC-1 interacting and coiled-coil domain-containing
FT protein 1"
FT /evidence="ECO:0000305"
FT /id="PRO_0000434729"
FT REGION 1..67
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 254..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 503..535
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 109..172
FT /evidence="ECO:0000255"
FT COILED 198..242
FT /evidence="ECO:0000255"
FT COMPBIAS 1..22
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 34..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..10
FT /note="Missing (in isoform b)"
FT /evidence="ECO:0000305"
FT /id="VSP_057978"
SQ SEQUENCE 535 AA; 60083 MW; 1D741A241EC054F6 CRC64;
MIITTPRRAN MSSESGSSAS TVHYAKPVLR HVPMPSSTTP SSIGSSSSSS SSYASSTKQT
PPRSPVIRYP TVVVSKNSIA TPSSSLTPQG TPSYAVPVSR NQMQYSASKL QYEHMRHRCK
MLDDENQKLM RMQSDVVNDA NRRVQMHVNE IRMLKEDNRK LAISNKELRD LSCFLDDDRQ
KTRKLAREWQ KFGRYTSSLM KQEVDSYHQK MVSIEEKLCT KEREVDELRQ LCMYLDEQRQ
SLMSNAAANV DCDNESEDLG CGSSEQSGGS EGHNDEEKHH EFNKCFNKHK ESTLRRIMAT
SMCSEPSEEE ERREVSKRER SRLLGYIQSL ENRIKHLEMS QNHESFWNSS SNVGSDCDEK
TIIERGWLGE EVMSNSEDCH LELKPVMTTS STSSSHIFGN DKCPMFDSMT SNMTSSGCTT
YASSGTDGDS VFVIGDEIDI GNLEVRTLSR IDEEATSASD TLKESARMPP KIAPPICSSL
VLTNFDNMSE DCAPRLMRSA SETCRPTTTL ISSTQPAQRS VSVEKNNNNN VHTHN
