PRIC1_XENTR
ID PRIC1_XENTR Reviewed; 833 AA.
AC Q28FG2;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Prickle-like protein 1;
DE Flags: Precursor;
GN Name=prickle1 {ECO:0000312|EMBL:CAJ81466.1};
GN Synonyms=pk {ECO:0000250|UniProtKB:Q90Z06}; ORFNames=TEgg011j18.1;
OS Xenopus tropicalis (Western clawed frog) (Silurana tropicalis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Silurana.
OX NCBI_TaxID=8364;
RN [1] {ECO:0000312|EMBL:CAJ81466.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Egg {ECO:0000312|EMBL:CAJ81466.1};
RG Sanger Xenopus tropicalis EST/cDNA project;
RL Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Acts in a planar cell polarity (PCP) complex; polarization
CC along the apical/basal axis of epithelial cells. Regulates the
CC polarized assembly of fibronectrin on the surface of the mesoderm
CC during gastrulation. Essential for gastrulation cell movements,
CC cooperating with dvl2/dsh to activate jnk. Acts together with tes to
CC control axial elongation (By similarity).
CC {ECO:0000250|UniProtKB:Q90Z06}.
CC -!- SUBUNIT: Interacts with dvl2/dsh and mapk8/jnk1.
CC {ECO:0000250|UniProtKB:Q90Z06}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
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DR EMBL; CR761986; CAJ81466.1; -; mRNA.
DR RefSeq; NP_001016939.1; NM_001016939.1.
DR AlphaFoldDB; Q28FG2; -.
DR SMR; Q28FG2; -.
DR PaxDb; Q28FG2; -.
DR PRIDE; Q28FG2; -.
DR GeneID; 549693; -.
DR KEGG; xtr:549693; -.
DR CTD; 144165; -.
DR Xenbase; XB-GENE-486941; prickle1.
DR eggNOG; KOG1704; Eukaryota.
DR InParanoid; Q28FG2; -.
DR OrthoDB; 997264at2759; -.
DR Proteomes; UP000008143; Chromosome 3.
DR Proteomes; UP000790000; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009948; P:anterior/posterior axis specification; ISS:UniProtKB.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; ISS:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; ISS:UniProtKB.
DR CDD; cd09415; LIM1_Prickle; 1.
DR CDD; cd09418; LIM2_Prickle; 1.
DR CDD; cd09420; LIM3_Prickle; 1.
DR CDD; cd09827; PET_Prickle; 1.
DR InterPro; IPR033725; LIM1_prickle.
DR InterPro; IPR033726; LIM2_prickle.
DR InterPro; IPR033727; LIM3_prickle.
DR InterPro; IPR010442; PET_domain.
DR InterPro; IPR033723; PET_prickle.
DR InterPro; IPR001781; Znf_LIM.
DR Pfam; PF00412; LIM; 3.
DR Pfam; PF06297; PET; 1.
DR SMART; SM00132; LIM; 3.
DR PROSITE; PS00478; LIM_DOMAIN_1; 2.
DR PROSITE; PS50023; LIM_DOMAIN_2; 3.
DR PROSITE; PS51303; PET; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Developmental protein; Gastrulation; LIM domain;
KW Lipoprotein; Membrane; Metal-binding; Methylation; Prenylation;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..830
FT /note="Prickle-like protein 1"
FT /id="PRO_0000288831"
FT PROPEP 831..833
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396717"
FT DOMAIN 14..122
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 124..188
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 189..249
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 250..313
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 312..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..456
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..702
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 767..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 805..833
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..450
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 651..668
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 683..702
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 816..833
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 830
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 830
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 833 AA; 94775 MW; E4E2629A3CB28CF8 CRC64;
MPLEMDQKIS KHTFGCQRSS TSDDDSGCAM EEYTWVPPGL RPEQVQLYFA CLPEEKVPYV
NSVGEKCRIK QLLYQLPPHD NEVRYCQSLS EEEKKELQMF SAQRKKEALG RGNIKMLSRA
VMHAMCEKCG EKINGGEIAI FVSRAGPGVC WHPSCFVCST CNELLVDLIY FYQDGKIHCG
RHHAELLKPR CSACDEIIFA DECTEAEGRH WHMNHFSCYE CETVLGGQRY IMKDGRPFCC
GCFESHYAEY CESCGEHIGV DHAQMTYDGQ HWHATETCFS CAQCKVSLLG CPFLPKKGRI
YCSKACSLGE DVHASDSSDS AFQSARSRES RRSVRMGKSS RSADQCRQSL LLSPALNYKF
PGMSGNADDT LSRKMDDLSI SRQGAGFDND FWKARDEQET PEDHEEWAEH DDYMTQLLLK
FGEKGLFQQA PEDNRSNEHW MSDNIKGKND LQRNSRNQSL ASKKYQSDMY WAQSQDGLGD
SAYGSHPGPA SSRKLQELDM DHGASGYMHE KMPWYKRSLE CLSDNLKPQN ENICDSMDSL
ALSNITGASV DRENKPRPSL FSYQNFQDLN TRDCEKMSNM GTLNSSMLNR STESLKSLNS
EICQEKPPPE EKPMHTSALR RSKSQTRPQV KFSDDVIDNG DCGSIDIRQP PMSERSRRRV
YNFEERSQRP HHHRRRKSRK SRSENALHLA TESKPSGRER NPRFYTAEDY EKLFHNRSAH
EVQAYIQNAD LFGQYPNAAS NFGLPSQVVD KFLGLYGEDE DSWCSTCSSS SSDSEEEGYF
LGQPIPKPLP QRYQYFSDDL CSPTNALSSS QFSQRTTKSK KKKGHKGKNC IIS
