PRI1A_XENLA
ID PRI1A_XENLA Reviewed; 835 AA.
AC Q90Z06; Q4KLX8;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Prickle-like protein 1-A;
DE AltName: Full=XPk-A;
DE Short=XpkA;
DE Flags: Precursor;
GN Name=prickle1-a; Synonyms=pk-a, pkA, prickle-a;
OS Xenopus laevis (African clawed frog).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Amphibia;
OC Batrachia; Anura; Pipoidea; Pipidae; Xenopodinae; Xenopus; Xenopus.
OX NCBI_TaxID=8355;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula;
RX PubMed=12128221; DOI=10.1016/s0925-4773(02)00133-8;
RA Wallingford J.B., Goto T., Keller R., Harland R.M.;
RT "Cloning and expression of Xenopus Prickle, an orthologue of a Drosophila
RT planar cell polarity gene.";
RL Mech. Dev. 116:183-186(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP FUNCTION, INTERACTION WITH DVL2 AND MAPK8, TISSUE SPECIFICITY, AND
RP DEVELOPMENTAL STAGE.
RX PubMed=12699625; DOI=10.1016/s0960-9822(03)00245-8;
RA Takeuchi M., Nakabayashi J., Sakaguchi T., Yamamoto T.S., Takahashi H.,
RA Takeda H., Ueno N.;
RT "The prickle-related gene in vertebrates is essential for gastrulation cell
RT movements.";
RL Curr. Biol. 13:674-679(2003).
RN [4]
RP FUNCTION.
RX PubMed=15854914; DOI=10.1016/j.cub.2005.03.040;
RA Goto T., Davidson L., Asashima M., Keller R.;
RT "Planar cell polarity genes regulate polarized extracellular matrix
RT deposition during frog gastrulation.";
RL Curr. Biol. 15:787-793(2005).
RN [5]
RP FUNCTION.
RX PubMed=16554046; DOI=10.1016/j.ydbio.2006.02.004;
RA Dingwell K.S., Smith J.C.;
RT "Tes regulates neural crest migration and axial elongation in Xenopus.";
RL Dev. Biol. 293:252-267(2006).
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. {ECO:0000269|PubMed:12699625,
CC ECO:0000269|PubMed:15854914, ECO:0000269|PubMed:16554046}.
CC -!- SUBUNIT: Interacts with dvl2/dsh and mapk8/jnk1.
CC {ECO:0000269|PubMed:12699625}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}.
CC -!- TISSUE SPECIFICITY: Expressed in the dorsal marginal zone of early
CC gastrulae (stage 10). As gastrulation proceeds, expression expands to
CC include the lateral and ventral marginal zones, excluding the few rows
CC of cells above the blastopore lip. Expression moves dorsally with
CC gastrulation cell movements, and by the end of gastrulation expression
CC is seen in dorsal mesoderm and posterior but not anterior neural
CC ectoderm. Expression becomes down-regulated in mesoderm but remains
CC strong in posterior ectoderm through the neurula stages. During tailbud
CC stages, expressed in the pronephric duct, tailbud, tailtip and forming
CC somites. In the most posterior regions, expressed in notochord and in
CC the floorplate of the neural tube with weak expression in the
CC roofplate. At stage 30, expressed in a complex pattern in the head
CC including strong expression in the lens and otic vesicle.
CC {ECO:0000269|PubMed:12128221, ECO:0000269|PubMed:12699625}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically. Zygotic
CC expression begins at the onset of gastrulation (stage 10), and steadily
CC increases until tadpole stage (stage 30). {ECO:0000269|PubMed:12128221,
CC ECO:0000269|PubMed:12699625}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
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DR EMBL; AF387815; AAK70878.1; -; mRNA.
DR EMBL; BC098954; AAH98954.1; -; mRNA.
DR RefSeq; NP_001082157.1; NM_001088688.1.
DR RefSeq; XP_018109644.1; XM_018254155.1.
DR AlphaFoldDB; Q90Z06; -.
DR SMR; Q90Z06; -.
DR DNASU; 398256; -.
DR GeneID; 398256; -.
DR KEGG; xla:398256; -.
DR CTD; 398256; -.
DR Xenbase; XB-GENE-865659; prickle1.S.
DR OMA; LNSEICQ; -.
DR OrthoDB; 344420at2759; -.
DR Proteomes; UP000186698; Chromosome 3S.
DR Bgee; 398256; Expressed in gastrula and 18 other tissues.
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; IMP:UniProtKB.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; IMP:UniProtKB.
DR GO; GO:0001736; P:establishment of planar polarity; IMP:UniProtKB.
DR CDD; cd09418; LIM2_Prickle; 1.
DR CDD; cd09420; LIM3_Prickle; 1.
DR CDD; cd09827; PET_Prickle; 1.
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; 2.
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 1: Evidence at protein level;
KW Cell membrane; Developmental protein; Gastrulation; LIM domain;
KW Lipoprotein; Membrane; Metal-binding; Methylation; Prenylation;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..832
FT /note="Prickle-like protein 1-A"
FT /id="PRO_0000288829"
FT PROPEP 833..835
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396715"
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 312..346
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 426..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 603..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 769..835
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 648..669
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..685
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 686..706
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 799..817
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 818..835
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 832
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 832
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 726
FT /note="A -> T (in Ref. 2; AAH98954)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 835 AA; 95011 MW; 0B52EB9A932318B7 CRC64;
MPLEMDQKVN KLTFGCQRSS TSDDDSGCAM EEYTWVPPGL RLEQVQLYFA CLPEEKIPYV
NSVGEKYRIK QLLYQLPPHD NEVRYCQSLS EEEKKELQMF SAQRKKEALG RGNIKMLSRA
VMHATCEKCG EKINGGEVAI FVSRAGPGVC WHPSCFVCST CNELLVDLIY FYQDGKIHCG
RHHAELLKPR CSACDEIIFA DECTEAEGRH WHMNHFCCYE CETVLGGQRY IMKDGRPFCC
GCFESHYAEY CESCGEHIGV DHAQMTYDGQ HWHATETCFS CAQCKVSLLG CPFLPKKGRI
YCCKACSLGE DVHASDSSDS AFQSARSRES RRSVRMGKSS RSADQCRQSL LLSPAVNYKF
PGMFGNADDT LSRKMDDLSM SRQGAGFDND TWKARDEQET AEDHEEWAEH DDYMTQLLLK
FGEKGLFQQP PEDNRSNDHW MSENIKGKND LQRNNRNQSL ASKKYQSDMY WAQSQDGLGD
SAYGSHPGPA SSRKLQELDM DHGASGYMHE KMPWYKRSLE CLSNNLKPQN ENICDSMDSL
ALSNITGASV DAESKSRPSL FSYQNFQELN TRDFDKMSNM GTLNSSMLNR STESLKSLNS
EICQEKPPPE EKPMHTSALK RSKSQTRPQV KFSDDVIDNG DYSSIEIRRP PMSERSRRRV
YNSEEQSQRP HHHHHHRRRK SRKSRSENAL HLATDSKSSG KERKRSYTAE DYERLFHNKS
AHEVQAYIQN ADLFGQYSNA ASNVGLPSQV VDKFLGLYGE DEDSWCSTCS SSSSDSEEEG
YFLGQPIPKP RPQRYQYFSD DLCSPTNALS SSQFSQRTSK SKKKKGHKGK NCIIS
