PRI1B_XENLA
ID PRI1B_XENLA Reviewed; 832 AA.
AC Q90WV2; Q6GPD3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Prickle-like protein 1-B;
DE AltName: Full=XPk-B;
DE Flags: Precursor;
GN Name=prickle1-b; Synonyms=pk-b, prickle-b;
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] {ECO:0000305, ECO:0000312|EMBL:AAL16403.1}
RP NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Gastrula {ECO:0000269|PubMed:12128221};
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] {ECO:0000312|EMBL:AAH73208.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Gastrula {ECO:0000312|EMBL:AAH73208.1};
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000305}
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).
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:0000250|UniProtKB:Q90Z06,
CC ECO:0000269|PubMed:15854914}.
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 -!- 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}.
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).
CC {ECO:0000269|PubMed:12128221}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH73208.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAL16403.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY055473; AAL16403.1; ALT_INIT; mRNA.
DR EMBL; BC073208; AAH73208.1; ALT_INIT; mRNA.
DR RefSeq; NP_001082169.1; NM_001088700.1.
DR AlphaFoldDB; Q90WV2; -.
DR SMR; Q90WV2; -.
DR DNASU; 398264; -.
DR GeneID; 398264; -.
DR KEGG; xla:398264; -.
DR CTD; 398264; -.
DR Xenbase; XB-GENE-6251800; prickle1.L.
DR OrthoDB; 997264at2759; -.
DR Proteomes; UP000186698; Chromosome 3L.
DR Bgee; 398264; Expressed in gastrula and 19 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; ISS:UniProtKB.
DR GO; GO:0060027; P:convergent extension involved in gastrulation; 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..829
FT /note="Prickle-like protein 1-B"
FT /id="PRO_0000288830"
FT PROPEP 830..832
FT /note="Removed in mature form"
FT /evidence="ECO:0000250"
FT /id="PRO_0000396716"
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 428..455
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 602..701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 766..832
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..453
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..701
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 796..814
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 815..832
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 829
FT /note="Cysteine methyl ester"
FT /evidence="ECO:0000250"
FT LIPID 829
FT /note="S-farnesyl cysteine"
FT /evidence="ECO:0000250"
FT CONFLICT 2
FT /note="P -> S (in Ref. 2; AAH73208)"
FT /evidence="ECO:0000305"
FT CONFLICT 431
FT /note="S -> P (in Ref. 2; AAH73208)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 832 AA; 94694 MW; 8A0190A4C9C0FC0E CRC64;
MPLEMDQKVN KLTFGCQRSS TSDDDSGCAM EEYTWVPPGL RPEQVQLYFA CLPEEKIPYV
NSIGEKYRIK QLLYQLPPHD NEVRYCQSLC EEEKKELQMF SGQRKKEALG RGNIKMLSRA
VMHAMCEKCG EKINGGEIAI FVSRAGPGVC WHPSCFVCST CNELLVDLIY FYQDGKIHCG
RHHAELLKPR CSACDEIIFA DECTEAEGRH WHMNHFCCYE CETVLGGQRY IMKDGRPFCC
GCFESHYAEY CESCGDHIGV DHAQMTYDGQ HWHATETCFS CAQCKVSLLG CPFLPKKGRI
YCSKACSLGE DVHASDSSDS AFQSARSRES RRSVRMGKSS RSADQCRQSL LLSPALNYKF
PGMSGNADDT LSRKMDDLGI SRQGAGFDND FWKARDEQET PEDHEEWAEH DDYMTQLLLK
FGEKGLFQQP SEDNRSTEHW MSENIKGKND LQRNNRNKSL ASKKYQSDMY WTQSQDGLGD
SAYGSHPGPA SSRKLQELDM DHGASAYMHE KMPWYKRSLE CLSDNLKPQN ENIRDSMDSL
ALSNITGASV DGENKSRPSL FCYQNFQDLN TRDCEKMSNM GTLNSSMLNR STESLKSLTS
EICQEKPPPE EKPMHTSALR RSKSQTRPQV KFSDDVIDNG DYGSIEIRQP PMSERSRRRV
YNFEERSQRP HHHRRRKSRK SRSENALHLA TDSKPSGKER NRFYTAEDYE RLFHNKSAHQ
VQAYIQNADL FGQYSNAASN VGLPSKVAGK FLGLYGEDED SWCSTCSSSS SDSEEEGYFL
GQPIPKPRPQ RYQYFSDDLC SPTNALSSSQ FSQRTTKSKK KKGHKGKNCI IS
