PRC3A_XENLA
ID PRC3A_XENLA Reviewed; 538 AA.
AC A8WH69;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 1.
DT 25-MAY-2022, entry version 49.
DE RecName: Full=Prickle planar cell polarity protein 3-A {ECO:0000250|UniProtKB:O43900};
DE AltName: Full=LIM domain only protein 6-A;
DE Short=LMO6-A {ECO:0000303|PubMed:27062996};
DE AltName: Full=Prickle-like protein 3-A;
DE Short=Pk3-A {ECO:0000303|PubMed:26079437};
DE Flags: Fragment;
GN Name=prickle3-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 {ECO:0000312|EMBL:AAI54996.1};
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Intestine;
RG NIH - Xenopus Gene Collection (XGC) project;
RL Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP REVIEW, AND FUNCTION.
RX PubMed=23140624; DOI=10.1016/b978-0-12-394592-1.00002-8;
RA Peng Y., Axelrod J.D.;
RT "Asymmetric protein localization in planar cell polarity: mechanisms,
RT puzzles, and challenges.";
RL Curr. Top. Dev. Biol. 101:33-53(2012).
RN [3]
RP TISSUE SPECIFICITY, FUNCTION, AND INTERACTION WITH VANGL2.
RX PubMed=26079437; DOI=10.1016/j.ydbio.2015.06.013;
RA Ossipova O., Chu C.W., Fillatre J., Brott B.K., Itoh K., Sokol S.Y.;
RT "The involvement of PCP proteins in radial cell intercalations during
RT Xenopus embryonic development.";
RL Dev. Biol. 408:316-327(2015).
RN [4]
RP FUNCTION IN CILIA GROWTH, AND INTERACTION WITH WTIP.
RX PubMed=27062996; DOI=10.1038/srep24104;
RA Chu C.W., Ossipova O., Ioannou A., Sokol S.Y.;
RT "Prickle3 synergizes with Wtip to regulate basal body organization and
RT cilia growth.";
RL Sci. Rep. 6:24104-24104(2016).
RN [5]
RP FUNCTION, INTERACTION WITH VANGL2, AND SUBCELLULAR LOCATION.
RX PubMed=27658614; DOI=10.7554/elife.16463;
RA Chu C.W., Sokol S.Y.;
RT "Wnt proteins can direct planar cell polarity in vertebrate ectoderm.";
RL Elife 5:0-0(2016).
CC -!- FUNCTION: Involved in the planar cell polarity (PCP) pathway that is
CC essential for the polarization of epithelial cells during morphogenetic
CC processes, including gastrulation and neurulation (PubMed:26079437,
CC PubMed:27658614). PCP is maintained by two molecular modules, the
CC global and the core modules (PubMed:23140624). Proteins of the core
CC module include the proteins Frizzled (Fz), Disheveled (Dsh), Van Gogh
CC (Vang), Prickle (Pk), Flamingo (Fmi, Celsr) and Diego (Dgo)
CC (PubMed:23140624). The core module proteins develop subcellular
CC asymmetry, accumulating in two groups on opposite sides of epithelial
CC cells (PubMed:23140624). Distinct proximal (Vang, Pk and Fmi) and
CC distal (Fz, Dsh, Dgo and Fmi) complexes segregate to opposite sides of
CC the cell, where they interact with the opposite complex in the
CC neighboring cell at or near the adherents junctions (PubMed:23140624).
CC Directional information to orient polarization with respect to the
CC tissue axes is provided by the global module which involves Wnt
CC proteins (PubMed:23140624). Involved in the organization of the basal
CC body (PubMed:27062996). Involved in cilia growth and positioning
CC (PubMed:27062996). Required for proper assembly, stability, and
CC function of mitochondrial membrane ATP synthase (mitochondrial complex
CC V) (By similarity). {ECO:0000250|UniProtKB:O43900,
CC ECO:0000269|PubMed:26079437, ECO:0000269|PubMed:27062996,
CC ECO:0000269|PubMed:27658614, ECO:0000303|PubMed:23140624}.
CC -!- SUBUNIT: Interacts with vangl2 via its C-terminus (PubMed:27658614,
CC PubMed:26079437). The vangl2-dependent membrane recruitment of prickle3
CC is a prerequisite for its polarization (PubMed:27062996). Interacts
CC with wtip. Wtip is involved in the recruitment of prickle3 to the basal
CC body (PubMed:27062996). {ECO:0000269|PubMed:26079437,
CC ECO:0000269|PubMed:27062996, ECO:0000269|PubMed:27658614}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:27658614}. Cell
CC membrane {ECO:0000269|PubMed:27658614}; Peripheral membrane protein
CC {ECO:0000269|PubMed:27658614}; Cytoplasmic side
CC {ECO:0000269|PubMed:27658614}. Mitochondrion
CC {ECO:0000250|UniProtKB:O43900}. Note=Recruited by vangl2 to anterior
CC cell borders. This polarity is controlled by wnt proteins
CC (PubMed:27658614). Wtip is involved in the recruitment of prickle3 to
CC the basal body (PubMed:27062996). {ECO:0000269|PubMed:27062996,
CC ECO:0000269|PubMed:27658614}.
CC -!- TISSUE SPECIFICITY: Predominantly expressed in the epidermal ectoderm
CC (PubMed:26079437). {ECO:0000269|PubMed:26079437}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
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DR EMBL; BC154995; AAI54996.1; -; mRNA.
DR AlphaFoldDB; A8WH69; -.
DR SMR; A8WH69; -.
DR Proteomes; UP000186698; Genome assembly.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
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; 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; Cilium biogenesis/degradation; Cytoplasm;
KW Developmental protein; LIM domain; Membrane; Metal-binding; Mitochondrion;
KW Reference proteome; Repeat; Zinc.
FT CHAIN <1..538
FT /note="Prickle planar cell polarity protein 3-A"
FT /id="PRO_0000442108"
FT DOMAIN 66..175
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 177..241
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 242..302
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 305..366
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 369..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 433..463
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 369..385
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 447..463
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 475..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 502..516
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 522..538
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000312|EMBL:AAI54996.1"
SQ SEQUENCE 538 AA; 60412 MW; 45716C4CA7042FF3 CRC64;
RRRRSQGSEV NLTGQGQPCH SCGERCPGFL AHRWRKICQH CQCPWEEHGH TASNQDLERS
LCRLVSGSQR DSLCESSSDS SVEKYAWVPS GLNPVQVHQF FKCFPEKKIP FINSPGEKYR
LKQLLHQLPP HDSEARYCCS LQGEEEEELL LLFSQKRRLE NLGRGCVRPV SGTMSGTVCQ
QCGHQISVGD VAVFASRAGL GFCWHPQCFT CAQCLELLCD LIYFYQDGKV YCGRHHAELK
RPRCLACDEV IFSLECTEAE GFHWHTRHFC CFECECPLGG QRYIMKDQRP FCCSCYERLY
AQYCDSCGEC IGIDEGQLTY GGQHWHASES CFRCGRCGVC LLGRPFLPRH GQIYCSRSCS
VLNATPESSF SPSQTDLSFQ KETKDVGTST NHELDGDSIN DCTLSGSRRS LSIIDQTPIS
RAAPIRSLHS SLRGAPKEFS RECPNRRSLP DLNSHTRTPT RVTFQLPLSS EVKESVSLSH
PSFTSSSSSD EEEGYFLGEP IPLPPFLRPP GYSAPPTHAP TSTTKKKKKK KDKSCLLS
