PRC3B_XENLA
ID PRC3B_XENLA Reviewed; 536 AA.
AC A0A1L8F1M4;
DT 25-OCT-2017, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2017, sequence version 1.
DT 25-MAY-2022, entry version 15.
DE RecName: Full=Prickle planar cell polarity protein 3-B {ECO:0000250|UniProtKB:O43900};
DE AltName: Full=LIM domain only protein 6-B;
DE Short=LMO6-B {ECO:0000250|UniProtKB:A8WH69};
DE AltName: Full=Prickle-like protein 3-B;
DE Short=Pk3-B {ECO:0000250|UniProtKB:A8WH69};
DE Flags: Fragment;
GN Name=prickle3-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]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=J {ECO:0000312|Proteomes:UP000186698};
RX PubMed=27762356; DOI=10.1038/nature19840;
RA Session A.M., Uno Y., Kwon T., Chapman J.A., Toyoda A., Takahashi S.,
RA Fukui A., Hikosaka A., Suzuki A., Kondo M., van Heeringen S.J., Quigley I.,
RA Heinz S., Ogino H., Ochi H., Hellsten U., Lyons J.B., Simakov O.,
RA Putnam N., Stites J., Kuroki Y., Tanaka T., Michiue T., Watanabe M.,
RA Bogdanovic O., Lister R., Georgiou G., Paranjpe S.S., van Kruijsbergen I.,
RA Shu S., Carlson J., Kinoshita T., Ohta Y., Mawaribuchi S., Jenkins J.,
RA Grimwood J., Schmutz J., Mitros T., Mozaffari S.V., Suzuki Y., Haramoto Y.,
RA Yamamoto T.S., Takagi C., Heald R., Miller K., Haudenschild C., Kitzman J.,
RA Nakayama T., Izutsu Y., Robert J., Fortriede J., Burns K., Lotay V.,
RA Karimi K., Yasuoka Y., Dichmann D.S., Flajnik M.F., Houston D.W.,
RA Shendure J., DuPasquier L., Vize P.D., Zorn A.M., Ito M., Marcotte E.M.,
RA Wallingford J.B., Ito Y., Asashima M., Ueno N., Matsuda Y., Veenstra G.J.,
RA Fujiyama A., Harland R.M., Taira M., Rokhsar D.S.;
RT "Genome evolution in the allotetraploid frog Xenopus laevis.";
RL Nature 538:336-343(2016).
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).
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 (By similarity). PCP
CC is maintained by two molecular modules, the global and the core modules
CC (PubMed:23140624). Proteins of the core module include the proteins
CC Frizzled (Fz), Disheveled (Dsh), Van Gogh (Vang), Prickle (Pk),
CC Flamingo (Fmi, Celsr) and Diego (Dgo) (PubMed:23140624). The core
CC module proteins develop subcellular asymmetry, accumulating in two
CC groups on opposite sides of epithelial cells (PubMed:23140624).
CC Distinct proximal (Vang, Pk and Fmi) and distal (Fz, Dsh, Dgo and Fmi)
CC complexes segregate to opposite sides of the cell, where they interact
CC with the opposite complex in the neighboring cell at or near the
CC adherents junctions (PubMed:23140624). Directional information to
CC orient polarization with respect to the tissue axes is provided by the
CC global module which involves Wnt proteins (PubMed:23140624). Involved
CC in the organization of the basal body (By similarity). Involved in
CC cilia growth and positioning (By similarity). Required for proper
CC assembly, stability, and function of mitochondrial membrane ATP
CC synthase (mitochondrial complex V) (By similarity).
CC {ECO:0000250|UniProtKB:A8WH69, ECO:0000250|UniProtKB:O43900,
CC ECO:0000303|PubMed:23140624}.
CC -!- SUBUNIT: Interacts with vangl2 via its C-terminus (By similarity). The
CC vangl2-dependent membrane recruitment of prickle3 is a prerequisite for
CC its polarization (By similarity). Interacts with wtip. Wtip is involved
CC in the recruitment of prickle3 to the basal body (By similarity).
CC {ECO:0000250|UniProtKB:A8WH69}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A8WH69}. Cell
CC membrane {ECO:0000250|UniProtKB:A8WH69}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:A8WH69}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:A8WH69}. Mitochondrion
CC {ECO:0000250|UniProtKB:O43900}. Note=Recruited by vangl2 to anterior
CC cell borders. This polarity is controlled by wnt proteins (By
CC similarity). Wtip is involved in the recruitment of prickle3 to the
CC basal body (By similarity). {ECO:0000250|UniProtKB:A8WH69}.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
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DR EMBL; CM004481; OCT65482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1L8F1M4; -.
DR SMR; A0A1L8F1M4; -.
DR STRING; 8355.A0A1L8F1M4; -.
DR OMA; HTAVENR; -.
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 InterPro; IPR033725; LIM1_prickle.
DR InterPro; IPR033726; LIM2_prickle.
DR InterPro; IPR033727; LIM3_prickle.
DR InterPro; IPR010442; PET_domain.
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 3: Inferred from homology;
KW Cell membrane; Cilium biogenesis/degradation; Cytoplasm;
KW Developmental protein; LIM domain; Membrane; Metal-binding; Mitochondrion;
KW Reference proteome; Repeat; Zinc.
FT CHAIN <1..536
FT /note="Prickle planar cell polarity protein 3-B"
FT /id="PRO_0000442109"
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 418..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 446..491
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
SQ SEQUENCE 536 AA; 60382 MW; 18C13D15B9E0AF47 CRC64;
RRRRSQGSEV NLTGQGQPCH SCGERCPGFL AHKWRKICQH CQCPWEEHGH TASNQDLERS
LCRLVSGSQR DSLCDSSSDS SVEKYAWVPS GLNPVQVHHF FKCFPEKKIP YINSPGEKYR
LKQLLHQLPP HDSEARYCCS LQGEEEEELL LLFSQKRRLE NLGRGCVRPI SGTMSGTVCQ
QCGHQINVGE VAVFASRAGL GFCWHPQCFT CAQCLELLCD LIYFYQDGKV YCGRHHAELK
RPRCLACDEV IFSLECTQAE GFHWHTRHFC CFECECPLGG QRYIMKDQRP FCCSCYERLY
AQYCDSCGEC IGIDEGQLTY GGQHWHASES CFCCGRCGEC LLGRPFLPRH GQIYCSRSCS
MLHTKSERPF SPSQMDLSFQ KETKDVGTST NHELEGDSIT NCTLAGSRTS LSVIDQTPTQ
AAPARSLHSS LRGAPKGFSR ECPNRRSLPD LSSHTRTPTR VTFQLPSHSE IKESISFSRP
SFTSSSSSDE EEGYFLGEPI PLPPFLRSPG YTAPPTHVPT STRKQKKKKD KSCFLS
