PRIC3_HUMAN
ID PRIC3_HUMAN Reviewed; 615 AA.
AC O43900; B7Z8F2; O76007; Q53XR5;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2002, sequence version 2.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Prickle planar cell polarity protein 3 {ECO:0000312|HGNC:HGNC:6645};
DE AltName: Full=LIM domain only protein 6;
DE Short=LMO-6;
DE AltName: Full=Prickle-like protein 3;
DE Short=Pk3 {ECO:0000305};
DE AltName: Full=Triple LIM domain protein 6;
GN Name=PRICKLE3 {ECO:0000312|HGNC:HGNC:6645}; Synonyms=LMO6;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Heart;
RA Strom T.M., Gutwillinger N., Nyakatura G., Hellebrand H., Drescher B.,
RA Rosenthal A., Meindl A.;
RT "Transcription map in Xp11.23.";
RL Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Thymus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon, and Kidney;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 69-615.
RX PubMed=9344658; DOI=10.1006/geno.1997.4941;
RA Fisher S.E., Ciccodicola A., Tanaka K., Curci A., Desicato S., D'Urso M.,
RA Craig I.W.;
RT "Sequence-based exon prediction around the synaptophysin locus reveals a
RT gene-rich area containing novel genes in human proximal Xp.";
RL Genomics 45:340-347(1997).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-475 AND SER-491, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [10]
RP VARIANT [LARGE SCALE ANALYSIS] ASP-558.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [11]
RP VARIANT LOAM TRP-53, INVOLVEMENT IN LOAM, CHARACTERIZATION OF VARIANT LOAM
RP TRP-53, SUBCELLULAR LOCATION, INTERACTION WITH MT-ATP8, AND FUNCTION.
RX PubMed=32516135; DOI=10.1172/jci134965;
RA Yu J., Liang X., Ji Y., Ai C., Liu J., Zhu L., Nie Z., Jin X., Wang C.,
RA Zhang J., Zhao F., Mei S., Zhao X., Zhou X., Zhang M., Wang M., Huang T.,
RA Jiang P., Guan M.X.;
RT "PRICKLE3 linked to ATPase biogenesis manifested Leber's hereditary optic
RT neuropathy.";
RL J. Clin. Invest. 130:4935-4946(2020).
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
CC modules, PRICKLE3 being part of the core module (By similarity).
CC Distinct complexes of the core module 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 (By similarity).
CC Involved in the organization of the basal body (By similarity).
CC Involved in cilia growth and positioning (By similarity). Required for
CC proper assembly, stability, and function of mitochondrial membrane ATP
CC synthase (mitochondrial complex V) (PubMed:32516135).
CC {ECO:0000250|UniProtKB:A8WH69, ECO:0000269|PubMed:32516135}.
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 Interacts with MT-ATP8, a component of the mitochondrial complex V
CC (PubMed:32516135). {ECO:0000250|UniProtKB:A8WH69,
CC ECO:0000269|PubMed:32516135}.
CC -!- INTERACTION:
CC O43900; P00519: ABL1; NbExp=2; IntAct=EBI-1751761, EBI-375543;
CC O43900; P06241: FYN; NbExp=2; IntAct=EBI-1751761, EBI-515315;
CC O43900; O00204: SULT2B1; NbExp=3; IntAct=EBI-1751761, EBI-749441;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:A8WH69,
CC ECO:0000269|PubMed:32516135}. Cell membrane
CC {ECO:0000250|UniProtKB:A8WH69}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:A8WH69}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:A8WH69}. Mitochondrion
CC {ECO:0000269|PubMed:32516135}. 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43900-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43900-2; Sequence=VSP_056568, VSP_056569;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DISEASE: Leber hereditary optic neuropathy, modifier (LOAM)
CC [MIM:308905]: A form of Leber hereditary optic neuropathy, a
CC mitochondrial disease resulting in bilateral painless loss of central
CC vision due to selective degeneration of the retinal ganglion cells and
CC their axons. The disorder shows incomplete penetrance and male
CC predominance. Leber hereditary optic neuropathy is maternally inherited
CC in most case and results from primary mitochondrial DNA mutations
CC affecting the respiratory chain complexes. Mutations in modifier genes
CC can influence disease expression. LOAM exhibits increased penetrance
CC and earlier age of onset compared to Leber optic atrophy caused by
CC MTND4 primary mutations, due to the action of mutations in PRICKLE3 as
CC a modifier gene. {ECO:0000269|PubMed:32516135}. Note=The gene
CC represented in this entry acts as a disease modifier.
CC -!- SIMILARITY: Belongs to the prickle / espinas / testin family.
CC {ECO:0000305}.
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DR EMBL; AJ011654; CAA09726.1; -; mRNA.
DR EMBL; BT007423; AAP36091.1; -; mRNA.
DR EMBL; AK303308; BAH13938.1; -; mRNA.
DR EMBL; AF196779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471224; EAW50686.1; -; Genomic_DNA.
DR EMBL; BC002468; AAH02468.1; -; mRNA.
DR EMBL; BC016856; AAH16856.1; -; mRNA.
DR EMBL; U93305; AAB92357.1; -; Genomic_DNA.
DR CCDS; CCDS14320.1; -. [O43900-1]
DR RefSeq; NP_006141.2; NM_006150.4. [O43900-1]
DR AlphaFoldDB; O43900; -.
DR SMR; O43900; -.
DR BioGRID; 110192; 80.
DR IntAct; O43900; 68.
DR STRING; 9606.ENSP00000470248; -.
DR iPTMnet; O43900; -.
DR PhosphoSitePlus; O43900; -.
DR BioMuta; PRICKLE3; -.
DR EPD; O43900; -.
DR jPOST; O43900; -.
DR MassIVE; O43900; -.
DR MaxQB; O43900; -.
DR PaxDb; O43900; -.
DR PeptideAtlas; O43900; -.
DR PRIDE; O43900; -.
DR ProteomicsDB; 49223; -. [O43900-1]
DR ProteomicsDB; 6945; -.
DR Antibodypedia; 404; 117 antibodies from 27 providers.
DR DNASU; 4007; -.
DR Ensembl; ENST00000599218.6; ENSP00000470248.1; ENSG00000012211.13. [O43900-1]
DR GeneID; 4007; -.
DR KEGG; hsa:4007; -.
DR MANE-Select; ENST00000599218.6; ENSP00000470248.1; NM_006150.5; NP_006141.2.
DR UCSC; uc004dmy.2; human. [O43900-1]
DR CTD; 4007; -.
DR DisGeNET; 4007; -.
DR GeneCards; PRICKLE3; -.
DR HGNC; HGNC:6645; PRICKLE3.
DR HPA; ENSG00000012211; Low tissue specificity.
DR MalaCards; PRICKLE3; -.
DR MIM; 300111; gene.
DR MIM; 308905; phenotype.
DR neXtProt; NX_O43900; -.
DR OpenTargets; ENSG00000012211; -.
DR PharmGKB; PA162400060; -.
DR VEuPathDB; HostDB:ENSG00000012211; -.
DR eggNOG; KOG1704; Eukaryota.
DR GeneTree; ENSGT00940000153629; -.
DR HOGENOM; CLU_008937_8_1_1; -.
DR InParanoid; O43900; -.
DR OMA; LPGRAMF; -.
DR PhylomeDB; O43900; -.
DR TreeFam; TF313265; -.
DR PathwayCommons; O43900; -.
DR SignaLink; O43900; -.
DR BioGRID-ORCS; 4007; 12 hits in 709 CRISPR screens.
DR ChiTaRS; PRICKLE3; human.
DR GenomeRNAi; 4007; -.
DR Pharos; O43900; Tbio.
DR PRO; PR:O43900; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; O43900; protein.
DR Bgee; ENSG00000012211; Expressed in lower esophagus mucosa and 94 other tissues.
DR ExpressionAtlas; O43900; baseline and differential.
DR Genevisible; O43900; HS.
DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB.
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; 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 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cilium biogenesis/degradation;
KW Cytoplasm; Developmental protein; Disease variant;
KW Leber hereditary optic neuropathy; LIM domain; Membrane; Metal-binding;
KW Mitochondrion; Phosphoprotein; Primary mitochondrial disease;
KW Reference proteome; Repeat; Zinc.
FT CHAIN 1..615
FT /note="Prickle planar cell polarity protein 3"
FT /id="PRO_0000075822"
FT DOMAIN 74..182
FT /note="PET"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00636"
FT DOMAIN 184..249
FT /note="LIM zinc-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 250..309
FT /note="LIM zinc-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT DOMAIN 310..373
FT /note="LIM zinc-binding 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00125"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..567
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 587..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 503..529
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 537..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 475
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056568"
FT VAR_SEQ 106..142
FT /note="YQFFSCLPEDKVPYVNSPGEKYRIKQLLHQLPPHDSE -> TRGQPSTLAVQ
FT WVHTNAHTHTHTQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056569"
FT VARIANT 53
FT /note="R -> W (in LOAM; acts as a modifier allele
FT increasing the penetrance and expressivity of LHON-
FT associated mtDNA mutations; reduced protein levels; does
FT not affect localization to mitochondria; results in altered
FT complex V stability and activity)"
FT /evidence="ECO:0000269|PubMed:32516135"
FT /id="VAR_084628"
FT VARIANT 343
FT /note="R -> C (in dbSNP:rs7065449)"
FT /id="VAR_050169"
FT VARIANT 558
FT /note="E -> D (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036188"
FT CONFLICT 185
FT /note="I -> S (in Ref. 7; AAB92357)"
FT /evidence="ECO:0000305"
FT CONFLICT 370..509
FT /note="Missing (in Ref. 7; AAB92357)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 615 AA; 68609 MW; CD024365C072B052 CRC64;
MFARGSRRRR SGRAPPEAED PDRGQPCNSC REQCPGFLLH GWRKICQHCK CPREEHAVHA
VPVDLERIMC RLISDFQRHS ISDDDSGCAS EEYAWVPPGL KPEQVYQFFS CLPEDKVPYV
NSPGEKYRIK QLLHQLPPHD SEAQYCTALE EEEKKELRAF SQQRKRENLG RGIVRIFPVT
ITGAICEECG KQIGGGDIAV FASRAGLGAC WHPQCFVCTT CQELLVDLIY FYHVGKVYCG
RHHAECLRPR CQACDEIIFS PECTEAEGRH WHMDHFCCFE CEASLGGQRY VMRQSRPHCC
ACYEARHAEY CDGCGEHIGL DQGQMAYEGQ HWHASDRCFC CSRCGRALLG RPFLPRRGLI
FCSRACSLGS EPTAPGPSRR SWSAGPVTAP LAASTASFSA VKGASETTTK GTSTELAPAT
GPEEPSRFLR GAPHRHSMPE LGLRSVPEPP PESPGQPNLR PDDSAFGRQS TPRVSFRDPL
VSEGGPRRTL SAPPAQRRRP RSPPPRAPSR RRHHHHNHHH HHNRHPSRRR HYQCDAGSGS
DSESCSSSPS SSSSESSEDD GFFLGERIPL PPHLCRPMPA QDTAMETFNS PSLSLPRDSR
AGMPRQARDK NCIVA
