ID   UACA_BOVIN              Reviewed;        1401 AA.
AC   Q8HYY4;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Uveal autoantigen with coiled-coil domains and ankyrin repeats protein;
DE   AltName: Full=Beta-actin-binding protein;
DE   AltName: Full=BetaCAP73;
GN   Name=UACA;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, AND INDUCTION.
RX   PubMed=11950601; DOI=10.1016/s1357-2725(01)00159-5;
RA   Welch A.Y., Herman I.M.;
RT   "Cloning and characterization of betaCAP73, a novel regulator of beta-actin
RT   assembly.";
RL   Int. J. Biochem. Cell Biol. 34:864-881(2002).
RN   [2]
RP   INTERACTION WITH ARF6 AND ACTB, AND FUNCTION.
RX   PubMed=14517325; DOI=10.1091/mbc.e02-11-0726;
RA   Riley K.N., Maldonado A.E., Tellier P., D'Souza-Schorey C., Herman I.M.;
RT   "Betacap73-ARF6 interactions modulate cell shape and motility after injury
RT   in vitro.";
RL   Mol. Biol. Cell 14:4155-4161(2003).
CC   -!- FUNCTION: Regulates APAF1 expression and plays an important role in the
CC       regulation of stress-induced apoptosis. Promotes apoptosis by
CC       regulating three pathways, apoptosome up-regulation, LGALS3/galectin-3
CC       down-regulation and NF-kappa-B inactivation. Regulates the
CC       redistribution of APAF1 into the nucleus after proapoptotic stress.
CC       Down-regulates the expression of LGALS3 by inhibiting NFKB1 (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: Modulates isoactin dynamics to regulate the morphological
CC       alterations required for cell growth and motility. Interaction with
CC       ARF6 may modulate cell shape and motility after injury
CC       (PubMed:11950601, PubMed:14517325). May be involved in multiple neurite
CC       formation (By similarity). {ECO:0000250|UniProtKB:Q8CGB3,
CC       ECO:0000269|PubMed:11950601, ECO:0000269|PubMed:14517325}.
CC   -!- SUBUNIT: Component of the apoptosome complex, composed of APAF1, pro-
CC       caspase-9 and UACA. In the complex, it probably interacts directly with
CC       APAF1. Interacts with LGALS3 (By similarity). Interacts with ARF6 and
CC       ACTB. Interacts with RAB39A (By similarity).
CC       {ECO:0000250|UniProtKB:Q8CGB3, ECO:0000269|PubMed:14517325}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}. Note=Expressed diffusely in
CC       cytoplasm. {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in muscle and heart, moderately in
CC       liver, kidney and pancreas, and weakly in placenta and lung.
CC       {ECO:0000269|PubMed:11950601}.
CC   -!- INDUCTION: Down-regulated in crawling cells. Up-regulated in motility-
CC       defective cells. {ECO:0000269|PubMed:11950601}.
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DR   EMBL; AY152693; AAN74017.1; -; mRNA.
DR   RefSeq; NP_776634.1; NM_174209.2.
DR   AlphaFoldDB; Q8HYY4; -.
DR   SMR; Q8HYY4; -.
DR   STRING; 9913.ENSBTAP00000018584; -.
DR   iPTMnet; Q8HYY4; -.
DR   PaxDb; Q8HYY4; -.
DR   PRIDE; Q8HYY4; -.
DR   GeneID; 281559; -.
DR   KEGG; bta:281559; -.
DR   CTD; 55075; -.
DR   eggNOG; ENOG502QPYN; Eukaryota.
DR   InParanoid; Q8HYY4; -.
DR   OrthoDB; 876605at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0097190; P:apoptotic signaling pathway; IEA:InterPro.
DR   GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IBA:GO_Central.
DR   GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IBA:GO_Central.
DR   Gene3D; 1.25.40.20; -; 2.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR030227; UACA.
DR   PANTHER; PTHR24173:SF23; PTHR24173:SF23; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   PRINTS; PR01415; ANKYRIN.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
PE   1: Evidence at protein level;
KW   ANK repeat; Coiled coil; Cytoplasm; Cytoskeleton; Isopeptide bond; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN           1..1401
FT                   /note="Uveal autoantigen with coiled-coil domains and
FT                   ankyrin repeats protein"
FT                   /id="PRO_0000231648"
FT   REPEAT          25..53
FT                   /note="ANK 1"
FT   REPEAT          54..83
FT                   /note="ANK 2"
FT   REPEAT          87..116
FT                   /note="ANK 3"
FT   REPEAT          120..149
FT                   /note="ANK 4"
FT   REPEAT          153..182
FT                   /note="ANK 5"
FT   REPEAT          186..215
FT                   /note="ANK 6"
FT   COILED          273..361
FT                   /evidence="ECO:0000255"
FT   COILED          423..827
FT                   /evidence="ECO:0000255"
FT   COILED          856..1368
FT                   /evidence="ECO:0000255"
FT   MOD_RES         265
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8CGB3"
FT   CROSSLNK        1020
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZF9"
SQ   SEQUENCE   1401 AA;  161299 MW;  429312A3F658546A CRC64;
     MMSCWFSCAP KNRQAADWNK YDDRLMRAAE RGDVEKVSSI LAKKGVNPGK LDVEGRSAFH
     VVASKGNLEC LNAILIHGVD ITTSDTAGRN ALHLAAKYGH ALCLQKLLQY NCPTEHVDLQ
     GRTALHDAAM ADCPSSIQLL CDHGASVNAK DVDGRTPLVL ATQMCRPTIC QLLIDRGADI
     NSRDKQNRTA LMLGCEYGCK DAVEVLIKNG ADVTLLDALG HDSSYYARIG DNLDILTLLK
     TASENSNKGR ELWKKGPSLQ QRNLSQMLDE VNTKSNQREH QNIQDLEIEN EDLKERLRKI
     QQEQRILLDK VNGLQLQLNE EVMVADDLES EKEKLKSLLA AKEKQHEESL RTIEALKSRF
     KYFESDHLGS GSHFRKEDML LKQGQMYMTD SQCTSTGMPV HMQSRSMLRP LELALPNQAS
     YSENEILKKE LEAMRTFCDS AKQDRLKLQN ELAHKVAECK ALALECERVK EDSDEQIKQL
     EDALKDVQKR MYESEGKVKQ MQTHFLALKE HLTSDAATGN HRLMEELKDQ LKDMKVKYEG
     ASAEVGKLRN QIKQNEMLVE EFKRDEGKLM EENKRLQKEL SMCELEREKR GRKLTEMEGQ
     LKDLSAKLAL SIPAEKFENM KSLLSNELNE KAKKLIDVER EYERSLNETR PLKRELENLK
     AKLAQHVKPE EHEQLKSRLE QKSGELGKRI TELTSKNQTL QKEIEKVCLD NKLLTQQVNN
     LTTEMKNHYV PLKVSEEMKK SHDVIVDDLN KKLSDVTHKY TEKKLEMEKL LMENASLSKN
     VSRLETVFIP PERHEKEMMA LKSNITELKK QLSELNKKCG EDQEKIYSLM SENNDLKKTM
     SHQYVPVKTH EEIKTALSST LDKTNRELVD VKKKCEDINQ EFVKIKDENE ILKRNLENTQ
     NQVKAEYISL REHEEKMSGL RKSMKKVQDN SAEILAKYKK SQEEIVTLHE EIAAQKRELD
     TIQECIKLKY APIISLEECE RKFKATEKEL KEQLSQQTQK YNTSEEEAKK CKQENDKLKK
     EILTLQKDLK DKNVHIENSY ETERALSRKT EELNRQLKDL LQKYTEAKKE KEKLVEENAK
     QTSEILAAQT LLQKQHVPLE QVESLKKSLS GTIETLKEEL KTKQRCYEKE QQTVTQLRQM
     LENQKNSSVP LAEHLQVKEA FEKEVGIIKA SLREKEEESQ NKTEEVSKLQ SEIQNTKQAL
     KKLETREVVD LSKYKATKSD LETQISDLNE KLANLNRKYE EVCEEVLHAK KKELSAKDEK
     ELLHFSIEQE IKDQQERCDK SLTTITELQR RIQESAKQIE AKDNKITELL NDVERLKQAL
     NGLSQLTYGS GSPSKRQSQL IDSLQQQVRS LQQQLADADR QHQEVIAIYR THLLSAAQGH
     MDEDVQAALL QIIQMRQGLV C