ID   UACA_CANLF              Reviewed;        1415 AA.
AC   Q9GL21;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-APR-2006, sequence version 2.
DT   03-AUG-2022, entry version 112.
DE   RecName: Full=Uveal autoantigen with coiled-coil domains and ankyrin repeats;
GN   Name=UACA; ORFNames=C3VS;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), TISSUE SPECIFICITY, AND INDUCTION.
RC   TISSUE=Thyroid;
RX   PubMed=8910471; DOI=10.1074/jbc.271.45.28451;
RA   Wilkin F., Savonet V., Radulescu A., Petermans J., Dumont J.E.,
RA   Maenhaut C.;
RT   "Identification and characterization of novel genes modulated in the
RT   thyroid of dogs treated with methimazole and propylthiouracil.";
RL   J. Biol. Chem. 271:28451-28457(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Boxer;
RX   PubMed=16341006; DOI=10.1038/nature04338;
RA   Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA   Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA   Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA   Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA   Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA   Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA   Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA   Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA   Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA   Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA   Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA   Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA   Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA   Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA   Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA   Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA   Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA   Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA   Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA   Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA   Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA   Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA   Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA   LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA   Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA   Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA   Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA   Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA   Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA   Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA   Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA   Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA   Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA   Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA   Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA   Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA   Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA   Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA   Zembek L., Zimmer A., Lander E.S.;
RT   "Genome sequence, comparative analysis and haplotype structure of the
RT   domestic dog.";
RL   Nature 438:803-819(2005).
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. May be involved
CC       in multiple neurite formation (By similarity).
CC       {ECO:0000250|UniProtKB:Q8CGB3, ECO:0000250|UniProtKB:Q8HYY4}.
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, ARF6 and ACTB. Interacts with RAB39A (By
CC       similarity). {ECO:0000250|UniProtKB:Q8CGB3,
CC       ECO:0000250|UniProtKB:Q8HYY4}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC       Cytoplasm, cytoskeleton {ECO:0000250}. Note=Expressed diffusely in
CC       cytoplasm. {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q9GL21-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q9GL21-2; Sequence=VSP_017873;
CC   -!- TISSUE SPECIFICITY: Highly expressed in adrenal, testis, kidney and
CC       large intestine. {ECO:0000269|PubMed:8910471}.
CC   -!- INDUCTION: Up-regulated in stimulated thyroids. Down-regulated by
CC       forskolin and TSH. Up-regulated by EGF. {ECO:0000269|PubMed:8910471}.
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DR   EMBL; X99145; CAC14169.1; -; mRNA.
DR   EMBL; AAEX02018681; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAEX02018682; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AAEX02018683; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; NP_001003112.1; NM_001003112.1. [Q9GL21-2]
DR   AlphaFoldDB; Q9GL21; -.
DR   SMR; Q9GL21; -.
DR   STRING; 9612.ENSCAFP00000034132; -.
DR   PaxDb; Q9GL21; -.
DR   PRIDE; Q9GL21; -.
DR   Ensembl; ENSCAFT00845039181; ENSCAFP00845030687; ENSCAFG00845022131. [Q9GL21-2]
DR   GeneID; 403704; -.
DR   KEGG; cfa:403704; -.
DR   CTD; 55075; -.
DR   eggNOG; ENOG502QPYN; Eukaryota.
DR   GeneTree; ENSGT00940000157475; -.
DR   InParanoid; Q9GL21; -.
DR   OrthoDB; 876605at2759; -.
DR   Reactome; R-CFA-9013407; RHOH GTPase cycle.
DR   Proteomes; UP000002254; Chromosome 30.
DR   Bgee; ENSCAFG00000017611; Expressed in adrenal cortex and 45 other tissues.
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; 1.
DR   SMART; SM00248; ANK; 6.
DR   SUPFAM; SSF48403; SSF48403; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 5.
PE   2: Evidence at transcript level;
KW   Alternative splicing; ANK repeat; Coiled coil; Cytoplasm; Cytoskeleton;
KW   Isopeptide bond; Nucleus; Reference proteome; Repeat; Ubl conjugation.
FT   CHAIN           1..1415
FT                   /note="Uveal autoantigen with coiled-coil domains and
FT                   ankyrin repeats"
FT                   /id="PRO_0000231649"
FT   REPEAT          69..98
FT                   /note="ANK 1"
FT   REPEAT          102..131
FT                   /note="ANK 2"
FT   REPEAT          135..164
FT                   /note="ANK 3"
FT   REPEAT          168..197
FT                   /note="ANK 4"
FT   REPEAT          201..230
FT                   /note="ANK 5"
FT   REPEAT          617..646
FT                   /note="ANK 6"
FT   REGION          1186..1205
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          288..376
FT                   /evidence="ECO:0000255"
FT   COILED          759..1381
FT                   /evidence="ECO:0000255"
FT   CROSSLNK        1034
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q9BZF9"
FT   VAR_SEQ         380..406
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8910471"
FT                   /id="VSP_017873"
SQ   SEQUENCE   1415 AA;  162540 MW;  98666A5645F0D844 CRC64;
     MPSSLLLATR NQILSMMNCW FSCAPKNRHA ADWNKYDDRL MKAAERGDVE KVSSILAKKG
     INPGKLDVEG RSAFHVVASK GNLECLNAIL IHGVDITTSD TAGRNALHLA AKYGHALCLQ
     KLLQYNCPTE HADLQGRTAL HDAAMADCPS SIQLLCDHGA SVNAKDVDGR TPLVLATQMC
     RPAICQLLID RGAEINSRDK QNRTALMLGC EYGCKDAVEV LLKNGADVSL LDALGHDSSY
     YARIGDNLDI LTLLKTASEN TNKGRELWKK GPSLQQRNLP YMLDEVNVKS SQREHRNIQE
     LEIENEDLKD RLRKIQQEQR ILLDKVNGLQ LQLNEEVMVA DDLESEKEKL KSLLVAKEKQ
     HEESLRTIES LKNRFKYFES DHLGSGSHFS NRKEDMLLKQ GQMYMTCTSP GVPAHMQSRS
     MLRPLELSLP NQTSYSENDL LKKELEAMRT FCESAKQDRL KLQNELAHKV AECKALGLEC
     ERIKEDSDEQ IKQLEDALKD VQKRMYESEG KVKQMQTHFL ALKEHLTSEA AIGNHRLMEE
     LKDQLKDMKA KYEGASAEVG KLRNQIKQNE LLVEQFRRDE GKLVEENKRL QKELSMCETE
     RDKKGRRVAE VEGQVKELLA KLTLSVPTEK FESMKSLLSS EVNEKVKKIG ETEREYEKSL
     TEIRQLRREL ENCKAKLAQH VKPEEHEQLK SRLEQRAGEL AKKVTELTSK NQVLQRDVEK
     VYLDNKLLNQ QVHNLTSEIK SHYVPLQVSE EMKKSHDVTV EELKKQLLDV TQKCADKQLE
     MEKLLLENDS LSKNVSRLET VFVPPEKHQK EVTALKSSVA DLKRQLLELN KKCGEDREKI
     NALVSENTSL KKTLSNQYVP AKTHEEVKTA LSGTLDKTNR ELLDAKKKWE DLNQEFVKTK
     DENEILKRNL ENTQSQIKAE YISLREHEEK MSAINQNMKS VQDNSAEILA NYRKGQEEIV
     TLHAEIEAQK KELDTIQECI KLKYAPIISF EECERKFKAT EKELKEQLSE QMQKYHVREE
     EAKKYKQEND KLKKEIFTLQ KDLKDKNVLI ENSHDMERAL NRKAEELNKQ LKDLLQKYSE
     IKTEKEKLVD DNARQTSELL AAQTLLQKQH VPLEQVETLK KSLNSTIEHL KEELKNKQKC
     YEKEQQTVAK LHQMLENQKN SSVPLGEHLR VKEAFEKEVG MIKASLREKE EESQNKTEEV
     SKLQSEVQDT KQALQKLETR EVVDLSKYKA TKSDLETQIS NLNEKLANLN RKYEEACEEV
     LRAQRKQLSA KDEKELLHFS IEQEIKDQQE RCDKSLTTIT ELQKRIQESA KQIEAKDNKI
     TELLNDVERL KQALSGLSQL TSPSGSPSKR QSQLIDTLQH QVKSLQQQLA DTDRQHQEVI
     AIYRTHLLSA AQGHMDEDVQ AALLQIIQMR QGLVC