UACA_MOUSE
ID UACA_MOUSE Reviewed; 1411 AA.
AC Q8CGB3; Q69ZG3; Q7TN77; Q8BJC8;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Uveal autoantigen with coiled-coil domains and ankyrin repeats;
DE AltName: Full=Nuclear membrane-binding protein;
DE Short=Nucling;
GN Name=Uaca; Synonyms=Kiaa1561;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, DEVELOPMENTAL STAGE, AND INDUCTION.
RC STRAIN=129;
RX PubMed=12761289; DOI=10.1093/jb/mvg056;
RA Sakai T., Liu L., Shishido Y., Fukui K.;
RT "Identification of a novel, embryonal carcinoma cell-associated molecule,
RT nucling, that is up-regulated during cardiac muscle differentiation.";
RL J. Biochem. 133:429-436(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Embryonic intestine;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary gland, and Salivary gland;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-306.
RC STRAIN=C57BL/6J; TISSUE=Eye;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP FUNCTION, AND INTERACTION WITH APAF1.
RX PubMed=15271982; DOI=10.1074/jbc.m402902200;
RA Sakai T., Liu L., Teng X., Mukai-Sakai R., Shimada H., Kaji R., Mitani T.,
RA Matsumoto M., Toida K., Ishimura K., Shishido Y., Mak T.W., Fukui K.;
RT "Nucling recruits Apaf-1/pro-caspase-9 complex for the induction of stress-
RT induced apoptosis.";
RL J. Biol. Chem. 279:41131-41140(2004).
RN [6]
RP FUNCTION, INTERACTION WITH LGALS3, AND DISRUPTION PHENOTYPE.
RX PubMed=14961764; DOI=10.1042/bj20031300;
RA Liu L., Sakai T., Sano N., Fukui K.;
RT "Nucling mediates apoptosis by inhibiting expression of galectin-3 through
RT interference with nuclear factor kappaB signalling.";
RL Biochem. J. 380:31-41(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Kidney, Lung, Pancreas, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [9]
RP FUNCTION, AND INTERACTION WITH RAB39A.
RX PubMed=23624502; DOI=10.1016/j.bbrc.2013.04.051;
RA Mori Y., Matsui T., Omote D., Fukuda M.;
RT "Small GTPase Rab39A interacts with UACA and regulates the retinoic acid-
RT induced neurite morphology of Neuro2A cells.";
RL Biochem. Biophys. Res. Commun. 435:113-119(2013).
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.
CC {ECO:0000269|PubMed:14961764, ECO:0000269|PubMed:15271982}.
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 (By similarity).
CC May be involved in multiple neurite formation (PubMed:23624502).
CC {ECO:0000250|UniProtKB:Q8HYY4, ECO:0000269|PubMed:23624502}.
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.
CC {ECO:0000269|PubMed:14961764, ECO:0000269|PubMed:15271982,
CC ECO:0000269|PubMed:23624502}.
CC -!- INTERACTION:
CC Q8CGB3-3; Q8BHD0: Rab39a; NbExp=3; IntAct=EBI-10767725, EBI-10767908;
CC Q8CGB3-3; Q8BHC1: Rab39b; NbExp=4; IntAct=EBI-10767725, EBI-10767682;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:12761289}. Cytoplasm
CC {ECO:0000269|PubMed:12761289}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12761289}. Note=Expressed diffusely in cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8CGB3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8CGB3-2; Sequence=VSP_017874;
CC Name=3;
CC IsoId=Q8CGB3-3; Sequence=VSP_017875;
CC -!- TISSUE SPECIFICITY: Highly expressed in heart, liver, kidney and
CC testis. Weakly expressed in lung and skeletal muscle. Not expressed in
CC brain and spleen. {ECO:0000269|PubMed:12761289}.
CC -!- DEVELOPMENTAL STAGE: First detected at 9.5 dpc in heart at the edge of
CC both sides of the common ventricular chamber and is then progressively
CC increased and restricted to the myocardial wall of left common
CC ventricular chamber of heart. {ECO:0000269|PubMed:12761289}.
CC -!- INDUCTION: Up-regulated during cardiomyogenic differentiation. By
CC apoptotic stress in a dose-dependent manner.
CC {ECO:0000269|PubMed:12761289}.
CC -!- DISRUPTION PHENOTYPE: Mice show a high incidence of inflammatory
CC lesions in preputial glands. Cells around the lesions showed resistance
CC to apoptosis. {ECO:0000269|PubMed:14961764}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC78213.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAD32481.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB030647; BAC78213.1; ALT_INIT; mRNA.
DR EMBL; AK173203; BAD32481.1; ALT_INIT; mRNA.
DR EMBL; BC042415; AAH42415.1; -; mRNA.
DR EMBL; AK087466; BAC39886.1; -; mRNA.
DR CCDS; CCDS23259.1; -. [Q8CGB3-3]
DR CCDS; CCDS90590.1; -. [Q8CGB3-1]
DR RefSeq; NP_082559.1; NM_028283.2.
DR RefSeq; XP_017169098.1; XM_017313609.1.
DR AlphaFoldDB; Q8CGB3; -.
DR SMR; Q8CGB3; -.
DR BioGRID; 215442; 9.
DR IntAct; Q8CGB3; 5.
DR STRING; 10090.ENSMUSP00000062047; -.
DR iPTMnet; Q8CGB3; -.
DR PhosphoSitePlus; Q8CGB3; -.
DR EPD; Q8CGB3; -.
DR jPOST; Q8CGB3; -.
DR MaxQB; Q8CGB3; -.
DR PaxDb; Q8CGB3; -.
DR PeptideAtlas; Q8CGB3; -.
DR PRIDE; Q8CGB3; -.
DR ProteomicsDB; 297767; -. [Q8CGB3-1]
DR ProteomicsDB; 297768; -. [Q8CGB3-2]
DR ProteomicsDB; 297769; -. [Q8CGB3-3]
DR DNASU; 72565; -.
DR GeneID; 72565; -.
DR KEGG; mmu:72565; -.
DR UCSC; uc009pzi.1; mouse. [Q8CGB3-3]
DR UCSC; uc009pzk.1; mouse. [Q8CGB3-1]
DR CTD; 55075; -.
DR MGI; MGI:1919815; Uaca.
DR eggNOG; ENOG502QPYN; Eukaryota.
DR InParanoid; Q8CGB3; -.
DR OrthoDB; 876605at2759; -.
DR PhylomeDB; Q8CGB3; -.
DR TreeFam; TF331274; -.
DR Reactome; R-MMU-9013407; RHOH GTPase cycle.
DR BioGRID-ORCS; 72565; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Uaca; mouse.
DR PRO; PR:Q8CGB3; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8CGB3; protein.
DR GO; GO:0043293; C:apoptosome; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0005635; C:nuclear envelope; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:MGI.
DR GO; GO:0008630; P:intrinsic apoptotic signaling pathway in response to DNA damage; IMP:MGI.
DR GO; GO:0008631; P:intrinsic apoptotic signaling pathway in response to oxidative stress; IMP:MGI.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:1901223; P:negative regulation of NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0038061; P:NIK/NF-kappaB signaling; IMP:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IDA:MGI.
DR GO; GO:0043280; P:positive regulation of cysteine-type endopeptidase activity involved in apoptotic process; IDA:MGI.
DR GO; GO:0042307; P:positive regulation of protein import into nucleus; IMP:MGI.
DR GO; GO:0006606; P:protein import into nucleus; IMP:MGI.
DR GO; GO:0009411; P:response to UV; IMP:MGI.
DR Gene3D; 1.25.40.20; -; 2.
DR InterPro; IPR002110; Ankyrin_rpt.
DR InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR InterPro; IPR000727; T_SNARE_dom.
DR InterPro; IPR030227; UACA.
DR PANTHER; PTHR24173:SF23; PTHR24173:SF23; 1.
DR Pfam; PF12796; Ank_2; 1.
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.
DR PROSITE; PS50192; T_SNARE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; ANK repeat; Coiled coil; Cytoplasm;
KW Cytoskeleton; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1411
FT /note="Uveal autoantigen with coiled-coil domains and
FT ankyrin repeats"
FT /id="PRO_0000231651"
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 234..263
FT /note="ANK 6"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 263..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1006..1031
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 299..379
FT /evidence="ECO:0000255"
FT COILED 442..624
FT /evidence="ECO:0000255"
FT COILED 652..1380
FT /evidence="ECO:0000255"
FT COMPBIAS 13..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..301
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:Q9BZF9"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319,
FT ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..398
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15368895"
FT /id="VSP_017874"
FT VAR_SEQ 264
FT /note="G -> GGG (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_017875"
FT CONFLICT 144
FT /note="V -> A (in Ref. 3; AAH42415)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="P -> L (in Ref. 3; AAH42415)"
FT /evidence="ECO:0000305"
FT CONFLICT 757
FT /note="R -> K (in Ref. 3; AAH42415)"
FT /evidence="ECO:0000305"
FT CONFLICT 778
FT /note="A -> T (in Ref. 3; AAH42415)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1411 AA; 160813 MW; 0809D2DE9732F879 CRC64;
MKSLKSRLWK QDAPGPTSPS SPTAVASTQS AEWNKYDDRL MKAAERGDVE KVSSILAKKG
VHPGKLDVEG RSAFHVVASK GNLECLNAIL THGIDVATRD SAGRNALHLA AKYGHALCLQ
KLLQYNCPTE HVDLQGRTAL HDAVMADCPS SIQLLCDHGA SVNAKDIDGR TPLVLATQMC
RPTICQLLID RGADVNSRDK QNRTALMLGC EYGCRDAVEV LVKNGADLTL LDALGHDSSY
YARIGDNLDI LNLLKTASEN TNKGRELWRK GPPLQQRNLS HTQDEGSVKS TQREQREPHS
FQDLEIENED LREKLRKIQQ EQRILLDKVN GLQLQLNEEV MVADDLESER EKPKSLLAAK
EKQHEESLRT IEALKNRFKY FESDHPGPGS YPSNRKEDML HKQGQMYTTE PQCASPGIPP
HMHSRSMLRP LELSLPSQTS YSENEILKKE LETLRTYYDS AKQDRLKFQN ELAHKVAECK
ALALECERVK EDSDEQIKQL EDALKDVQKR MYESEGKVKQ MQTHFLALKE HLTNEAATGS
HRIIEELREQ LKDLKGKYEG ASAEVGKLRS QIKQSEMLVG EFKRDEGRLV EENKRLQKEC
GTCEVELERR GRRVVELEGQ LKELGAKLAL SVPTEKFESM KSSLSNDINE KVKRLAEVGR
DYESAQGEIR QLKRDLESVR AQHIRPEEHE QLRSRLEQKS GELGKKVSEL TLKNQTLQKD
VEKLHADNKL LNQQVHSLTV EMKTRYVPLR VSEEMKRSHD VNVEDLNKKL SEATQRYAEK
KQEAERLLAE NDKLTKNVSR LEAVFVAPEK HEKELMGLKS NIAELKKQLS ELNKKCGEGQ
EKIRALMSEN SSLKKTLSSQ YVPAKTHEEV KASLNSTVEK TNRALLEAKK RFDDTSQEVS
KLRDENEVLR RNLENVQNQM KADYVSLEEH SRRMSTVSQS LKEAQEANAA ILADHRQGQE
EIVSLHAEIK AQKKELDTIQ ECIKLKYAPL ARLEECERKF KATEKGLKEQ LSEQTHKCRQ
RDEEVKKGKQ ENERLRADLA ALQKELQDRN ALAEEAREAE RALSGKADEL SKQLKDLSQK
YSDVKSEREK LVEEKAKQAS EILAAQNLLQ KQPVPLEQVE ALKKSLNGTI EQLKEELRSK
QRCLEREQQT VSQLQQLLEN QKNSSVTLAE HLKLKEALEK EVGIMKASLR EKEEESQKKT
KEVSKLQTEV QTTKQALKNL ETREVVDMSK YKATKNDLET QISNLNDKLA SLNRKYDQAC
EEKVSAKDEK ELLHLSIEQE IRDQKERCDK SLTTIMELQQ RIQESAKQIE AKDNKITELL
NDVERLKQAL NGLSQLTYSS GSPTKRQSQL VDTLQQRVRD LQQQLADADR QHQEVIAIYR
THLLSAAQGH MDEDVQAALL QIIQMRQGLV C
