CATIN_HUMAN
ID CATIN_HUMAN Reviewed; 758 AA.
AC Q8WUQ7; A6NNA9; A9UL12; O75229; Q7LE08; Q9BTA6; Q9Y5A4;
DT 04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 08-FEB-2011, sequence version 3.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Cactin;
DE AltName: Full=Renal carcinoma antigen NY-REN-24;
GN Name=CACTIN; Synonyms=C19orf29;
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 [MRNA] (ISOFORM 1).
RA Cai Y., Yan Y.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 123-758.
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 69-758.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 469-758 (ISOFORM 1).
RC TISSUE=Cervix, and Uterus;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 534-758 (ISOFORM 1), AND IDENTIFICATION AS A
RP RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [7]
RP FUNCTION, INTERACTION WITH NFKBIL1, AND SUBCELLULAR LOCATION.
RX PubMed=20829348; DOI=10.1074/jbc.m110.139113;
RA Atzei P., Gargan S., Curran N., Moynagh P.N.;
RT "Cactin targets the MHC class III protein IkappaB-like (IkappaBL) and
RT inhibits NF-kappaB and interferon-regulatory factor signaling pathways.";
RL J. Biol. Chem. 285:36804-36817(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-476, AND IDENTIFICATION BY
RP 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-559, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, INDUCTION BY TNFA, AND INTERACTION WITH
RP TRIM39.
RX PubMed=26363554; DOI=10.1007/s00018-015-2040-x;
RA Suzuki M., Watanabe M., Nakamaru Y., Takagi D., Takahashi H., Fukuda S.,
RA Hatakeyama S.;
RT "TRIM39 negatively regulates the NFkappaB-mediated signaling pathway
RT through stabilization of Cactin.";
RL Cell. Mol. Life Sci. 73:1085-1101(2016).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-469 AND LYS-484, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
CC -!- FUNCTION: Involved in the regulation of innate immune response
CC (PubMed:20829348). Acts as negative regulator of Toll-like receptor,
CC interferon-regulatory factor (IRF) and canonical NF-kappa-B signaling
CC pathways (PubMed:20829348, PubMed:26363554). Contributes to the
CC regulation of transcriptional activation of NF-kappa-B target genes in
CC response to endogenous pro-inflammatory stimuli (PubMed:20829348,
CC PubMed:26363554). {ECO:0000269|PubMed:20829348,
CC ECO:0000269|PubMed:26363554}.
CC -!- SUBUNIT: Interacts (via N-terminal domain) with NFKBIL1; the
CC interaction occurs in a pro-inflammatory-independent manner
CC (PubMed:20829348). Does not interact with RELA NF-kappa-B subunit
CC (PubMed:20829348). Identified in the spliceosome C complex
CC (PubMed:11991638). Interacts with isoform 2 of TRIM39 (via domain B
CC box-type) (PubMed:26363554). {ECO:0000269|PubMed:11991638,
CC ECO:0000269|PubMed:20829348, ECO:0000269|PubMed:26363554}.
CC -!- INTERACTION:
CC Q8WUQ7; P49760: CLK2; NbExp=3; IntAct=EBI-348479, EBI-750020;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:20829348,
CC ECO:0000269|PubMed:26363554}. Cytoplasm, cytosol
CC {ECO:0000269|PubMed:26363554}. Note=Nuclear localization with a
CC speckled expression pattern in some cells. Colocalizes with NFKBIL1 in
CC the nucleus. {ECO:0000269|PubMed:20829348}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8WUQ7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8WUQ7-2; Sequence=VSP_017856;
CC -!- INDUCTION: Up-regulated by TNF-alpha/TNFA (at protein level).
CC {ECO:0000269|PubMed:26363554}.
CC -!- MISCELLANEOUS: Antigen recognized by autologous antibody in patients
CC with renal-cell carcinoma.
CC -!- MISCELLANEOUS: [Isoform 1]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay.
CC -!- SIMILARITY: Belongs to the CACTIN family. {ECO:0000305}.
CC -!- CAUTION: An ORF (C19orf029 OS) has been described in the opposite
CC strand of the C-terminus of this gene. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC24305.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAC32903.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAD42868.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH04262.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=EAW69298.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AY917150; AAX84551.1; -; mRNA.
DR EMBL; AC005175; AAC24305.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AC005542; AAC32903.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AF155102; AAD42868.1; ALT_FRAME; mRNA.
DR EMBL; CH471139; EAW69298.1; ALT_FRAME; Genomic_DNA.
DR EMBL; BC004262; AAH04262.1; ALT_INIT; mRNA.
DR EMBL; BC019848; AAH19848.1; -; mRNA.
DR CCDS; CCDS45920.1; -. [Q8WUQ7-1]
DR PIR; T02672; T02672.
DR RefSeq; NP_001074012.1; NM_001080543.1. [Q8WUQ7-1]
DR RefSeq; NP_067054.1; NM_021231.1. [Q8WUQ7-1]
DR PDB; 6QDV; EM; 3.30 A; F=637-758.
DR PDBsum; 6QDV; -.
DR AlphaFoldDB; Q8WUQ7; -.
DR SMR; Q8WUQ7; -.
DR BioGRID; 121836; 111.
DR CORUM; Q8WUQ7; -.
DR IntAct; Q8WUQ7; 26.
DR MINT; Q8WUQ7; -.
DR STRING; 9606.ENSP00000415078; -.
DR iPTMnet; Q8WUQ7; -.
DR MetOSite; Q8WUQ7; -.
DR PhosphoSitePlus; Q8WUQ7; -.
DR BioMuta; CACTIN; -.
DR DMDM; 322510133; -.
DR EPD; Q8WUQ7; -.
DR jPOST; Q8WUQ7; -.
DR MassIVE; Q8WUQ7; -.
DR MaxQB; Q8WUQ7; -.
DR PaxDb; Q8WUQ7; -.
DR PeptideAtlas; Q8WUQ7; -.
DR PRIDE; Q8WUQ7; -.
DR ProteomicsDB; 74701; -. [Q8WUQ7-1]
DR ProteomicsDB; 74702; -. [Q8WUQ7-2]
DR Antibodypedia; 52584; 89 antibodies from 19 providers.
DR DNASU; 58509; -.
DR Ensembl; ENST00000221899.7; ENSP00000221899.4; ENSG00000105298.14. [Q8WUQ7-1]
DR Ensembl; ENST00000248420.9; ENSP00000248420.5; ENSG00000105298.14. [Q8WUQ7-1]
DR Ensembl; ENST00000429344.7; ENSP00000415078.1; ENSG00000105298.14. [Q8WUQ7-1]
DR Ensembl; ENST00000585942.5; ENSP00000465751.1; ENSG00000105298.14. [Q8WUQ7-1]
DR GeneID; 58509; -.
DR KEGG; hsa:58509; -.
DR MANE-Select; ENST00000429344.7; ENSP00000415078.1; NM_001080543.2; NP_001074012.1.
DR UCSC; uc002lyh.4; human. [Q8WUQ7-1]
DR CTD; 58509; -.
DR DisGeNET; 58509; -.
DR GeneCards; CACTIN; -.
DR HGNC; HGNC:29938; CACTIN.
DR HPA; ENSG00000105298; Low tissue specificity.
DR MIM; 618536; gene.
DR neXtProt; NX_Q8WUQ7; -.
DR OpenTargets; ENSG00000105298; -.
DR PharmGKB; PA134932683; -.
DR VEuPathDB; HostDB:ENSG00000105298; -.
DR eggNOG; KOG2370; Eukaryota.
DR GeneTree; ENSGT00950000183102; -.
DR HOGENOM; CLU_011759_0_0_1; -.
DR InParanoid; Q8WUQ7; -.
DR OMA; HEPYMLL; -.
DR OrthoDB; 1252926at2759; -.
DR PhylomeDB; Q8WUQ7; -.
DR TreeFam; TF300906; -.
DR PathwayCommons; Q8WUQ7; -.
DR SignaLink; Q8WUQ7; -.
DR BioGRID-ORCS; 58509; 707 hits in 1085 CRISPR screens.
DR ChiTaRS; CACTIN; human.
DR GeneWiki; C19orf29; -.
DR GenomeRNAi; 58509; -.
DR Pharos; Q8WUQ7; Tbio.
DR PRO; PR:Q8WUQ7; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; Q8WUQ7; protein.
DR Bgee; ENSG00000105298; Expressed in sural nerve and 190 other tissues.
DR ExpressionAtlas; Q8WUQ7; baseline and differential.
DR Genevisible; Q8WUQ7; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0005681; C:spliceosomal complex; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0071347; P:cellular response to interleukin-1; IDA:UniProtKB.
DR GO; GO:0071222; P:cellular response to lipopolysaccharide; IDA:UniProtKB.
DR GO; GO:0071356; P:cellular response to tumor necrosis factor; IDA:UniProtKB.
DR GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0043124; P:negative regulation of I-kappaB kinase/NF-kappaB signaling; IDA:UniProtKB.
DR GO; GO:0045824; P:negative regulation of innate immune response; IBA:GO_Central.
DR GO; GO:0032688; P:negative regulation of interferon-beta production; IMP:UniProtKB.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IDA:UniProtKB.
DR GO; GO:0031665; P:negative regulation of lipopolysaccharide-mediated signaling pathway; IMP:UniProtKB.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:UniProtKB.
DR GO; GO:0001933; P:negative regulation of protein phosphorylation; IMP:UniProtKB.
DR GO; GO:0034122; P:negative regulation of toll-like receptor signaling pathway; IDA:UniProtKB.
DR GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IDA:UniProtKB.
DR GO; GO:0060339; P:negative regulation of type I interferon-mediated signaling pathway; IMP:UniProtKB.
DR InterPro; IPR019134; Cactin_C.
DR InterPro; IPR018816; Cactin_central.
DR Pfam; PF10312; Cactin_mid; 1.
DR Pfam; PF09732; CactinC_cactus; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Coiled coil; Cytoplasm;
KW Developmental protein; Immunity; Innate immunity; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Spliceosome; Ubl conjugation.
FT CHAIN 1..758
FT /note="Cactin"
FT /id="PRO_0000231617"
FT REGION 1..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 155..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 135..185
FT /evidence="ECO:0000255"
FT COILED 225..277
FT /evidence="ECO:0000255"
FT COMPBIAS 10..53
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 54..69
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 521..536
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9CS00"
FT MOD_RES 476
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 559
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CROSSLNK 469
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 484
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 758
FT /note="R -> RPGPCWRPIRHCRRDPLWTPTLCRDWPPTHPVLAGGVHFPAAGIPPP
FT GLLTGPWSMRPVTPSFAHIRTVAPSHSPFSGQEGRGPHGCHSPGRSGPAGRLVLQHPTG
FT TSPTEAKRKVPPGPPEGHPTSPVTSPRPPTAPPRHPASSGNSSVCFSKKTCRWEKKSFV
FT LMELAYWQDRMFF (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_017856"
FT CONFLICT 499
FT /note="A -> V (in Ref. 4; AAH19848)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 758 AA; 88702 MW; F540F151EB96BEFB CRC64;
MGRDTRSRSR SAGRRGRRRQ SQSGSRSRSR SHGRRNRRRR EDEGRRRRRR RSRERRSDSE
EERWQRSGMR SRSPPRPKWH SRDGSSQSDS GEEQSRGQWA RRRRRARSWS PSSSASSSAS
PGRSQSPRAA AAALSQQQSL QERLRLREER KQQEELMKAF ETPEEKRARR LAKKEAKERK
KREKMGWGEE YMGYTNTDNP FGDNNLLGTF IWNKALEKKG ISHLEEKELK ERNKRIQEDN
RLELQKVKQL RLEREREKAM REQELEMLQR EKEAEHFKTW EEQEDNFHLQ QAKLRSKIRI
RDGRAKPIDL LAKYISAEDD DLAVEMHEPY TFLNGLTVAD MEDLLEDIQV YMELEQGKNA
DFWRDMTTIT EDEISKLRKL EASGKGPGER REGVNASVSS DVQSVFKGKT YNQLQVIFQG
IEGKIRAGGP NLDMGYWESL LQQLRAHMAR ARLRERHQDV LRQKLYKLKQ EQGVESEPLF
PILKQEPQSP SRSLEPEDAA PTPPGPSSEG GPAEAEVDGA TPTEGDGDGD GEGEGEGEAV
LMEEDLIQQS LDDYDAGRYS PRLLTAHELP LDAHVLEPDE DLQRLQLSRQ QLQVTGDASE
SAEDIFFRRA KEGMGQDEAQ FSVEMPLTGK AYLWADKYRP RKPRFFNRVH TGFEWNKYNQ
THYDFDNPPP KIVQGYKFNI FYPDLIDKRS TPEYFLEACA DNKDFAILRF HAGPPYEDIA
FKIVNREWEY SHRHGFRCQF ANGIFQLWFH FKRYRYRR
