C2D1A_RAT
ID C2D1A_RAT Reviewed; 941 AA.
AC Q66HA5;
DT 13-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-JUN-2006, sequence version 2.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Coiled-coil and C2 domain-containing protein 1A;
DE AltName: Full=Five prime repressor element under dual repression-binding protein 1;
DE Short=FRE under dual repression-binding protein 1;
DE Short=Freud-1;
GN Name=Cc2d1a;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Lung;
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 [3]
RP TISSUE SPECIFICITY, SUBCELLULAR LOCATION, AND FUNCTION.
RX PubMed=12917378; DOI=10.1523/jneurosci.23-19-07415.2003;
RA Ou X.-M., Lemonde S., Jafar-Nejad H., Bown C.D., Goto A., Rogaeva A.,
RA Albert P.R.;
RT "Freud-1: a neuronal calcium-regulated repressor of the 5-HT1A receptor
RT gene.";
RL J. Neurosci. 23:7415-7425(2003).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-91 AND SER-434, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
CC -!- FUNCTION: Transcription factor that binds specifically to the DRE (dual
CC repressor element) and represses 5-HT1A gene transcription though this
CC element. Mediates HDAC-independent repression of HTR1A promoter. CAMK2G
CC inhibits CC2D1a-induced repression of the HTR1A. May play a role in the
CC altered regulation of 5-HT1A receptors associated with anxiety and
CC major depression. Performs essential function in controlling functional
CC maturation of synapses (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12917378}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:12917378}. Nucleus
CC {ECO:0000269|PubMed:12917378}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q6P1N0}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q66HA5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q66HA5-2; Sequence=VSP_019243;
CC -!- TISSUE SPECIFICITY: Strongly expressed in several brain areas including
CC frontal cortex, cortex, mesencephalon, hippocampus, midbrain and
CC hypothalamus. Also expressed in testis and at low levels in pituitary,
CC liver and kidney. In brain the highest levels are detected in
CC hippocampal pyramidal cells and raphe nuclei.
CC {ECO:0000269|PubMed:12917378}.
CC -!- DOMAIN: The C2 domain is required for the repression. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CC2D1 family. {ECO:0000305}.
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DR EMBL; AABR03113552; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC081948; AAH81948.1; -; mRNA.
DR RefSeq; NP_001013891.1; NM_001013869.1. [Q66HA5-2]
DR RefSeq; XP_006255296.1; XM_006255234.2. [Q66HA5-1]
DR AlphaFoldDB; Q66HA5; -.
DR SMR; Q66HA5; -.
DR IntAct; Q66HA5; 1.
DR MINT; Q66HA5; -.
DR STRING; 10116.ENSRNOP00000009806; -.
DR iPTMnet; Q66HA5; -.
DR PhosphoSitePlus; Q66HA5; -.
DR jPOST; Q66HA5; -.
DR PaxDb; Q66HA5; -.
DR PRIDE; Q66HA5; -.
DR GeneID; 288908; -.
DR KEGG; rno:288908; -.
DR CTD; 54862; -.
DR RGD; 1306108; Cc2d1a.
DR VEuPathDB; HostDB:ENSRNOG00000006747; -.
DR eggNOG; KOG3837; Eukaryota.
DR HOGENOM; CLU_008808_1_0_1; -.
DR InParanoid; Q66HA5; -.
DR OMA; LHRIKIM; -.
DR OrthoDB; 959801at2759; -.
DR PhylomeDB; Q66HA5; -.
DR PRO; PR:Q66HA5; -.
DR Proteomes; UP000002494; Chromosome 19.
DR Bgee; ENSRNOG00000006747; Expressed in frontal cortex and 19 other tissues.
DR Genevisible; Q66HA5; RN.
DR GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR GO; GO:0001650; C:fibrillar center; IEA:Ensembl.
DR GO; GO:0005815; C:microtubule organizing center; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IBA:GO_Central.
DR GO; GO:0001227; F:DNA-binding transcription repressor activity, RNA polymerase II-specific; ISO:RGD.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; ISO:RGD.
DR GO; GO:1905381; P:negative regulation of snRNA transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; ISO:RGD.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR CDD; cd08690; C2_Freud-1; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR037772; C2_Freud.
DR InterPro; IPR039725; CC2D1A/B.
DR InterPro; IPR006608; DM14.
DR PANTHER; PTHR13076; PTHR13076; 1.
DR Pfam; PF00168; C2; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00685; DM14; 4.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; DNA-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Repressor; Transcription;
KW Transcription regulation.
FT CHAIN 1..941
FT /note="Coiled-coil and C2 domain-containing protein 1A"
FT /id="PRO_0000239611"
FT DOMAIN 628..762
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 183..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 301..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 428..482
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 338..384
FT /evidence="ECO:0000255"
FT COILED 475..508
FT /evidence="ECO:0000255"
FT COMPBIAS 225..242
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 305..321
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 91
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 247
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6P1N0"
FT MOD_RES 434
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT VAR_SEQ 125..169
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019243"
SQ SEQUENCE 941 AA; 103587 MW; 17A2DC070FC9217E CRC64;
MHKRNGPQAP PGRGAVTARQ LGLLVDFSPD GLMIPEDGVN DEELEAEFLA LVGGQPQALE
KLKGKGPLPM EAIEKMARLC MRDLDEDEEG TDEDVEADED LLAELNEVLG EERKAVEPAM
PVVQPKPSSP NPGIEATLQE RLILYQSAVE SARQAGDSAK MRRYDRGLKT LENLLVSAKK
GNTINEADIP PPVASGKGPA IGHSHTHTTS HLAPVSPPAP EPSVTLEAPS TTAQTSAKPQ
LSPDPCSPLA RLQSLQHEYK VAALRAKHQD DTATAARYLR VSKSFDPVLE ALSRGELVDL
SRLPPPPDQL SPEPPLPAAQ PVTPASTLTR PEVPQPPKNL LEALEQRMER YHVAAAQAKA
KGDQRKARMH ERIVKQYQDA IRAHKAGRAV DVAELPVPPG FPPIQGLESA EPSQQSLVGV
LETAMKLANH EEGSDEEEEE TPKKNTPAAS TAQPKASPSR APPSGPAPAG KAASKGTSTR
AQQQLAFLEG RKKQLLQAAL RAKQKNDVEG AKMHLRQAKG LEPMLEASRN GLPVDIAKVP
PAPVNKDDFV LVQRPGPGMS QEAVRRYGEL TKLLRQQHEM CLNHSTQFTH LGNIAETIKF
EKLAEDCKRS MDTLKQAFAR SLPTPAARFE QRTFSVIKIF PDLSNNDMLL FIVKGINLPT
PPGLSPSDLD AFVRFDFPYP NVEEAQKDKT SVIKSTDSPE FKEQFKLCIN RGHRGFRRAI
QTKGIKFEVV HKGGLFKTDR VLGTAQLKLD TLETACEVHE ILEVLDGRRP TGGRLEVMVR
IREPLTAQQL ETTTERWLVI DHIPAAVPTV TGPKAKVPLI PASSKEAGNR SSRPLHSLSV
LAFDQERLER KILALRQARR PVPPEVAQQY QDVVQRSQWQ RAQLEQGGAA LRREYASHLE
RQLHFYTEAA RRLGYDGSRE AAKEALYRRN LVESELQRLR R
