CABIN_RAT
ID CABIN_RAT Reviewed; 2182 AA.
AC O88480;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 25-MAY-2022, entry version 144.
DE RecName: Full=Calcineurin-binding protein cabin-1;
DE AltName: Full=Calcineurin inhibitor;
DE Short=CAIN;
GN Name=Cabin1;
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 [MRNA], FUNCTION, INTERACTION WITH CALCINEURIN,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RC TISSUE=Hippocampus;
RX PubMed=9660798; DOI=10.1074/jbc.273.29.18325;
RA Lai M.M., Burnett P.E., Wolosker H., Blackshaw S., Snyder S.H.;
RT "Cain, a novel physiologic protein inhibitor of calcineurin.";
RL J. Biol. Chem. 273:18325-18331(1998).
RN [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2003, AND IDENTIFICATION BY
RP 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: May be required for replication-independent chromatin
CC assembly (By similarity). May serve as a negative regulator of T-cell
CC receptor (TCR) signaling via inhibition of calcineurin. {ECO:0000250,
CC ECO:0000269|PubMed:9660798}.
CC -!- SUBUNIT: Component of a complex that includes at least ASF1A, CABIN1,
CC HIRA, histone H3.3 and UBN1 (By similarity). Interacts with MEF2B (By
CC similarity). Interacts with calcineurin. {ECO:0000250,
CC ECO:0000269|PubMed:9660798}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm
CC {ECO:0000269|PubMed:9660798}.
CC -!- TISSUE SPECIFICITY: Widely expressed with prominent expression in
CC neurons. {ECO:0000269|PubMed:9660798}.
CC -!- PTM: Activated through PKC-mediated hyperphosphorylation.
CC {ECO:0000250}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF061947; AAC40176.1; -; mRNA.
DR PIR; T14320; T14320.
DR RefSeq; NP_446027.2; NM_053575.2.
DR AlphaFoldDB; O88480; -.
DR SMR; O88480; -.
DR STRING; 10116.ENSRNOP00000001659; -.
DR iPTMnet; O88480; -.
DR PhosphoSitePlus; O88480; -.
DR PaxDb; O88480; -.
DR PRIDE; O88480; -.
DR GeneID; 94165; -.
DR KEGG; rno:94165; -.
DR UCSC; RGD:620263; rat.
DR CTD; 23523; -.
DR RGD; 620263; Cabin1.
DR eggNOG; ENOG502QPUI; Eukaryota.
DR InParanoid; O88480; -.
DR OrthoDB; 56555at2759; -.
DR PhylomeDB; O88480; -.
DR Reactome; R-RNO-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
DR PRO; PR:O88480; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IMP:RGD.
DR GO; GO:0030346; F:protein phosphatase 2B binding; IDA:RGD.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; TAS:RGD.
DR GO; GO:0006336; P:DNA replication-independent chromatin assembly; ISO:RGD.
DR GO; GO:0060548; P:negative regulation of cell death; IDA:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR CDD; cd13839; MEF2_binding; 1.
DR Gene3D; 1.25.40.10; -; 2.
DR InterPro; IPR033053; Hir3/CABIN1.
DR InterPro; IPR015134; MEF2-bd.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR PANTHER; PTHR15502; PTHR15502; 1.
DR Pfam; PF09047; MEF2_binding; 1.
DR SMART; SM00028; TPR; 5.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 4.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Chromatin regulator; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..2182
FT /note="Calcineurin-binding protein cabin-1"
FT /id="PRO_0000106276"
FT REPEAT 36..69
FT /note="TPR 1"
FT REPEAT 90..123
FT /note="TPR 2"
FT REPEAT 125..157
FT /note="TPR 3"
FT REPEAT 615..648
FT /note="TPR 4"
FT REPEAT 1055..1088
FT /note="TPR 5"
FT REPEAT 1106..1139
FT /note="TPR 6"
FT REGION 356..400
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1299..1496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1671..1848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1917..2035
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2054..2126
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2078..2115
FT /note="Required for interaction with calcineurin"
FT REGION 2160..2182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..400
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1299..1321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1329..1348
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1357..1371
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1372..1397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1428..1444
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1741..1756
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1798..1812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1981..1997
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2054..2079
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2168..2182
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 10
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6J0"
FT MOD_RES 11
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6J0"
FT MOD_RES 12
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6J0"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6J0"
FT MOD_RES 673
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6J0"
FT MOD_RES 1439
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6J0"
FT MOD_RES 2003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 2113
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6J0"
FT MOD_RES 2116
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9Y6J0"
SQ SEQUENCE 2182 AA; 242813 MW; 2904C335AB3F440A CRC64;
MIRIAALNAS STIEDDHEGS FKSHKIQTKE AQEAEAFALY HKALDLQKHD RFEESAKAYH
ELLEARLLRE AVSSGDEKEG LKHPGLILKY STYKNLAQLA AQREDLETAM EFYLEAVMLD
STDVNLWYKI GHVALRLIRL PLARHAFEEG LRCNPDHWPC LDNLITVLYT LSDYTTCLYF
ICKALEKDCR YSKGLVLKEK IFEEQPCLRK DSLRMFLKCD MSVHEVSVNA AETQAIVDEA
LGLRKKRQAL IVREKEPDLK LVQPIPFFTW KCLGESLLAM YNHLTTCEPP RPSLGKRIDL
SDYQDPSQLL APSIVVTPVS VVQPSPVCTN PTVAVAEPVL SYTSVTTTSF PLHSPGLLDT
GTPMGDVSGG DKSKKGVKRK KTLEESGETA KRRSARVRNT KCKKEEKVDF QGLLVKFLPS
RLRKLDPEEE DDPFNNYEVQ SEAKLESFSN VGPHRLSFDS ATFMESEKQD VHAFLMENLT
NGGVLELMMR YLKSMGHKFL LKWPPGLAEV VLSVYHSWRR HSTSLPNPLL RDCSNKHIKD
MMLMSLSCME LQLDQWLLTK GRSSTVSPRN CPAGVVTGRF GPDFPGTHCL GDLLQLSFAS
SQRDLFEDGW LEFVVRVYWL KARFLALQGD MEQALENYDI CTEILQSSTA LQAQAGAEQR
DIVIRLPNLH NDSIVSLEEI DKNLKSLERC QSLEEIQRLF EAGDYKAVVQ LLRPTLCTSG
FDRAKHLEFM TSIPERPAQL LLLQDSLLRL EEHRQCFECS DVALNEAVQQ MLNSSDSAAK
EEWAATVTQL LLGMEQALSS DSRGSILKES SSPTGLVRLT NNLIQVIDCS MAVQEEPKEP
YVSSVLPWII LHRIIWQEED TFRSLCHQQQ LQNPTEEGIS EMPMLPSSLM LLNTAHEYLG
RRSWCCNSDG ALLRFYVHVL QKELAASASE DTHPYKEELE TALEQCFYCL YSFPSKKSKA
RYLEEHSAQQ VDLTWEDALF MFEYFKPKTL PEFDSYKTST VSADLANLLK RIATIVPRTE
KPALSMDKVS AYIEGTSAEV PCLPDGADPA PPVLNELYYL LADYHFKNKE QSKAIKFYMH
DICICPNRFD SWAGMALARA SRIQDKLNSN ELKSDGPIWR HATPVLNCFR RALEIDSSNL
SLWIEYGTMS YALHSFASRQ LKQWRAELPP EVVQQMEDRR DSMLETARHC FTSAAHCEGD
GDEEEWLIHY MLGKVAEKQQ QPPTVYLLHY RQAGHYLHEE AARYPKKIHY HNPPELAMEA
LEVYFRLHAS ILKLLGKPDS GVSAEVLVSF MKEAAEGPFA RGEEKNTPKA SEKEKACLVD
EDSHSSAGTL PGPGASLPSS SGPGLTSPPY TATPIDHDYV KCKKPRQQAT PDDRSQDSTA
VALSDSSSTQ DFFNEPTSLL DGSRKLLPEK RISGLSAQAG PSGKDLPGPT EERGKTEESL
ESTEAFRVVE PSVQKPVADS SASAYIPSKP AVSTPPPWDG KKRSDPLGEP VAFPQGLPAG
AEEQRQFLTE QCIASFCLCL SRFPQHYKSL YRLAFLYTYS KTHRNLQWAR DVLLGSSIPW
QQLQHMPAQG LFCERNKTNF FNGIWRIPVD EIDRPGSFAW HMNRSIVLLL KVLAQLRDHS
TLLKVSSMLQ RTPDQGKKYL RDADRQVLAQ RAFILTVKVL EDTLSELAEG LEHPGSKACG
LSGARMTTDV SHKASPEDGQ ESLPHPKKLP LADGSGPGPE PGGKVGPLHQ LPVATDTRDN
TEQGGEPKDK ERPPVGPTEP MDTGETAARH PDLEPTPRLL PGRPPRDRGP ESRSAELSLE
ELSISTRQQP APLVPSPVTP TTAAPTTMGA RAAGHPEEAP PRPNRKRKLL QDTESGKTLL
LDAYRVWQQG QKAMAYDLSR IEKIMSETYM LIKQVDEETA LEQAVKFCQV HLGAAAQRQA
SGDAPTTPKH PKDSRENFFP ATVAPSAPDT TAPDALQRPS DSHLKPGLAA AITCPPSASA
STPDPGIPQP HRPEAVPSRA PLSPDGEEVS GVTEGPSFLS QEPRHSHQMK MAATGPLAEQ
HCWPVEAACQ TGAEPTFSQA TSTKVPSSGS TQTPESHQGK TESSRAKSRL LPNMPKLVIP
SATTKFPPEI TVTPPTPTLL SPKGSISEET KQKLKSAILS AQSAANVRKE SLCQPALEVL
ETSSQESSLE SETDEDDDFM DV
