ARVC_RAT
ID ARVC_RAT Reviewed; 973 AA.
AC B4F7F3;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Splicing regulator ARVCF {ECO:0000305};
DE AltName: Full=Armadillo repeat protein deleted in velo-cardio-facial syndrome homolog {ECO:0000305};
GN Name=Arvcf {ECO:0000312|RGD:1306655};
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 {ECO:0000312|EMBL:AAI68253.1};
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].
RC TISSUE=Prostate {ECO:0000312|EMBL:AAI68253.1};
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] {ECO:0007744|PubMed:22673903}
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).
RN [4]
RP TISSUE SPECIFICITY.
RX PubMed=29445566; DOI=10.5826/dpc.0801a01;
RA Abreu-Velez A.M., Gao W., Howard M.S.;
RT "Patients affected by endemic pemphigus foliaceus in Colombia, South
RT America exhibit autoantibodies to optic nerve sheath envelope cell
RT junctions.";
RL Dermatol. Pract. Concept. 8:1-6(2018).
RN [5]
RP TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=31384490; DOI=10.5826/dpc.0903a02;
RA Abreu-Velez A.M., Upegui-Zapata Y.A., Valencia-Yepes C.A.,
RA Upegui-Quiceno E., Jimenez-Echavarria A.M., Nino-Pulido C.D., Smoller B.R.,
RA Howard M.S.;
RT "Involvement of the Areae Compositae of the Heart in Endemic Pemphigus
RT Foliaceus.";
RL Dermatol. Pract. Concept. 9:181-186(2019).
CC -!- FUNCTION: Contributes to the regulation of alternative splicing of pre-
CC mRNAs. {ECO:0000250|UniProtKB:O00192}.
CC -!- SUBUNIT: Component of a ribonucleoprotein complex containing mRNAs and
CC RNA-binding proteins including DDX5, HNRNPH2 and SRSF1 as well as ARVCF
CC (By similarity). Interacts (via the extreme C-terminus) with FRMPD2
CC (via the PDZ 2 domain). Interacts with CCDC85B (By similarity).
CC {ECO:0000250|UniProtKB:O00192}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:O00192}. Nucleus {ECO:0000250|UniProtKB:O00192}.
CC Cytoplasm {ECO:0000250|UniProtKB:O00192}. Note=In heart, localizes at
CC area composita, the mixed-type junctional structure composed of both
CC desmosomal and adherens junctional proteins.
CC {ECO:0000269|PubMed:31384490}.
CC -!- TISSUE SPECIFICITY: Expressed in optic nerve sheath envelope (at
CC protein level) (PubMed:29445566). Expressed in heart (at protein level)
CC (PubMed:31384490). {ECO:0000269|PubMed:29445566,
CC ECO:0000269|PubMed:31384490}.
CC -!- SIMILARITY: Belongs to the beta-catenin family. {ECO:0000305}.
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DR EMBL; AC121199; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC168253; AAI68253.1; -; mRNA.
DR RefSeq; NP_001124485.1; NM_001131013.1.
DR AlphaFoldDB; B4F7F3; -.
DR SMR; B4F7F3; -.
DR STRING; 10116.ENSRNOP00000047113; -.
DR PhosphoSitePlus; B4F7F3; -.
DR SwissPalm; B4F7F3; -.
DR jPOST; B4F7F3; -.
DR PaxDb; B4F7F3; -.
DR PeptideAtlas; B4F7F3; -.
DR PRIDE; B4F7F3; -.
DR GeneID; 303798; -.
DR KEGG; rno:303798; -.
DR CTD; 421; -.
DR RGD; 1306655; Arvcf.
DR VEuPathDB; HostDB:ENSRNOG00000001888; -.
DR eggNOG; KOG1048; Eukaryota.
DR HOGENOM; CLU_009111_1_0_1; -.
DR InParanoid; B4F7F3; -.
DR OMA; CGQPLPM; -.
DR OrthoDB; 233858at2759; -.
DR TreeFam; TF321877; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Bgee; ENSRNOG00000001888; Expressed in pancreas and 19 other tissues.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:1990124; C:messenger ribonucleoprotein complex; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:RGD.
DR GO; GO:0045296; F:cadherin binding; ISS:UniProtKB.
DR GO; GO:0016339; P:calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules; IEA:InterPro.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; ISS:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR000225; Armadillo.
DR InterPro; IPR028444; ARVCF.
DR InterPro; IPR028435; Plakophilin/d_Catenin.
DR PANTHER; PTHR10372; PTHR10372; 1.
DR PANTHER; PTHR10372:SF5; PTHR10372:SF5; 1.
DR Pfam; PF00514; Arm; 4.
DR SMART; SM00185; ARM; 6.
DR SUPFAM; SSF48371; SSF48371; 1.
DR PROSITE; PS50176; ARM_REPEAT; 3.
PE 1: Evidence at protein level;
KW Cell adhesion; Cell junction; Cytoplasm; Methylation; mRNA processing;
KW mRNA splicing; Nucleus; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..973
FT /note="Splicing regulator ARVCF"
FT /id="PRO_0000455122"
FT REPEAT 349..388
FT /note="ARM 1"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT REPEAT 391..430
FT /note="ARM 2"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT REPEAT 434..468
FT /note="ARM 3"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT REPEAT 469..509
FT /note="ARM 4"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT REPEAT 527..566
FT /note="ARM 5"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT REPEAT 576..623
FT /note="ARM 6"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT REPEAT 641..681
FT /note="ARM 7"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT REPEAT 694..733
FT /note="ARM 8"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT REPEAT 734..776
FT /note="ARM 9"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT REPEAT 777..821
FT /note="ARM 10"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT REGION 95..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 233..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..331
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 593..623
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 771..955
FT /note="Required for interaction with RNA-binding proteins
FT DDX5, HNRNPH2 and SRSF1 and with mRNAs"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT REGION 844..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 608..624
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 99..116
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..314
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 607..623
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 844..863
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 895..916
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 105
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 171
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT MOD_RES 333
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT MOD_RES 336
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT MOD_RES 344
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 346
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 607
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 637
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P98203"
FT MOD_RES 865
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
FT MOD_RES 866
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O00192"
SQ SEQUENCE 973 AA; 105487 MW; 3F2F3A7CF8658E9E CRC64;
MEDCNVHSAA SILASVKEQE ARFERLTRAL EQERRHVALQ LERAQQPGMS SGGMVGSGQP
LPMAWQQLVL QEQSPGSQAS LATMPEAPEV LEETVTVEED PGTPTSHVSI VTSEDGTTRR
TETKVTKTVK TVTTRTVRQV PLGPDGLPLL DGGPPLGSFA DGPLDRHYVL RGGGPAATLS
RAYLSSGGGF PDGPEPRDIP SYGSLSRGLG VRPPRTGLLG PGPGDGCFTL PGRREAFPMG
SESGPPSGRS LPEHFQAEPY GLEDDTRSLA ADDEGGPDLE PDYSTATRRR PEYGRGLRAR
ALEDTADDTG ELVEERPPFP AATAPLAQPE RGSLGSLDRV VRRSPSVDST RKEPRWRDPE
LPEVLAMLRH PVDPVKANAA AYLQHLCFEN EGIKRRVRQL RGLPLLVALL DHPRAEVRRR
ACGALRNLSY GRDADNKAAI RDCGGVPALV RLLRAARDNE VRELVTGTLW NLSSYEPLKM
VIIDHGLQTL THEVIVPHSG WEREPNEDSK PRDAEWTTVF KNTSGCLRNV SSDGAEARRR
LRECEGLVDA LLHALQSAVG RKDTDNKSVE NCVCIMRNLS YHVHKEVPGA DRYQEVEPGI
PGSAATSQRR RKDDASCFGG KKAKGKKDAE ADRNFDTLDL PKRTEAAKGF ELLYQPEVVR
LYLSLLTESR NFNTLEAAAG ALQNLSAGNW MWATYIRATV RKERGLPVLV ELLQSETDKV
VRAVAIALRN LSLDQRNKDL IGSYAMTELV RNVRNAQAPA HPSAHLEEDT VVAVLNTIHE
IVSDSLDNAR SLLQARGVPA LVALVASSQS VREAKAASHV LQTVWSYKEL RGALQRDGWT
KAHFQSASTA KGPKGTPNSG GFDDSTLPLV DKNLDGEKST TRDVIPMDTL GPDGYSTVDR
RERRTLGSDS IGDSSEKELL KGPGPAVCSS DHMEVIGRGP SGTDPVLGPG APPFCVGLAK
PLVYLALPSS LLS
