ARP21_MOUSE
ID ARP21_MOUSE Reviewed; 807 AA.
AC Q9DCB4; A1A561; Q3UUU8; Q7TS83; Q8BLD1; Q8BWM1; Q8C018; Q8C038; Q8C0Y6;
AC Q91Y59;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 136.
DE RecName: Full=cAMP-regulated phosphoprotein 21;
DE Short=ARPP-21;
DE AltName: Full=Regulator of calmodulin signaling;
DE AltName: Full=Thymocyte cAMP-regulated phosphoprotein;
GN Name=Arpp21; Synonyms=Rcs, Tarpp;
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), TISSUE SPECIFICITY, INDUCTION, AND
RP SUBCELLULAR LOCATION.
RC TISSUE=Thymus;
RX PubMed=11298339;
RX DOI=10.1002/1521-4141(200104)31:4<1141::aid-immu1141>3.0.co;2-r;
RA Kisielow J., Nairn A.C., Karjalainen K.;
RT "TARPP, a novel protein that accompanies TCR gene rearrangement and
RT thymocyte education.";
RL Eur. J. Immunol. 31:1141-1149(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4; 6; 7; 8 AND 9), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-807 (ISOFORM 5).
RC STRAIN=C57BL/6J;
RC TISSUE=Brain, Corpora quadrigemina, Head, Olfactory bulb, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 10).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Retina;
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 PROTEIN SEQUENCE OF 55-61 AND 201-227, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION AT SER-55.
RX PubMed=10854908; DOI=10.1016/s0028-3908(99)00230-0;
RA Caporaso G.L., Bibb J.A., Snyder G.L., Valle C., Rakhilin S.,
RA Fienberg A.A., Hemmings H.C. Jr., Nairn A.C., Greengard P.;
RT "Drugs of abuse modulate the phosphorylation of ARPP-21, a cyclic AMP-
RT regulated phosphoprotein enriched in the basal ganglia.";
RL Neuropharmacology 39:1637-1644(2000).
RN [6]
RP METHYLATION AT ARG-650, MUTAGENESIS OF ARG-650, AND SUBCELLULAR LOCATION.
RX PubMed=15096520; DOI=10.1074/jbc.m402544200;
RA Kim J., Lee J., Yadav N., Wu Q., Carter C., Richard S., Richie E.,
RA Bedford M.T.;
RT "Loss of CARM1 results in hypomethylation of thymocyte cyclic AMP-regulated
RT phosphoprotein and deregulated early T cell development.";
RL J. Biol. Chem. 279:25339-25344(2004).
RN [7]
RP INTERACTION WITH CALM1, FUNCTION, AND PHOSPHORYLATION AT SER-55.
RX PubMed=15499021; DOI=10.1126/science.1099961;
RA Rakhilin S.V., Olson P.A., Nishi A., Starkova N.N., Fienberg A.A.,
RA Nairn A.C., Surmeier D.J., Greengard P.;
RT "A network of control mediated by regulator of calcium/calmodulin-dependent
RT signaling.";
RL Science 306:698-701(2004).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-133; SER-298; SER-361
RP AND SER-557, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-265 (ISOFORM 4),
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Lung;
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).
CC -!- FUNCTION: [Isoform 2]: May act as a competitive inhibitor of
CC calmodulin-dependent enzymes such as calcineurin in neurons.
CC {ECO:0000269|PubMed:15499021}.
CC -!- SUBUNIT: Interacts with CALM1. {ECO:0000269|PubMed:15499021}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11298339,
CC ECO:0000269|PubMed:15096520}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1; Synonyms=TARPP;
CC IsoId=Q9DCB4-1; Sequence=Displayed;
CC Name=2; Synonyms=ARPP-21, RCS;
CC IsoId=Q9DCB4-2; Sequence=VSP_029477, VSP_029478;
CC Name=3;
CC IsoId=Q9DCB4-3; Sequence=VSP_029485, VSP_029490;
CC Name=4;
CC IsoId=Q9DCB4-4; Sequence=VSP_029485, VSP_029488, VSP_029490;
CC Name=5;
CC IsoId=Q9DCB4-5; Sequence=VSP_029485;
CC Name=6;
CC IsoId=Q9DCB4-6; Sequence=VSP_029479, VSP_029480;
CC Name=7;
CC IsoId=Q9DCB4-7; Sequence=VSP_029487, VSP_029489;
CC Name=8;
CC IsoId=Q9DCB4-8; Sequence=VSP_029483, VSP_029484;
CC Name=9;
CC IsoId=Q9DCB4-9; Sequence=VSP_029479, VSP_029481, VSP_029491,
CC VSP_029492;
CC Name=10;
CC IsoId=Q9DCB4-10; Sequence=VSP_029482, VSP_029486;
CC -!- TISSUE SPECIFICITY: [Isoform 1]: Present at high levels in thymus and
CC low levels in brain. In thymus, isoform 1 is specifically found in
CC immature thymocytes (at protein level). {ECO:0000269|PubMed:11298339}.
CC -!- INDUCTION: [Isoform 1]: Down-regulated in thymocytes upon TCR
CC engagement (at protein level). {ECO:0000269|PubMed:11298339}.
CC -!- PTM: Phosphorylation of isoform 2 at Ser-55 is enhanced upon dopamine
CC D1 receptor activation and favors interaction with CALM1.
CC {ECO:0000269|PubMed:10854908, ECO:0000269|PubMed:15499021}.
CC -!- PTM: [Isoform 1]: Methylated by CARM1 at Arg-650 in immature
CC thymocytes. {ECO:0000305|PubMed:15096520}.
CC -!- MISCELLANEOUS: [Isoform 10]: May be produced at very low levels due to
CC a premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
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DR EMBL; AF324451; AAK48713.1; -; mRNA.
DR EMBL; AK002950; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK029467; BAC26463.1; -; mRNA.
DR EMBL; AK032417; BAC27859.1; -; mRNA.
DR EMBL; AK032543; BAC27918.1; -; mRNA.
DR EMBL; AK045507; BAC32399.1; -; mRNA.
DR EMBL; AK050613; BAC34343.1; -; mRNA.
DR EMBL; AK137974; BAE23526.1; -; mRNA.
DR EMBL; BC027107; AAH27107.1; -; mRNA.
DR EMBL; BC053001; AAH53001.1; -; mRNA.
DR EMBL; BC128376; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS23587.1; -. [Q9DCB4-1]
DR CCDS; CCDS40786.1; -. [Q9DCB4-2]
DR CCDS; CCDS52943.1; -. [Q9DCB4-9]
DR CCDS; CCDS52944.1; -. [Q9DCB4-4]
DR CCDS; CCDS52945.1; -. [Q9DCB4-3]
DR CCDS; CCDS52946.1; -. [Q9DCB4-8]
DR RefSeq; NP_001171086.1; NM_001177615.1. [Q9DCB4-2]
DR RefSeq; NP_001171087.1; NM_001177616.1. [Q9DCB4-4]
DR RefSeq; NP_001171088.1; NM_001177617.1.
DR RefSeq; NP_001171089.1; NM_001177618.1. [Q9DCB4-3]
DR RefSeq; NP_001171090.1; NM_001177619.1.
DR RefSeq; NP_001171091.1; NM_001177620.1. [Q9DCB4-2]
DR RefSeq; NP_001171094.1; NM_001177623.1. [Q9DCB4-8]
DR RefSeq; NP_083031.1; NM_028755.3. [Q9DCB4-2]
DR RefSeq; NP_150289.1; NM_033264.2. [Q9DCB4-1]
DR RefSeq; XP_006512407.1; XM_006512344.3. [Q9DCB4-3]
DR RefSeq; XP_006512411.1; XM_006512348.3. [Q9DCB4-1]
DR RefSeq; XP_006512413.1; XM_006512350.3. [Q9DCB4-4]
DR RefSeq; XP_006512414.1; XM_006512351.3. [Q9DCB4-5]
DR RefSeq; XP_006512424.1; XM_006512361.3.
DR RefSeq; XP_006512425.1; XM_006512362.3.
DR RefSeq; XP_017169139.1; XM_017313650.1. [Q9DCB4-3]
DR RefSeq; XP_017169140.1; XM_017313651.1.
DR RefSeq; XP_017169141.1; XM_017313652.1.
DR RefSeq; XP_017169142.1; XM_017313653.1.
DR RefSeq; XP_017169146.1; XM_017313657.1.
DR RefSeq; XP_017169148.1; XM_017313659.1.
DR RefSeq; XP_017169149.1; XM_017313660.1.
DR RefSeq; XP_017169152.1; XM_017313663.1.
DR AlphaFoldDB; Q9DCB4; -.
DR SMR; Q9DCB4; -.
DR BioGRID; 216492; 1.
DR iPTMnet; Q9DCB4; -.
DR PhosphoSitePlus; Q9DCB4; -.
DR jPOST; Q9DCB4; -.
DR MaxQB; Q9DCB4; -.
DR PeptideAtlas; Q9DCB4; -.
DR PRIDE; Q9DCB4; -.
DR ProteomicsDB; 283233; -. [Q9DCB4-1]
DR ProteomicsDB; 283234; -. [Q9DCB4-2]
DR ProteomicsDB; 283235; -. [Q9DCB4-3]
DR ProteomicsDB; 283236; -. [Q9DCB4-4]
DR ProteomicsDB; 283237; -. [Q9DCB4-5]
DR ProteomicsDB; 283238; -. [Q9DCB4-6]
DR ProteomicsDB; 283239; -. [Q9DCB4-7]
DR ProteomicsDB; 283240; -. [Q9DCB4-8]
DR ProteomicsDB; 283241; -. [Q9DCB4-9]
DR ProteomicsDB; 283242; -. [Q9DCB4-10]
DR Antibodypedia; 2806; 162 antibodies from 27 providers.
DR DNASU; 74100; -.
DR Ensembl; ENSMUST00000035085; ENSMUSP00000035085; ENSMUSG00000032503. [Q9DCB4-4]
DR Ensembl; ENSMUST00000070218; ENSMUSP00000069264; ENSMUSG00000032503. [Q9DCB4-3]
DR Ensembl; ENSMUST00000111872; ENSMUSP00000107503; ENSMUSG00000032503. [Q9DCB4-3]
DR Ensembl; ENSMUST00000161412; ENSMUSP00000125282; ENSMUSG00000032503. [Q9DCB4-8]
DR Ensembl; ENSMUST00000162065; ENSMUSP00000125684; ENSMUSG00000032503. [Q9DCB4-3]
DR Ensembl; ENSMUST00000162097; ENSMUSP00000124502; ENSMUSG00000032503. [Q9DCB4-1]
DR Ensembl; ENSMUST00000164754; ENSMUSP00000125862; ENSMUSG00000032503. [Q9DCB4-1]
DR Ensembl; ENSMUST00000172380; ENSMUSP00000130558; ENSMUSG00000032503. [Q9DCB4-2]
DR Ensembl; ENSMUST00000178410; ENSMUSP00000136769; ENSMUSG00000032503. [Q9DCB4-2]
DR GeneID; 74100; -.
DR KEGG; mmu:74100; -.
DR UCSC; uc009rvx.2; mouse. [Q9DCB4-3]
DR UCSC; uc009rvy.2; mouse. [Q9DCB4-5]
DR UCSC; uc009rvz.2; mouse. [Q9DCB4-1]
DR UCSC; uc009rwa.2; mouse. [Q9DCB4-4]
DR UCSC; uc009rwc.2; mouse. [Q9DCB4-7]
DR UCSC; uc009rwe.2; mouse. [Q9DCB4-8]
DR UCSC; uc009rwf.1; mouse. [Q9DCB4-6]
DR UCSC; uc009rwg.2; mouse. [Q9DCB4-2]
DR CTD; 10777; -.
DR MGI; MGI:107562; Arpp21.
DR VEuPathDB; HostDB:ENSMUSG00000032503; -.
DR GeneTree; ENSGT00940000160796; -.
DR HOGENOM; CLU_007817_1_0_1; -.
DR InParanoid; Q9DCB4; -.
DR OMA; SCRTNCT; -.
DR OrthoDB; 137913at2759; -.
DR PhylomeDB; Q9DCB4; -.
DR TreeFam; TF315915; -.
DR BioGRID-ORCS; 74100; 0 hits in 68 CRISPR screens.
DR ChiTaRS; Arpp21; mouse.
DR PRO; PR:Q9DCB4; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q9DCB4; protein.
DR Bgee; ENSMUSG00000032503; Expressed in caudate-putamen and 168 other tissues.
DR ExpressionAtlas; Q9DCB4; baseline and differential.
DR Genevisible; Q9DCB4; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:CACAO.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR GO; GO:0034605; P:cellular response to heat; IDA:MGI.
DR Gene3D; 3.30.1370.50; -; 1.
DR InterPro; IPR001374; R3H_dom.
DR InterPro; IPR036867; R3H_dom_sf.
DR InterPro; IPR024771; SUZ.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF12752; SUZ; 1.
DR SMART; SM00393; R3H; 1.
DR SUPFAM; SSF82708; SSF82708; 1.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS51673; SUZ; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Calmodulin-binding; Coiled coil;
KW Cytoplasm; Direct protein sequencing; Methylation; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7M2N1"
FT CHAIN 2..807
FT /note="cAMP-regulated phosphoprotein 21"
FT /id="PRO_0000064683"
FT DOMAIN 163..226
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT DOMAIN 227..298
FT /note="SUZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01009"
FT REGION 1..127
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..434
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 474..536
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 595..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..57
FT /evidence="ECO:0000255"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..58
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 85..99
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 360..434
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..515
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 552..567
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 595..619
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:Q7M2N1"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 55
FT /note="Phosphoserine; by PKA"
FT /evidence="ECO:0000269|PubMed:10854908,
FT ECO:0000269|PubMed:15499021"
FT MOD_RES 133
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 298
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 381
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UBL0"
FT MOD_RES 557
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 650
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000269|PubMed:15096520"
FT VAR_SEQ 87..88
FT /note="ES -> TL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029477"
FT VAR_SEQ 89..807
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029478"
FT VAR_SEQ 228
FT /note="I -> M (in isoform 6 and isoform 9)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029479"
FT VAR_SEQ 229..807
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029480"
FT VAR_SEQ 229..330
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029481"
FT VAR_SEQ 229..282
FT /note="PEQRFCEHLKDEKSEESQKRFILKRDNSSIDKEDNQNRMHPFRDDRRSKSIE
FT ER -> QFAPRKAYFWTTGLTETAQEELPGAGRAAQRLSSGGQTTSGLGAAQIRTVPTA
FT I (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029482"
FT VAR_SEQ 229..248
FT /note="PEQRFCEHLKDEKSEESQKR -> VQDTGWRCKHAHRTGAVCTN (in
FT isoform 8)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029483"
FT VAR_SEQ 249..807
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029484"
FT VAR_SEQ 265..297
FT /note="Missing (in isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029485"
FT VAR_SEQ 283..807
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029486"
FT VAR_SEQ 298..371
FT /note="SVCSQESLFLDNSRLQEDMHICNETYKKRQLFRAHRDSSGRTSGSRQSSSET
FT ELRWPDHQRAWSSTDSDSSNRN -> VSSCFNCLLSMVLPSAERPLVARTEIWQGVQRL
FT GARNELQSRKHKCFWERTWFRDALKQSKSLCMCPPGHHLPG (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029487"
FT VAR_SEQ 310..329
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029488"
FT VAR_SEQ 372..807
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029489"
FT VAR_SEQ 543
FT /note="Q -> QSVQSLQPSSQSVQYPAVSFPPQHLLPMSPTQHFPL (in
FT isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_029490"
FT VAR_SEQ 674..703
FT /note="YQPVLSGQQGFQGMMGVQQSAHSQGVMSSQ -> LMIAPDTWPTVPAELALQ
FT KVTLLWISEGRW (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029491"
FT VAR_SEQ 704..807
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_029492"
FT MUTAGEN 650
FT /note="R->A: Abolishes methylation, no effect on
FT subcellular location."
FT /evidence="ECO:0000269|PubMed:15096520"
FT CONFLICT 263
FT /note="N -> NQ (in Ref. 2; BAC26463)"
FT /evidence="ECO:0000305"
FT MOD_RES Q9DCB4-4:265
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 807 AA; 88567 MW; 99DD32A59954E139 CRC64;
MSEQGGLTPT ILEEGQTEPE SAPENGILKS ESLDEEEKLE LQRRLAAQNQ ERRKSKSGAG
KGKLTRSLAV CEESSARSGG ESHQDQESIH LQLSSFPSLQ EEDKSRKDDS EREKEKDKNR
EKLSERPKIR MLSKDCSQEY TDSTGIDLHG FLINTLKNNS RDRMILLKME QEMIDFIADS
NNHYKKFPQM SSYQRMLVHR VAAYFGLDHN VDQTGKSVII NKTSSTRIPE QRFCEHLKDE
KSEESQKRFI LKRDNSSIDK EDNQNRMHPF RDDRRSKSIE EREEEYQRVR ERIFAHDSVC
SQESLFLDNS RLQEDMHICN ETYKKRQLFR AHRDSSGRTS GSRQSSSETE LRWPDHQRAW
SSTDSDSSNR NLKPTMTKTA SFGGITVLTR GDSTSSTRSA GKLSKTGSES SSSAGSSGSL
SRTHPQSTAL TSSVAAGSPG CMAYSENGMG GQVPPSSTSY ILLPLESATG IPPGSILLNP
HTGQPFVNPD GTPAIYNPPG SQQTLRGTVG GQPQQPPQQQ PSPQPQQQVQ ASQPQMAGPL
VTQREELAAQ FSQLSMSRQS SGDTPEPPSG TVYPASLLPQ TAQPQSYVIT SAGQQLSTGG
FSDSGPPISQ QVLQAPPSPQ GFVQQPPPAQ MSVYYYPSGQ YPTSTSQQYR PLASVQYSAQ
RSQQIPQTTQ QAGYQPVLSG QQGFQGMMGV QQSAHSQGVM SSQQGAPVHG VMVSYPTMSS
YQVPMTQGSQ AVPQQTYQPP IMLPSQAGQG SLPATGMPVY CNVTPPNPQN NLRLMGPHCP
SSTVPVMSAS CRTNCGNVSN AGWQVKF
