ARP21_HUMAN
ID ARP21_HUMAN Reviewed; 812 AA.
AC Q9UBL0; B4DG96; Q49AK3; Q49AS6; Q4G0V4; Q6NYC3; Q86V31; Q9UF93;
DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 2.
DT 03-AUG-2022, entry version 145.
DE RecName: Full=cAMP-regulated phosphoprotein 21;
DE Short=ARPP-21;
DE AltName: Full=Thymocyte cAMP-regulated phosphoprotein;
GN Name=ARPP21; Synonyms=TARPP;
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 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=8120638; DOI=10.1523/jneurosci.14-03-00985.1994;
RA Brene S., Lindefors N., Ehrlich M., Taubes T., Horiuchi A., Kopp J.,
RA Hall H., Sedvall G., Greengard P., Persson H.;
RT "Expression of mRNAs encoding ARPP-16/19, ARPP-21, and DARPP-32 in human
RT brain tissue.";
RL J. Neurosci. 14:985-998(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Hypothalamus;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H., Gu B.-W.,
RA Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J., Xu S.-H., Gu J.,
RA Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M., Huang G.-Y., Chen Z.,
RA Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal axis
RT and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Amygdala;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 4; 5 AND 6).
RC TISSUE=Hippocampus, Lung, and Testis;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 162-812 (ISOFORM 3).
RC TISSUE=Kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [8]
RP TISSUE SPECIFICITY, AND METHYLATION AT ARG-655.
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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-383 AND SER-562, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
CC -!- FUNCTION: Isoform 2 may act as a competitive inhibitor of calmodulin-
CC dependent enzymes such as calcineurin in neurons. {ECO:0000250}.
CC -!- SUBUNIT: Interacts with CALM1. {ECO:0000250}.
CC -!- INTERACTION:
CC Q9UBL0-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-25931672, EBI-5235340;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1; Synonyms=TARPP;
CC IsoId=Q9UBL0-1; Sequence=Displayed;
CC Name=2; Synonyms=ARPP-21;
CC IsoId=Q9UBL0-2; Sequence=VSP_029471, VSP_029472;
CC Name=3;
CC IsoId=Q9UBL0-3; Sequence=VSP_029474, VSP_029476;
CC Name=4;
CC IsoId=Q9UBL0-4; Sequence=VSP_029474, VSP_029475, VSP_029476;
CC Name=5;
CC IsoId=Q9UBL0-5; Sequence=VSP_029469, VSP_029476;
CC Name=6;
CC IsoId=Q9UBL0-6; Sequence=VSP_029470, VSP_029473;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in brain. Isoform 1 is
CC present in immature thymocytes (at protein level).
CC {ECO:0000269|PubMed:15096520, ECO:0000269|PubMed:8120638}.
CC -!- PTM: Phosphorylation at Ser-56 favors interaction with CALM1.
CC {ECO:0000250}.
CC -!- PTM: Isoform 1 is methylated by CARM1 at Arg-655 in immature
CC thymocytes. {ECO:0000305|PubMed:15096520}.
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DR EMBL; AF112220; AAF17207.1; -; mRNA.
DR EMBL; AK294484; BAG57707.1; -; mRNA.
DR EMBL; CH471055; EAW64471.1; -; Genomic_DNA.
DR EMBL; BC017805; AAH17805.1; -; mRNA.
DR EMBL; BC031106; AAH31106.1; -; mRNA.
DR EMBL; BC036399; AAH36399.1; -; mRNA.
DR EMBL; BC041385; AAH41385.1; -; mRNA.
DR EMBL; BC051828; AAH51828.1; -; mRNA.
DR EMBL; BC066651; AAH66651.1; -; mRNA.
DR EMBL; AL133109; CAB61414.1; -; mRNA.
DR CCDS; CCDS2661.1; -. [Q9UBL0-1]
DR CCDS; CCDS43063.1; -. [Q9UBL0-2]
DR CCDS; CCDS58823.1; -. [Q9UBL0-3]
DR CCDS; CCDS58824.1; -. [Q9UBL0-4]
DR PIR; T42644; T42644.
DR RefSeq; NP_001020239.1; NM_001025068.1. [Q9UBL0-2]
DR RefSeq; NP_001020240.1; NM_001025069.1. [Q9UBL0-2]
DR RefSeq; NP_001254545.1; NM_001267616.1. [Q9UBL0-2]
DR RefSeq; NP_001254546.1; NM_001267617.1. [Q9UBL0-4]
DR RefSeq; NP_001254547.1; NM_001267618.1. [Q9UBL0-2]
DR RefSeq; NP_001254548.1; NM_001267619.1. [Q9UBL0-3]
DR RefSeq; NP_057384.2; NM_016300.4. [Q9UBL0-1]
DR RefSeq; NP_938409.1; NM_198399.1. [Q9UBL0-2]
DR RefSeq; XP_006713006.1; XM_006712943.2. [Q9UBL0-3]
DR RefSeq; XP_006713007.1; XM_006712944.2. [Q9UBL0-4]
DR RefSeq; XP_016861081.1; XM_017005592.1. [Q9UBL0-3]
DR RefSeq; XP_016861082.1; XM_017005593.1. [Q9UBL0-3]
DR RefSeq; XP_016861083.1; XM_017005594.1. [Q9UBL0-3]
DR RefSeq; XP_016861084.1; XM_017005595.1. [Q9UBL0-3]
DR RefSeq; XP_016861091.1; XM_017005602.1. [Q9UBL0-4]
DR RefSeq; XP_016861092.1; XM_017005603.1. [Q9UBL0-4]
DR RefSeq; XP_016861093.1; XM_017005604.1. [Q9UBL0-4]
DR RefSeq; XP_016861094.1; XM_017005605.1. [Q9UBL0-4]
DR RefSeq; XP_016861095.1; XM_017005606.1. [Q9UBL0-4]
DR AlphaFoldDB; Q9UBL0; -.
DR SMR; Q9UBL0; -.
DR BioGRID; 115995; 3.
DR IntAct; Q9UBL0; 3.
DR STRING; 9606.ENSP00000412326; -.
DR GlyGen; Q9UBL0; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UBL0; -.
DR PhosphoSitePlus; Q9UBL0; -.
DR BioMuta; ARPP21; -.
DR DMDM; 160332340; -.
DR jPOST; Q9UBL0; -.
DR MassIVE; Q9UBL0; -.
DR MaxQB; Q9UBL0; -.
DR PaxDb; Q9UBL0; -.
DR PeptideAtlas; Q9UBL0; -.
DR PRIDE; Q9UBL0; -.
DR ProteomicsDB; 83988; -. [Q9UBL0-1]
DR ProteomicsDB; 83989; -. [Q9UBL0-2]
DR ProteomicsDB; 83990; -. [Q9UBL0-3]
DR ProteomicsDB; 83991; -. [Q9UBL0-4]
DR ProteomicsDB; 83992; -. [Q9UBL0-5]
DR ProteomicsDB; 83993; -. [Q9UBL0-6]
DR Antibodypedia; 2806; 162 antibodies from 27 providers.
DR DNASU; 10777; -.
DR Ensembl; ENST00000187397.8; ENSP00000187397.4; ENSG00000172995.17. [Q9UBL0-1]
DR Ensembl; ENST00000396481.6; ENSP00000379741.2; ENSG00000172995.17. [Q9UBL0-2]
DR Ensembl; ENST00000396482.6; ENSP00000379742.2; ENSG00000172995.17. [Q9UBL0-2]
DR Ensembl; ENST00000412048.5; ENSP00000390151.1; ENSG00000172995.17. [Q9UBL0-2]
DR Ensembl; ENST00000417925.5; ENSP00000412326.1; ENSG00000172995.17. [Q9UBL0-3]
DR Ensembl; ENST00000427542.5; ENSP00000401602.1; ENSG00000172995.17. [Q9UBL0-2]
DR Ensembl; ENST00000428373.5; ENSP00000412411.1; ENSG00000172995.17. [Q9UBL0-2]
DR Ensembl; ENST00000432682.5; ENSP00000389754.1; ENSG00000172995.17. [Q9UBL0-2]
DR Ensembl; ENST00000436702.5; ENSP00000397720.1; ENSG00000172995.17. [Q9UBL0-2]
DR Ensembl; ENST00000438071.1; ENSP00000410171.1; ENSG00000172995.17. [Q9UBL0-2]
DR Ensembl; ENST00000441454.5; ENSP00000406964.1; ENSG00000172995.17. [Q9UBL0-2]
DR Ensembl; ENST00000444190.5; ENSP00000405276.1; ENSG00000172995.17. [Q9UBL0-4]
DR Ensembl; ENST00000474696.5; ENSP00000417838.1; ENSG00000172995.17. [Q9UBL0-2]
DR GeneID; 10777; -.
DR KEGG; hsa:10777; -.
DR UCSC; uc003cfz.5; human. [Q9UBL0-1]
DR CTD; 10777; -.
DR DisGeNET; 10777; -.
DR GeneCards; ARPP21; -.
DR HGNC; HGNC:16968; ARPP21.
DR HPA; ENSG00000172995; Tissue enhanced (brain, lymphoid tissue, skeletal muscle).
DR MIM; 605488; gene.
DR neXtProt; NX_Q9UBL0; -.
DR OpenTargets; ENSG00000172995; -.
DR VEuPathDB; HostDB:ENSG00000172995; -.
DR eggNOG; KOG2953; Eukaryota.
DR GeneTree; ENSGT00940000160796; -.
DR HOGENOM; CLU_2256194_0_0_1; -.
DR InParanoid; Q9UBL0; -.
DR OMA; SCRTNCT; -.
DR OrthoDB; 137913at2759; -.
DR PhylomeDB; Q9UBL0; -.
DR TreeFam; TF315915; -.
DR PathwayCommons; Q9UBL0; -.
DR SignaLink; Q9UBL0; -.
DR SIGNOR; Q9UBL0; -.
DR BioGRID-ORCS; 10777; 8 hits in 1059 CRISPR screens.
DR ChiTaRS; ARPP21; human.
DR GeneWiki; ARPP-21; -.
DR GenomeRNAi; 10777; -.
DR Pharos; Q9UBL0; Tbio.
DR PRO; PR:Q9UBL0; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9UBL0; protein.
DR Bgee; ENSG00000172995; Expressed in lateral globus pallidus and 133 other tissues.
DR ExpressionAtlas; Q9UBL0; baseline and differential.
DR Genevisible; Q9UBL0; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
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; Methylation; Phosphoprotein; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q7M2N1"
FT CHAIN 2..812
FT /note="cAMP-regulated phosphoprotein 21"
FT /id="PRO_0000064682"
FT DOMAIN 164..227
FT /note="R3H"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00382"
FT DOMAIN 228..300
FT /note="SUZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01009"
FT REGION 1..130
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 485..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..632
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 32..58
FT /evidence="ECO:0000255"
FT COMPBIAS 14..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 30..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..100
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..130
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..350
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 498..522
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 523..537
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 581..614
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..632
FT /note="Pro 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 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 56
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCB4"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCB4"
FT MOD_RES 300
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCB4"
FT MOD_RES 363
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9DCB4"
FT MOD_RES 383
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 562
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 655
FT /note="Asymmetric dimethylarginine"
FT /evidence="ECO:0000305|PubMed:15096520"
FT VAR_SEQ 1..512
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029469"
FT VAR_SEQ 88..108
FT /note="ESIHLQLSSFSSLQEEDKSRK -> VYPLAIIINCMNGIHLCVHDS (in
FT isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029470"
FT VAR_SEQ 88..89
FT /note="ES -> TL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10931946,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8120638"
FT /id="VSP_029471"
FT VAR_SEQ 90..812
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10931946,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:8120638"
FT /id="VSP_029472"
FT VAR_SEQ 109..812
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029473"
FT VAR_SEQ 266..299
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_029474"
FT VAR_SEQ 312..331
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_029475"
FT VAR_SEQ 548
FT /note="Q -> QSVQGLQASSQSVQYPAVSFPPQHLLPVSPTQHFPM (in
FT isoform 3, isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005"
FT /id="VSP_029476"
FT CONFLICT 312
FT /note="Missing (in Ref. 6; CAB61414)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 812 AA; 89196 MW; 73981A8341BB3359 CRC64;
MSEQGDLNQA IAEEGGTEQE TATPENGIVK SESLDEEEKL ELQRRLEAQN QERRKSKSGA
GKGKLTRSLA VCEESSARPG GESLQDQESI HLQLSSFSSL QEEDKSRKDD SEREKEKDKN
KDKTSEKPKI RMLSKDCSQE YTDSTGIDLH EFLINTLKNN SRDRMILLKM EQEIIDFIAD
NNNHYKKFPQ MSSYQRMLVH RVAAYFGLDH NVDQTGKSVI INKTSSTRIP EQRFCEHLKD
EKGEESQKRF ILKRDNSSID KEDNQQNRMH PFRDDRRSKS IEEREEEYQR VRERIFAHDS
VCSQESLFVE NSRLLEDSNI CNETYKKRQL FRGNRDGSGR TSGSRQSSSE NELKWSDHQR
AWSSTDSDSS NRNLKPAMTK TASFGGITVL TRGDSTSSTR STGKLSKAGS ESSSSAGSSG
SLSRTHPPLQ STPLVSGVAA GSPGCVPYPE NGIGGQVAPS STSYILLPLE AATGIPPGSI
LLNPHTGQPF VNPDGTPAIY NPPTSQQPLR SAMVGQSQQQ PPQQQPSPQP QQQVQPPQPQ
MAGPLVTQRD DVATQFGQMT LSRQSSGETP EPPSGPVYPS SLMPQPAQQP SYVIASTGQQ
LPTGGFSGSG PPISQQVLQP PPSPQGFVQQ PPPAQMPVYY YPSGQYPTST TQQYRPMAPV
QYNAQRSQQM PQAAQQAGYQ PVLSGQQGFQ GLIGVQQPPQ SQNVINNQQG TPVQSVMVSY
PTMSSYQVPM TQGSQGLPQQ SYQQPIMLPN QAGQGSLPAT GMPVYCNVTP PTPQNNLRLI
GPHCPSSTVP VMSASCRTNC ASMSNAGWQV KF
