RARG_MOUSE
ID RARG_MOUSE Reviewed; 458 AA.
AC P18911; P20787; Q3UG86; Q62149; Q91VK5; Q91YX2;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 3.
DT 03-AUG-2022, entry version 210.
DE RecName: Full=Retinoic acid receptor gamma;
DE Short=RAR-gamma;
DE AltName: Full=Nuclear receptor subfamily 1 group B member 3;
GN Name=Rarg; Synonyms=Nr1b3;
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), AND TISSUE SPECIFICITY.
RX PubMed=2544807; DOI=10.1038/339714a0;
RA Zelent A., Krust A., Petkovich M., Kastner P., Chambon P.;
RT "Cloning of murine alpha and beta retinoic acid receptors and a novel
RT receptor gamma predominantly expressed in skin.";
RL Nature 339:714-717(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
RX PubMed=2157970; DOI=10.1128/mcb.10.5.2335-2340.1990;
RA Giguere V., Shago M., Zirngibl R., Tate P., Rossant J., Varmuza S.;
RT "Identification of a novel isoform of the retinoic acid receptor gamma
RT expressed in the mouse embryo.";
RL Mol. Cell. Biol. 10:2335-2340(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Czech II; TISSUE=Mammary tumor;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-74 (ISOFORMS 1; 2 AND 3).
RX PubMed=2157210; DOI=10.1073/pnas.87.7.2700;
RA Kastner P., Krust A., Mendelsohn C., Garnier J.-M., Zelent A., Leroy P.,
RA Staub A., Chambon P.;
RT "Murine isoforms of retinoic acid receptor gamma with specific patterns of
RT expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 87:2700-2704(1990).
RN [6]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=8388780; DOI=10.1016/0092-8674(93)90246-m;
RA Lohnes D., Kastner P., Dierich A., Mark M., LeMeur M., Chambon P.;
RT "Function of retinoic acid receptor gamma in the mouse.";
RL Cell 73:643-658(1993).
RN [7]
RP IDENTIFICATION IN A COMPLEX WITH PUS1 AND SRA1, AND SUBCELLULAR LOCATION.
RX PubMed=15327771; DOI=10.1016/j.molcel.2004.06.044;
RA Zhao X., Patton J.R., Davis S.L., Florence B., Ames S.J., Spanjaard R.A.;
RT "Regulation of nuclear receptor activity by a pseudouridine synthase
RT through posttranscriptional modification of steroid receptor RNA
RT activator.";
RL Mol. Cell 15:549-558(2004).
RN [8]
RP DISRUPTION PHENOTYPE, AND FUNCTION.
RX PubMed=19389355; DOI=10.1016/j.ydbio.2009.01.031;
RA Williams J.A., Kondo N., Okabe T., Takeshita N., Pilchak D.M., Koyama E.,
RA Ochiai T., Jensen D., Chu M.L., Kane M.A., Napoli J.L., Enomoto-Iwamoto M.,
RA Ghyselinck N., Chambon P., Pacifici M., Iwamoto M.;
RT "Retinoic acid receptors are required for skeletal growth, matrix
RT homeostasis and growth plate function in postnatal mouse.";
RL Dev. Biol. 328:315-327(2009).
RN [9]
RP DISRUPTION PHENOTYPE, POSSIBLE FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=20043900; DOI=10.1016/j.ydbio.2009.12.024;
RA Pennimpede T., Cameron D.A., MacLean G.A., Petkovich M.;
RT "Analysis of Cyp26b1/Rarg compound-null mice reveals two genetically
RT separable effects of retinoic acid on limb outgrowth.";
RL Dev. Biol. 339:179-186(2010).
RN [10]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-34, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Receptor for retinoic acid. Retinoic acid receptors bind as
CC heterodimers to their target response elements in response to their
CC ligands, all-trans or 9-cis retinoic acid, and regulate gene expression
CC in various biological processes. The RAR/RXR heterodimers bind to the
CC retinoic acid response elements (RARE) composed of tandem 5'-AGGTCA-3'
CC sites known as DR1-DR5. In the absence of ligand, acts mainly as an
CC activator of gene expression due to weak binding to corepressors (By
CC similarity). Required for limb bud development. In concert with RARA or
CC RARB, required for skeletal growth, matrix homeostasis and growth plate
CC function. {ECO:0000250, ECO:0000269|PubMed:19389355,
CC ECO:0000269|PubMed:8388780}.
CC -!- SUBUNIT: Homodimer (By similarity). Heterodimer with a RXR molecule (By
CC similarity). Binds DNA preferentially as a RAR/RXR heterodimer (By
CC similarity). Forms a complex with PUS1 and the SRA1 RNA in the nucleus.
CC {ECO:0000250, ECO:0000269|PubMed:15327771}.
CC -!- INTERACTION:
CC P18911; Q91XC0: Ajuba; NbExp=2; IntAct=EBI-8053650, EBI-1565930;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-ProRule:PRU00407,
CC ECO:0000269|PubMed:15327771}. Cytoplasm {ECO:0000250|UniProtKB:P13631}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=A;
CC IsoId=P18911-1; Sequence=Displayed;
CC Name=2; Synonyms=B;
CC IsoId=P18911-2, P20787-1;
CC Sequence=VSP_031082;
CC Name=3;
CC IsoId=P18911-3; Sequence=VSP_031081;
CC -!- DEVELOPMENTAL STAGE: In 9.5-12.5 dpc embryos, expression throughout
CC limb bud mesenchyme. This expression overlaps with that of CYP26B1.
CC Also strongly expressed in the caudal and craniofacial regions.
CC {ECO:0000269|PubMed:20043900}.
CC -!- DOMAIN: Composed of three domains: a modulating N-terminal domain, a
CC DNA-binding domain and a C-terminal ligand-binding domain.
CC -!- DISRUPTION PHENOTYPE: Rarg and Rarb double null mice exhibit growth
CC retardation 3 weeks after birth. Defects are found in the growth plates
CC with deficiency in cartilage. Growth retardation was noticable in limb
CC sketal elements such as femurs. Early lethality and male sterility due
CC to squamous metaplasia of the seminal vesicles and prostate are also
CC observed. Isoform 2 mutants appear normal. The Rarg and Cyp26b1 double
CC null mutation is able to partially rescue limb skeletal morphology
CC without restoring normal expression of proximo-distal patterning genes.
CC {ECO:0000269|PubMed:19389355, ECO:0000269|PubMed:20043900,
CC ECO:0000269|PubMed:8388780}.
CC -!- SIMILARITY: Belongs to the nuclear hormone receptor family. NR1
CC subfamily. {ECO:0000305}.
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DR EMBL; X15848; CAA33845.1; -; mRNA.
DR EMBL; M34475; AAA40036.1; -; mRNA.
DR EMBL; M34476; AAA40035.1; -; mRNA.
DR EMBL; AK148064; BAE28323.1; -; mRNA.
DR EMBL; BC012923; AAH12923.1; -; mRNA.
DR EMBL; BC013709; AAH13709.1; -; mRNA.
DR EMBL; M32068; AAA40032.1; -; mRNA.
DR EMBL; M32069; AAA40033.1; -; mRNA.
DR EMBL; M32070; AAA40034.1; -; mRNA.
DR CCDS; CCDS27875.1; -. [P18911-1]
DR CCDS; CCDS37226.1; -. [P18911-2]
DR PIR; B34714; B34714.
DR PIR; S05052; A34714.
DR RefSeq; NP_001036192.1; NM_001042727.2. [P18911-2]
DR RefSeq; NP_035374.3; NM_011244.4. [P18911-1]
DR RefSeq; XP_006520713.1; XM_006520650.1. [P18911-1]
DR RefSeq; XP_011243827.1; XM_011245525.2. [P18911-1]
DR AlphaFoldDB; P18911; -.
DR SMR; P18911; -.
DR BioGRID; 202595; 12.
DR DIP; DIP-42822N; -.
DR IntAct; P18911; 2.
DR MINT; P18911; -.
DR STRING; 10090.ENSMUSP00000048838; -.
DR BindingDB; P18911; -.
DR ChEMBL; CHEMBL4177; -.
DR DrugCentral; P18911; -.
DR GuidetoPHARMACOLOGY; 592; -.
DR iPTMnet; P18911; -.
DR PhosphoSitePlus; P18911; -.
DR EPD; P18911; -.
DR MaxQB; P18911; -.
DR PaxDb; P18911; -.
DR PeptideAtlas; P18911; -.
DR PRIDE; P18911; -.
DR ProteomicsDB; 255100; -. [P18911-1]
DR ProteomicsDB; 255101; -. [P18911-2]
DR ProteomicsDB; 255102; -. [P18911-3]
DR Antibodypedia; 15142; 219 antibodies from 37 providers.
DR DNASU; 19411; -.
DR Ensembl; ENSMUST00000043172; ENSMUSP00000048838; ENSMUSG00000001288. [P18911-1]
DR Ensembl; ENSMUST00000063339; ENSMUSP00000067266; ENSMUSG00000001288. [P18911-2]
DR GeneID; 19411; -.
DR KEGG; mmu:19411; -.
DR UCSC; uc007xvc.2; mouse. [P18911-2]
DR UCSC; uc007xvd.2; mouse. [P18911-1]
DR CTD; 5916; -.
DR MGI; MGI:97858; Rarg.
DR VEuPathDB; HostDB:ENSMUSG00000001288; -.
DR eggNOG; KOG3575; Eukaryota.
DR GeneTree; ENSGT00940000156458; -.
DR HOGENOM; CLU_007368_18_2_1; -.
DR InParanoid; P18911; -.
DR OMA; MQYTCHK; -.
DR OrthoDB; 1165737at2759; -.
DR PhylomeDB; P18911; -.
DR TreeFam; TF328382; -.
DR Reactome; R-MMU-383280; Nuclear Receptor transcription pathway.
DR Reactome; R-MMU-5362517; Signaling by Retinoic Acid.
DR BioGRID-ORCS; 19411; 2 hits in 77 CRISPR screens.
DR ChiTaRS; Rarg; mouse.
DR PRO; PR:P18911; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; P18911; protein.
DR Bgee; ENSMUSG00000001288; Expressed in postcranial axial skeleton and 318 other tissues.
DR ExpressionAtlas; P18911; baseline and differential.
DR Genevisible; P18911; MM.
DR GO; GO:0000785; C:chromatin; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0005667; C:transcription regulator complex; IDA:BHF-UCL.
DR GO; GO:0003682; F:chromatin binding; IDA:MGI.
DR GO; GO:0003677; F:DNA binding; IDA:BHF-UCL.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0004879; F:nuclear receptor activity; ISO:MGI.
DR GO; GO:0046965; F:nuclear retinoid X receptor binding; IMP:BHF-UCL.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IBA:GO_Central.
DR GO; GO:1990837; F:sequence-specific double-stranded DNA binding; ISO:MGI.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0009952; P:anterior/posterior pattern specification; IMP:MGI.
DR GO; GO:0006915; P:apoptotic process; IGI:MGI.
DR GO; GO:0060348; P:bone development; IMP:UniProtKB.
DR GO; GO:0060349; P:bone morphogenesis; IMP:MGI.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0008283; P:cell population proliferation; IGI:MGI.
DR GO; GO:1990830; P:cellular response to leukemia inhibitory factor; IEP:MGI.
DR GO; GO:0071300; P:cellular response to retinoic acid; IEA:Ensembl.
DR GO; GO:0002063; P:chondrocyte development; IMP:UniProtKB.
DR GO; GO:0031076; P:embryonic camera-type eye development; IGI:MGI.
DR GO; GO:0048048; P:embryonic eye morphogenesis; IGI:MGI.
DR GO; GO:0035116; P:embryonic hindlimb morphogenesis; IGI:MGI.
DR GO; GO:0060429; P:epithelium development; IMP:MGI.
DR GO; GO:0060324; P:face development; IGI:MGI.
DR GO; GO:0048732; P:gland development; IMP:MGI.
DR GO; GO:0002068; P:glandular epithelial cell development; IGI:MGI.
DR GO; GO:0003430; P:growth plate cartilage chondrocyte growth; IMP:UniProtKB.
DR GO; GO:0003417; P:growth plate cartilage development; IGI:MGI.
DR GO; GO:0070384; P:Harderian gland development; IMP:MGI.
DR GO; GO:0009755; P:hormone-mediated signaling pathway; IBA:GO_Central.
DR GO; GO:0060173; P:limb development; IMP:UniProtKB.
DR GO; GO:0035264; P:multicellular organism growth; IGI:MGI.
DR GO; GO:0061037; P:negative regulation of cartilage development; IMP:MGI.
DR GO; GO:0045596; P:negative regulation of cell differentiation; IMP:MGI.
DR GO; GO:0032331; P:negative regulation of chondrocyte differentiation; IMP:MGI.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IGI:MGI.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0001843; P:neural tube closure; IGI:MGI.
DR GO; GO:0043065; P:positive regulation of apoptotic process; IGI:MGI.
DR GO; GO:0008284; P:positive regulation of cell population proliferation; ISO:MGI.
DR GO; GO:0010628; P:positive regulation of gene expression; IDA:MGI.
DR GO; GO:0043068; P:positive regulation of programmed cell death; IGI:MGI.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:MGI.
DR GO; GO:0012501; P:programmed cell death; IGI:MGI.
DR GO; GO:0060740; P:prostate gland epithelium morphogenesis; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IGI:MGI.
DR GO; GO:0031641; P:regulation of myelination; ISO:MGI.
DR GO; GO:0045637; P:regulation of myeloid cell differentiation; IGI:MGI.
DR GO; GO:0048608; P:reproductive structure development; IMP:MGI.
DR GO; GO:0032526; P:response to retinoic acid; ISO:MGI.
DR GO; GO:0048384; P:retinoic acid receptor signaling pathway; IMP:MGI.
DR GO; GO:0072089; P:stem cell proliferation; IGI:MGI.
DR GO; GO:0060534; P:trachea cartilage development; IMP:MGI.
DR Gene3D; 1.10.565.10; -; 1.
DR Gene3D; 3.30.50.10; -; 1.
DR InterPro; IPR035500; NHR-like_dom_sf.
DR InterPro; IPR000536; Nucl_hrmn_rcpt_lig-bd.
DR InterPro; IPR001723; Nuclear_hrmn_rcpt.
DR InterPro; IPR003078; Retinoic_acid_rcpt.
DR InterPro; IPR001628; Znf_hrmn_rcpt.
DR InterPro; IPR013088; Znf_NHR/GATA.
DR Pfam; PF00104; Hormone_recep; 1.
DR Pfam; PF00105; zf-C4; 1.
DR PRINTS; PR01292; RETNOICACIDR.
DR PRINTS; PR00398; STRDHORMONER.
DR PRINTS; PR00047; STROIDFINGER.
DR SMART; SM00430; HOLI; 1.
DR SMART; SM00399; ZnF_C4; 1.
DR SUPFAM; SSF48508; SSF48508; 1.
DR PROSITE; PS51843; NR_LBD; 1.
DR PROSITE; PS00031; NUCLEAR_REC_DBD_1; 1.
DR PROSITE; PS51030; NUCLEAR_REC_DBD_2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; DNA-binding; Isopeptide bond;
KW Metal-binding; Methylation; Nucleus; Receptor; Reference proteome;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..458
FT /note="Retinoic acid receptor gamma"
FT /id="PRO_0000053474"
FT DOMAIN 185..419
FT /note="NR LBD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01189"
FT DNA_BIND 90..155
FT /note="Nuclear receptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 90..110
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT ZN_FING 126..150
FT /note="NR C4-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00407"
FT REGION 1..89
FT /note="Modulating"
FT REGION 58..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 156..184
FT /note="Hinge"
FT REGION 161..180
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 60..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 34
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT CROSSLNK 172
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P13631"
FT CROSSLNK 401
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:P13631"
FT VAR_SEQ 1..62
FT /note="MATNKERLFAPGALGPGSGYPGAGFPFAFPGALRGSPPFEMLSPSFRGLGQP
FT DLPKEMASLS -> MHKGDNSGHQQVPRKRGHGMRVLLLSFCLSSHAAFHSA (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:2157210"
FT /id="VSP_031081"
FT VAR_SEQ 1..61
FT /note="MATNKERLFAPGALGPGSGYPGAGFPFAFPGALRGSPPFEMLSPSFRGLGQP
FT DLPKEMASL -> MYDCMESFVPGPRRLYGAAGPGAGLLRRATGSSCFAGLESFAWAQP
FT ASLQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:2157210,
FT ECO:0000303|PubMed:2157970"
FT /id="VSP_031082"
FT CONFLICT 63
FT /note="V -> E (in Ref. 3; BAE28323)"
FT /evidence="ECO:0000305"
FT CONFLICT 78
FT /note="P -> A (in Ref. 3; BAE28323)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="S -> L (in Ref. 4; AAH13709)"
FT /evidence="ECO:0000305"
FT CONFLICT 369..372
FT /note="RPSQ -> DPAK (in Ref. 2; AAA40035/AAA40036)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 458 AA; 50891 MW; 1D13D2F1482D7194 CRC64;
MATNKERLFA PGALGPGSGY PGAGFPFAFP GALRGSPPFE MLSPSFRGLG QPDLPKEMAS
LSVETQSTSS EEMVPSSPSP PPPPRVYKPC FVCNDKSSGY HYGVSSCEGC KGFFRRSIQK
NMVYTCHRDK NCIINKVTRN RCQYCRLQKC FEVGMSKEAV RNDRNKKKKE VKEEGSPDSY
ELSPQLEELI TKVSKAHQET FPSLCQLGKY TTNSSADHRV QLDLGLWDKF SELATKCIIK
IVEFAKRLPG FTGLSIADQI TLLKAACLDI LMLRICTRYT PEQDTMTFSD GLTLNRTQMH
NAGFGPLTDL VFAFAGQLLP LEMDDTETGL LSAICLICGD RMDLEEPEKV DKLQEPLLEA
LRLYARRRRP SQPYMFPRML MKITDLRGIS TKGAERAITL KMEIPGPMPP LIREMLENPE
MFEDDSSKPG PHPKASSEDE APGGQGKRGQ SPQPDQGP
