ABR_MOUSE
ID ABR_MOUSE Reviewed; 859 AA.
AC Q5SSL4; Q3U5G0; Q3UQJ6; Q3UY38; Q5SYJ5; Q5SYJ7; Q5SYJ8; Q5SYJ9; Q6PCY1;
AC Q6PDH3;
DT 25-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 156.
DE RecName: Full=Active breakpoint cluster region-related protein {ECO:0000305};
GN Name=Abr {ECO:0000312|MGI:MGI:107771};
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 [LARGE SCALE MRNA] (ISOFORMS 3 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-407 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Lung, 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 FUNCTION.
RX PubMed=17116687; DOI=10.1128/mcb.00756-06;
RA Cho Y.J., Cunnick J.M., Yi S.J., Kaartinen V., Groffen J., Heisterkamp N.;
RT "Abr and Bcr, two homologous Rac GTPase-activating proteins, control
RT multiple cellular functions of murine macrophages.";
RL Mol. Cell. Biol. 27:899-911(2007).
RN [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-57, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Lung, and Spleen;
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).
RN [7]
RP DISRUPTION PHENOTYPE, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=20962234; DOI=10.1523/jneurosci.1711-10.2010;
RA Oh D., Han S., Seo J., Lee J.R., Choi J., Groffen J., Kim K., Cho Y.S.,
RA Choi H.S., Shin H., Woo J., Won H., Park S.K., Kim S.Y., Jo J.,
RA Whitcomb D.J., Cho K., Kim H., Bae Y.C., Heisterkamp N., Choi S.Y., Kim E.;
RT "Regulation of synaptic Rac1 activity, long-term potentiation maintenance,
RT and learning and memory by BCR and ABR Rac GTPase-activating proteins.";
RL J. Neurosci. 30:14134-14144(2010).
CC -!- FUNCTION: Protein with a unique structure having two opposing
CC regulatory activities toward small GTP-binding proteins. The C-terminus
CC is a GTPase-activating protein domain which stimulates GTP hydrolysis
CC by RAC1, RAC2 and CDC42. Accelerates the intrinsic rate of GTP
CC hydrolysis of RAC1 or CDC42, leading to down-regulation of the active
CC GTP-bound form. The central Dbl homology (DH) domain functions as
CC guanine nucleotide exchange factor (GEF) that modulates the GTPases
CC CDC42, RHOA and RAC1. Promotes the conversion of CDC42, RHOA and RAC1
CC from the GDP-bound to the GTP-bound form (By similarity). Functions as
CC an important negative regulator of neuronal RAC1 activity
CC (PubMed:20962234). Regulates macrophage functions such as CSF-1
CC directed motility and phagocytosis through the modulation of RAC1
CC activity (PubMed:17116687). {ECO:0000250|UniProtKB:Q12979,
CC ECO:0000269|PubMed:17116687, ECO:0000269|PubMed:20962234}.
CC -!- SUBUNIT: Interacts with DLG4. {ECO:0000250|UniProtKB:Q12979}.
CC -!- SUBCELLULAR LOCATION: Cell projection, dendritic spine
CC {ECO:0000269|PubMed:20962234}. Cell projection, axon
CC {ECO:0000269|PubMed:20962234}. Synapse
CC {ECO:0000250|UniProtKB:A0A0G2JTR4}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q5SSL4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5SSL4-2; Sequence=VSP_035905;
CC Name=3;
CC IsoId=Q5SSL4-3; Sequence=VSP_035903, VSP_035906;
CC Name=4;
CC IsoId=Q5SSL4-4; Sequence=VSP_035904;
CC -!- TISSUE SPECIFICITY: In hippocampal subregions, expressed at similarly
CC high levels in the dentate gyrus and CA1 regions, but lower in the CA3
CC region. {ECO:0000269|PubMed:20962234}.
CC -!- DOMAIN: The central Dbl homology (DH) domain functions as guanine
CC nucleotide exchange factor (GEF) that modulates the GTPases CDC42, RHOA
CC and RAC1. Promotes the conversion of CDC42, RHOA and RAC1 from the GDP-
CC bound to the GTP-bound form. The C-terminus is a Rho-GAP domain which
CC stimulates GTP hydrolysis by RAC1, RAC2 and CDC42. The protein has a
CC unique structure having two opposing regulatory activities toward small
CC GTP-binding proteins. {ECO:0000250|UniProtKB:Q12979}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice show impaired spatial and object
CC recognition memory with reduced maintenance of long-term potentiation
CC (LTP) in Schaffer collateral-CA1 pyramidal neuron synapses.
CC {ECO:0000269|PubMed:20962234}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAI24542.3; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=CAQ11499.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AK134993; BAE22375.1; -; mRNA.
DR EMBL; AK142364; BAE25044.1; -; mRNA.
DR EMBL; AK153615; BAE32119.1; -; mRNA.
DR EMBL; AL591143; CAI24541.2; -; Genomic_DNA.
DR EMBL; AL663050; CAI24541.2; JOINED; Genomic_DNA.
DR EMBL; AL591143; CAI24542.3; ALT_SEQ; Genomic_DNA.
DR EMBL; AL663050; CAI24542.3; JOINED; Genomic_DNA.
DR EMBL; AL591143; CAI24543.2; -; Genomic_DNA.
DR EMBL; AL663050; CAI24543.2; JOINED; Genomic_DNA.
DR EMBL; AL591143; CAI24545.1; -; Genomic_DNA.
DR EMBL; AL663050; CAI24545.1; JOINED; Genomic_DNA.
DR EMBL; AL591143; CAI24547.2; -; Genomic_DNA.
DR EMBL; AL663050; CAI25860.1; -; Genomic_DNA.
DR EMBL; AL591143; CAI25860.1; JOINED; Genomic_DNA.
DR EMBL; AL663050; CAQ11498.1; -; Genomic_DNA.
DR EMBL; AL591143; CAQ11498.1; JOINED; Genomic_DNA.
DR EMBL; AL663050; CAQ11499.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AL591143; CAQ11499.1; JOINED; Genomic_DNA.
DR EMBL; AL663050; CAQ11500.1; -; Genomic_DNA.
DR EMBL; AL591143; CAQ11500.1; JOINED; Genomic_DNA.
DR EMBL; BC056385; AAH56385.1; -; mRNA.
DR EMBL; BC058708; AAH58708.1; -; mRNA.
DR EMBL; BC059064; AAH59064.1; -; mRNA.
DR CCDS; CCDS25066.1; -. [Q5SSL4-1]
DR CCDS; CCDS36231.1; -. [Q5SSL4-2]
DR CCDS; CCDS70246.1; -. [Q5SSL4-3]
DR CCDS; CCDS83843.1; -. [Q5SSL4-4]
DR RefSeq; NP_001278115.1; NM_001291186.1. [Q5SSL4-3]
DR RefSeq; NP_001333599.1; NM_001346670.1. [Q5SSL4-4]
DR RefSeq; NP_932135.1; NM_198018.2. [Q5SSL4-2]
DR RefSeq; NP_942597.1; NM_198894.2.
DR RefSeq; NP_942598.1; NM_198895.2. [Q5SSL4-1]
DR AlphaFoldDB; Q5SSL4; -.
DR SMR; Q5SSL4; -.
DR BioGRID; 225161; 21.
DR IntAct; Q5SSL4; 13.
DR STRING; 10090.ENSMUSP00000091551; -.
DR iPTMnet; Q5SSL4; -.
DR PhosphoSitePlus; Q5SSL4; -.
DR SwissPalm; Q5SSL4; -.
DR EPD; Q5SSL4; -.
DR jPOST; Q5SSL4; -.
DR MaxQB; Q5SSL4; -.
DR PaxDb; Q5SSL4; -.
DR PeptideAtlas; Q5SSL4; -.
DR PRIDE; Q5SSL4; -.
DR ProteomicsDB; 286021; -. [Q5SSL4-1]
DR ProteomicsDB; 286022; -. [Q5SSL4-2]
DR ProteomicsDB; 286023; -. [Q5SSL4-3]
DR ProteomicsDB; 286024; -. [Q5SSL4-4]
DR Antibodypedia; 22668; 74 antibodies from 18 providers.
DR DNASU; 109934; -.
DR Ensembl; ENSMUST00000065028; ENSMUSP00000068982; ENSMUSG00000017631. [Q5SSL4-3]
DR Ensembl; ENSMUST00000072740; ENSMUSP00000072522; ENSMUSG00000017631. [Q5SSL4-1]
DR Ensembl; ENSMUST00000094012; ENSMUSP00000091551; ENSMUSG00000017631. [Q5SSL4-2]
DR Ensembl; ENSMUST00000108408; ENSMUSP00000104045; ENSMUSG00000017631. [Q5SSL4-4]
DR GeneID; 109934; -.
DR KEGG; mmu:109934; -.
DR UCSC; uc007kfr.2; mouse. [Q5SSL4-3]
DR UCSC; uc007kfs.2; mouse. [Q5SSL4-2]
DR UCSC; uc007kft.2; mouse. [Q5SSL4-1]
DR UCSC; uc007kfv.1; mouse. [Q5SSL4-4]
DR CTD; 29; -.
DR MGI; MGI:107771; Abr.
DR VEuPathDB; HostDB:ENSMUSG00000017631; -.
DR eggNOG; KOG4269; Eukaryota.
DR GeneTree; ENSGT00940000153491; -.
DR InParanoid; Q5SSL4; -.
DR OrthoDB; 762492at2759; -.
DR PhylomeDB; Q5SSL4; -.
DR TreeFam; TF105082; -.
DR Reactome; R-MMU-193648; NRAGE signals death through JNK.
DR Reactome; R-MMU-416482; G alpha (12/13) signalling events.
DR Reactome; R-MMU-8980692; RHOA GTPase cycle.
DR Reactome; R-MMU-9013026; RHOB GTPase cycle.
DR Reactome; R-MMU-9013106; RHOC GTPase cycle.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013149; RAC1 GTPase cycle.
DR Reactome; R-MMU-9013404; RAC2 GTPase cycle.
DR Reactome; R-MMU-9013423; RAC3 GTPase cycle.
DR BioGRID-ORCS; 109934; 7 hits in 75 CRISPR screens.
DR ChiTaRS; Abr; mouse.
DR PRO; PR:Q5SSL4; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q5SSL4; protein.
DR Bgee; ENSMUSG00000017631; Expressed in dentate gyrus of hippocampal formation granule cell and 246 other tissues.
DR ExpressionAtlas; Q5SSL4; baseline and differential.
DR Genevisible; Q5SSL4; MM.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:MGI.
DR GO; GO:0043197; C:dendritic spine; IEA:UniProtKB-SubCell.
DR GO; GO:0098978; C:glutamatergic synapse; IMP:SynGO.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0099092; C:postsynaptic density, intracellular component; ISO:MGI.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IMP:SynGO.
DR GO; GO:0005096; F:GTPase activator activity; IDA:MGI.
DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; ISS:UniProtKB.
DR GO; GO:0030036; P:actin cytoskeleton organization; IGI:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0007420; P:brain development; IGI:MGI.
DR GO; GO:0016477; P:cell migration; IGI:MGI.
DR GO; GO:0051649; P:establishment of localization in cell; IGI:MGI.
DR GO; GO:0042472; P:inner ear morphogenesis; IGI:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:1905517; P:macrophage migration; IGI:MGI.
DR GO; GO:0050804; P:modulation of chemical synaptic transmission; IMP:SynGO.
DR GO; GO:0060313; P:negative regulation of blood vessel remodeling; IMP:CACAO.
DR GO; GO:0002692; P:negative regulation of cellular extravasation; IMP:CACAO.
DR GO; GO:0050728; P:negative regulation of inflammatory response; IMP:MGI.
DR GO; GO:1905522; P:negative regulation of macrophage migration; IGI:MGI.
DR GO; GO:0043314; P:negative regulation of neutrophil degranulation; IGI:MGI.
DR GO; GO:0050885; P:neuromuscular process controlling balance; IGI:MGI.
DR GO; GO:0043312; P:neutrophil degranulation; IGI:MGI.
DR GO; GO:0006909; P:phagocytosis; IGI:MGI.
DR GO; GO:0050766; P:positive regulation of phagocytosis; IGI:MGI.
DR GO; GO:0043114; P:regulation of vascular permeability; IMP:CACAO.
DR GO; GO:0032496; P:response to lipopolysaccharide; IMP:MGI.
DR CDD; cd13366; PH_ABR; 1.
DR CDD; cd00160; RhoGEF; 1.
DR Gene3D; 1.10.555.10; -; 1.
DR Gene3D; 1.20.900.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.60.40.150; -; 1.
DR InterPro; IPR037769; Abr/Bcr.
DR InterPro; IPR037865; ABR_PH.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR035899; DBL_dom_sf.
DR InterPro; IPR000219; DH-domain.
DR InterPro; IPR001331; GDS_CDC24_CS.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR000198; RhoGAP_dom.
DR PANTHER; PTHR23182; PTHR23182; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF00169; PH; 1.
DR Pfam; PF00620; RhoGAP; 1.
DR Pfam; PF00621; RhoGEF; 1.
DR SMART; SM00239; C2; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00324; RhoGAP; 1.
DR SMART; SM00325; RhoGEF; 1.
DR SUPFAM; SSF48065; SSF48065; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR PROSITE; PS50004; C2; 1.
DR PROSITE; PS00741; DH_1; 1.
DR PROSITE; PS50010; DH_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS50238; RHOGAP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; GTPase activation;
KW Guanine-nucleotide releasing factor; Phosphoprotein; Reference proteome;
KW Synapse.
FT CHAIN 1..859
FT /note="Active breakpoint cluster region-related protein"
FT /id="PRO_0000355539"
FT DOMAIN 91..284
FT /note="DH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00062"
FT DOMAIN 301..459
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT DOMAIN 484..613
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 647..845
FT /note="Rho-GAP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00172"
FT REGION 29..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 50..71
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT VAR_SEQ 1..218
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_035903"
FT VAR_SEQ 1..82
FT /note="MEPLSHRGLPRLSWIDTLYSNFSYGAEDYDAEGHEEQKGPPEGSETMPYIDE
FT SPTMSPQLSARSQGGGDSVSPTPPEGLAPG -> MEEEEEAIGFLDKVLEDEDVFLLEE
FT CELGTPTSPGSGSPFLVAVK (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_035904"
FT VAR_SEQ 1..21
FT /note="MEPLSHRGLPRLSWIDTLYSN -> MAAGGRRRRPLRYQSLAALVEDSQWPF
FT LFLVSD (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_035905"
FT VAR_SEQ 219..233
FT /note="GPKDSKDSHTSVTME -> MEILLIIRFCCNCTY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_035906"
FT CONFLICT 164
FT /note="W -> R (in Ref. 1; BAE32119)"
FT /evidence="ECO:0000305"
FT CONFLICT 630
FT /note="D -> E (in Ref. 1; BAE22375)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 859 AA; 97667 MW; 79ED2F432899A1F9 CRC64;
MEPLSHRGLP RLSWIDTLYS NFSYGAEDYD AEGHEEQKGP PEGSETMPYI DESPTMSPQL
SARSQGGGDS VSPTPPEGLA PGVEAGKGLE MRKLVLSGFL ASEEIYINQL EALLLPMKPL
KATATTSQPV LTIQQIETIF YKIQDIYEIH KEFYDNLCPK VQQWDSQVTM GHLFQKLASQ
LGVYKAFVDN YKVALETAEK CSQSNNQFQK ISEELKVKGP KDSKDSHTSV TMEALLYKPI
DRVTRSTLVL HDLLKHTPVD HPDYPLLQDA LRISQNFLSS INEDIDPRRT AVTTPKGETR
QLVKDGFLVE MSESSRKLRH VFLFTDVLLC AKLKKTSAGK HQQYDCKWYI PLADLVFPSP
EESEASPQVH PFPDHELEDM KTKISALKSE IQKEKANKGQ SRAIERLKKK MFENEFLLLL
NSPTIPFRIH NRNGKSYLFL LSSDYERSEW REAIQKLQKK DLQAFVLSSV ELQVLTGSCF
KLRTVHNIPV TSNKDDDESP GLYGFLHVIV HSAKGFKQSA NLYCTLEVDS FGYFVSKAKT
RVFRDTTEPK WDEEFEIELE GSQSLRILCY EKCYDKTKVN KDNNEIVDKI MGKGQIQLDP
QTVESKNWHT DVIEMNGIKV EFSMKFTSRD MSLKRTPSKK QTGVFGVKIS VVTKRERSKV
PYIVRQCIEE VEKRGIEEVG IYRISGVATD IQALKAVFDA NNKDILLMLS DMDINAIAGT
LKLYFRELPE PLLTDRLYPA FMEGIALSDP AAKENCMMHL LRSLPDPNLI TFLFLLEHLK
RVAEKEPINK MSLHNLATVF GPTLLRPSEV ESKAHLTSAA DIWSHDVMAQ VQVLLYYLQH
PPISFAELKR NTLYFSTDV
