RGS_DROME
ID RGS_DROME Reviewed; 1541 AA.
AC Q9VCX1; Q9NGQ0; Q9UB06; Q9XYX8;
DT 31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Regulator of G-protein signaling loco;
DE Short=RGS;
DE AltName: Full=Locomotion defects protein;
DE Short=Loco;
GN Name=loco; ORFNames=CG5248;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 3), FUNCTION, INTERACTION WITH
RP GALPHAI, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=10079238; DOI=10.1242/dev.126.8.1781;
RA Granderath S., Stollewerk A., Greig S., Goodman C.S., O'Kane C.J.,
RA Klambt C.;
RT "loco encodes an RGS protein required for Drosophila glial
RT differentiation.";
RL Development 126:1781-1791(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4), FUNCTION, AND DEVELOPMENTAL STAGE.
RC TISSUE=Ovary;
RX PubMed=11731228; DOI=10.1016/s0925-4773(01)00557-3;
RA Pathirana S., Zhao D., Bownes M.;
RT "The Drosophila RGS protein Loco is required for dorsal/ventral axis
RT formation of the egg and embryo, and nurse cell dumping.";
RL Mech. Dev. 109:137-150(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=Berkeley; TISSUE=Embryo;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16213218; DOI=10.1016/j.cell.2005.08.037;
RA Schwabe T., Bainton R.J., Fetter R.D., Heberlein U., Gaul U.;
RT "GPCR signaling is required for blood-brain barrier formation in
RT Drosophila.";
RL Cell 123:133-144(2005).
RN [7]
RP FUNCTION, INTERACTION WITH GALPHAI, AND SUBCELLULAR LOCATION.
RX PubMed=15937221; DOI=10.1101/gad.1295505;
RA Yu F., Wang H., Qian H., Kaushik R., Bownes M., Yang X., Chia W.;
RT "Locomotion defects, together with Pins, regulates heterotrimeric G-protein
RT signaling during Drosophila neuroblast asymmetric divisions.";
RL Genes Dev. 19:1341-1353(2005).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=21255223; DOI=10.1111/j.1474-9726.2011.00678.x;
RA Lin Y.R., Kim K., Yang Y., Ivessa A., Sadoshima J., Park Y.;
RT "Regulation of longevity by regulator of G-protein signaling (RGS) protein,
RT Loco.";
RL Aging Cell 10:438-447(2011).
CC -!- FUNCTION: Acts as a regulator of G protein signaling (RGS). Modulates G
CC protein alpha subunits nucleotide exchange and hydrolysis activities by
CC functioning either as a GTPase-activating protein (GAP), thereby
CC driving G protein alpha subunits into their inactive GDP-bound form, or
CC as a GDP-dissociation inhibitor (GDI). Confers GDI and GAP activities
CC on G(i) alpha subunit Galphai. Confers GAP activity on G(o)-alpha
CC subunit Galphao and G(i) alpha subunit Galphai. Involved in the dorsal-
CC ventral axis formation of the egg. Acts as a G-protein signaling for
CC glial cell differentiation during embryogenesis; Galphai, Galphao and
CC the G-protein coupled receptor, moody, are required in the surface glia
CC to achieve effective insulation of the nerve cord. May be essential for
CC nurse cell dumping during oogenesis. Required in neuroblast
CC asymmetrical cell division. Plays a role in stress resistance and life
CC span control. {ECO:0000269|PubMed:10079238,
CC ECO:0000269|PubMed:11731228, ECO:0000269|PubMed:15937221,
CC ECO:0000269|PubMed:16213218, ECO:0000269|PubMed:21255223}.
CC -!- SUBUNIT: Interacts (via GoLoco and RGS domains) with Galphai (via
CC GDP- or GTP-bound forms). {ECO:0000269|PubMed:10079238,
CC ECO:0000269|PubMed:15937221}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Cell membrane. Apical cell membrane.
CC Note=Recruited from the cytosol to the plasma membrane by the G(i)
CC alpha subunit. Colocalizes with moody at the plasma membrane. Localizes
CC as a crescent to the apical cortex in interphase and forms an apical
CC crescent and segregates into the apical daughter cell at telophase.
CC Colocalizes with Galphai and raps/pins at the apical cortex throughout
CC mitosis.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9VCX1-1; Sequence=Displayed;
CC Name=2; Synonyms=LOCO C1;
CC IsoId=Q9VCX1-2; Sequence=VSP_041115, VSP_041118;
CC Name=3; Synonyms=LOCO C2;
CC IsoId=Q9VCX1-3; Sequence=VSP_041116, VSP_041117;
CC Name=4; Synonyms=LOCO C3;
CC IsoId=Q9VCX1-4; Sequence=VSP_041114;
CC -!- TISSUE SPECIFICITY: Expressed in surface and longitudinal glial cells,
CC gut and heart (at protein level). {ECO:0000269|PubMed:16213218}.
CC -!- DEVELOPMENTAL STAGE: Expressed both maternally and zygotically.
CC Expressed during oogenesis and embryogenesis. Isoform 3 and isoform 4
CC are expressed in the germarium at stage 2. Isoform 4 is expressed in
CC the nurse cells at stage 6 until the nurse cells degenerate. Isoform 3
CC is expressed in the follicle cells at stage 8, in the anterior-dorsal
CC follicles cells from stage 10 until the follicles degenerate. Isoform 2
CC and isoform 3 are expressed in late stage 12 embryos, onwards. Isoform
CC 2 is expressed in tracheal cells and in lateral glial cells within the
CC CNS in late stage 16 embryos. {ECO:0000269|PubMed:10079238,
CC ECO:0000269|PubMed:11731228}.
CC -!- DISRUPTION PHENOTYPE: Homozygous mutant flies show dorsal-ventral
CC defects in egg (shorter egg length and fused appendages) and embryo
CC patterning. Fail to hatch and show severe glial cell differentiation
CC defects: disruption of intimate glial-glial cell contact and absence of
CC glial cell processes enwrapping neuronal cell bodies and axones,
CC resulting in loss of the blood-brain barrier (BBB) formation.
CC Heterozygous flies show an enhanced stress resistance, fat content and
CC extended lifespan. {ECO:0000269|PubMed:10079238,
CC ECO:0000269|PubMed:21255223}.
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DR EMBL; AF130744; AAD24580.1; -; mRNA.
DR EMBL; AF130745; AAD24581.1; -; mRNA.
DR EMBL; AF245455; AAF62552.1; -; mRNA.
DR EMBL; AE014297; AAF56034.2; -; Genomic_DNA.
DR EMBL; AY118939; AAM50799.1; -; mRNA.
DR RefSeq; NP_732773.1; NM_170030.2. [Q9VCX1-1]
DR AlphaFoldDB; Q9VCX1; -.
DR SMR; Q9VCX1; -.
DR BioGRID; 67624; 15.
DR IntAct; Q9VCX1; 1.
DR STRING; 7227.FBpp0083666; -.
DR PaxDb; Q9VCX1; -.
DR PRIDE; Q9VCX1; -.
DR DNASU; 42672; -.
DR EnsemblMetazoa; FBtr0084273; FBpp0083666; FBgn0020278. [Q9VCX1-1]
DR EnsemblMetazoa; FBtr0084276; FBpp0083669; FBgn0020278. [Q9VCX1-2]
DR GeneID; 42672; -.
DR KEGG; dme:Dmel_CG5248; -.
DR UCSC; CG5248-RD; d. melanogaster. [Q9VCX1-1]
DR FlyBase; FBgn0020278; loco.
DR VEuPathDB; VectorBase:FBgn0020278; -.
DR eggNOG; KOG3528; Eukaryota.
DR eggNOG; KOG3589; Eukaryota.
DR GeneTree; ENSGT00940000161426; -.
DR HOGENOM; CLU_002190_0_0_1; -.
DR InParanoid; Q9VCX1; -.
DR OMA; HKSEWSK; -.
DR PhylomeDB; Q9VCX1; -.
DR Reactome; R-DME-418594; G alpha (i) signalling events.
DR SignaLink; Q9VCX1; -.
DR BioGRID-ORCS; 42672; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 42672; -.
DR PRO; PR:Q9VCX1; -.
DR Proteomes; UP000000803; Chromosome 3R.
DR Bgee; FBgn0020278; Expressed in embryonic/larval hemocyte (Drosophila) and 49 other tissues.
DR ExpressionAtlas; Q9VCX1; baseline and differential.
DR Genevisible; Q9VCX1; DM.
DR GO; GO:0045179; C:apical cortex; IDA:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; IPI:FlyBase.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; IDA:UniProtKB.
DR GO; GO:0005096; F:GTPase activator activity; IDA:UniProtKB.
DR GO; GO:0055059; P:asymmetric neuroblast division; IMP:FlyBase.
DR GO; GO:0032291; P:axon ensheathment in central nervous system; IMP:UniProtKB.
DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0030866; P:cortical actin cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0007303; P:cytoplasmic transport, nurse cell to oocyte; IMP:FlyBase.
DR GO; GO:0050832; P:defense response to fungus; IMP:FlyBase.
DR GO; GO:0008069; P:dorsal/ventral axis specification, ovarian follicular epithelium; IMP:FlyBase.
DR GO; GO:0000578; P:embryonic axis specification; IMP:UniProtKB.
DR GO; GO:0060857; P:establishment of glial blood-brain barrier; IMP:UniProtKB.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IMP:UniProtKB.
DR GO; GO:0010001; P:glial cell differentiation; IMP:FlyBase.
DR GO; GO:0003015; P:heart process; IMP:FlyBase.
DR GO; GO:0007310; P:oocyte dorsal/ventral axis specification; IMP:UniProtKB.
DR GO; GO:0009786; P:regulation of asymmetric cell division; IDA:UniProtKB.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; IGI:FlyBase.
DR GO; GO:0009408; P:response to heat; IMP:UniProtKB.
DR GO; GO:0006979; P:response to oxidative stress; IMP:UniProtKB.
DR GO; GO:0042594; P:response to starvation; IMP:UniProtKB.
DR GO; GO:0019991; P:septate junction assembly; IMP:FlyBase.
DR GO; GO:0007419; P:ventral cord development; IMP:FlyBase.
DR Gene3D; 1.10.167.10; -; 1.
DR Gene3D; 1.10.196.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR003116; RBD_dom.
DR InterPro; IPR016137; RGS.
DR InterPro; IPR036305; RGS_sf.
DR InterPro; IPR024066; RGS_subdom1/3.
DR InterPro; IPR044926; RGS_subdomain_2.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR Pfam; PF00595; PDZ; 1.
DR Pfam; PF02196; RBD; 1.
DR Pfam; PF00615; RGS; 1.
DR PRINTS; PR01301; RGSPROTEIN.
DR SMART; SM00390; GoLoco; 1.
DR SMART; SM00228; PDZ; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00455; RBD; 2.
DR SMART; SM00315; RGS; 1.
DR SUPFAM; SSF48097; SSF48097; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR SUPFAM; SSF54236; SSF54236; 2.
DR PROSITE; PS50877; GOLOCO; 1.
DR PROSITE; PS50106; PDZ; 1.
DR PROSITE; PS01179; PID; 1.
DR PROSITE; PS50898; RBD; 2.
DR PROSITE; PS50132; RGS; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Cell division; Cell membrane; Cytoplasm;
KW Developmental protein; Differentiation; GTPase activation; Membrane;
KW Oogenesis; Reference proteome; Repeat.
FT CHAIN 1..1541
FT /note="Regulator of G-protein signaling loco"
FT /id="PRO_0000408736"
FT DOMAIN 71..148
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 247..423
FT /note="PID"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00148"
FT DOMAIN 827..943
FT /note="RGS"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00171"
FT DOMAIN 1072..1142
FT /note="RBD 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 1143..1213
FT /note="RBD 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00262"
FT DOMAIN 1354..1376
FT /note="GoLoco"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT REGION 1..66
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 449..473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 978..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1258..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1410..1513
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 35..52
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 456..473
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 725..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1307..1324
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1421..1438
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1479..1506
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..712
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10079238"
FT /id="VSP_041115"
FT VAR_SEQ 1..669
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11731228"
FT /id="VSP_041114"
FT VAR_SEQ 1..367
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10079238"
FT /id="VSP_041116"
FT VAR_SEQ 368..713
FT /note="SCHVFVIDTKLIEHAQHLQRAHEFRLQCTRDPISNLCLEFPNNSEYVVNLVR
FT SMYTMRILPPASRSHQADYEAGAGAAAAGGAVAAAHSPQPSNHSEISTTTSNSDSGIGF
FT NNDCTNISDRILVVDFLAAGAGAAAAAHAGPPTYPAPARPLGIVGIPDNRLTVRAMPDH
FT SALLRSPPASSSLRRPNLLASFNLIQSPATNLTSTRSCDDVLNLFVDDSPRTLAAVASM
FT DDISLHSAAPSLDEGHTFAHPACVPRKMRRSLALETPTTPHKLSAQVFGQPGSRHSLGF
FT EAIDSVQSSVSGACMDQTMDTWASLQNLHKSHKDRTSMSASSSSHCLLEATNSEPDLG
FT -> MNNTNTTRGTCSRIPIARNQEPTIASMVERFVQSLSQLNDSGTFDSSFEIKRIHPG
FT SSAGSTPKHVRHRCLTELDREQLTRFVQDFEERQASTPKIKSKISSPYICRKAKEFYQS
FT ASGRRSASPQITIAPETVQEEKVLVNPLPRKCAEAEDLMPPPMAMARVQAERRSCRSAS
FT RVLQFFSSATKRRSGNRKLSEPEMEDNRADSPVLIRVTRDRVEEQLGCSPLAASGGEVP
FT TSSEDEEEHDDGISSASSNLTSQSGSSNSRNLSPDSSFEMHAPLLPSFKVTPPRAVCRV
FT GKNAACEFARFLRGSFHSKRASVTTLRRSLSDPDAVQQMDFSKPPPLRDTTNVMR (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:10079238"
FT /id="VSP_041117"
FT VAR_SEQ 713
FT /note="G -> M (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10079238"
FT /id="VSP_041118"
FT CONFLICT 1326
FT /note="A -> T (in Ref. 1; AAD24580/AAD24581)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1541 AA; 167282 MW; D2C07198B3DAD5B4 CRC64;
MHHHHPPLPI TGASGSTAVG TGAAAAEDAS PAANSGPAPI STSTTPSGSN SQQHQRRRKK
RANYNYNGIR TVEVRRGYNG FGFTISGQQP CRLSCIISSS PAEQAGLRSG DFLISVNGLN
VSKLPHETVV QLIGNSFGSI RMQIAENYYS DSSDEENAHA TLRGQLLAAS LRHKPRFLHH
KAKLHRLRNS PQKKLNPPEA VEPHKSKSSP DHPTLKPVLE DPPLTANLSK AADVANVSAM
VRAVGSAALE CRVIVGYLGT IEMPKQISHS SKLQTVRSCI RKLRQEKRQP TIVLMCITPD
SLSLQSSSGG VLATYSSARL NFVSSSSESE NRFFGLVTSA VHNTQIEEEY EPSAGSAAAA
GHISISHSCH VFVIDTKLIE HAQHLQRAHE FRLQCTRDPI SNLCLEFPNN SEYVVNLVRS
MYTMRILPPA SRSHQADYEA GAGAAAAGGA VAAAHSPQPS NHSEISTTTS NSDSGIGFNN
DCTNISDRIL VVDFLAAGAG AAAAAHAGPP TYPAPARPLG IVGIPDNRLT VRAMPDHSAL
LRSPPASSSL RRPNLLASFN LIQSPATNLT STRSCDDVLN LFVDDSPRTL AAVASMDDIS
LHSAAPSLDE GHTFAHPACV PRKMRRSLAL ETPTTPHKLS AQVFGQPGSR HSLGFEAIDS
VQSSVSGACM DQTMDTWASL QNLHKSHKDR TSMSASSSSH CLLEATNSEP DLGNRALPAN
ASPFRRAWGQ SSFRTPRSDK VAKEQQQLGQ SSPVRRTASM NASDNDMYIK TLMLDSDLKS
SRSQHQLSLL QVPKVLTTPA PPSAITASVA AEGAAQDHGC PSSWAGSFER MLQDAAGMQT
FSEFLKKEFS AENIYFWTAC ERYRLLESEA DRVAQAREIF AKHLANNSSD PVNVDSQARS
LTEEKLADAA PDIFAPAQKQ IFSLMKFDSY QRFIRSDLYK SCVEAEQKNQ PLPYSGLDLD
ELLKTNFHLG AFSKLKKSAS NAEDRRRKSL LPWHRKTRSK SRDRTEIMAD MQHALMPAPP
VPQNAPLTSA SLKLVCGQNS LSDLHSSRSS LSSFDAGTAT GGQGASTESV YSLCRVILTD
GATTIVQTRP GETVGELVER LLEKRNLVYP YYDIVFQGST KSIDVQQPSQ ILAGKEVVIE
RRVAFKLDLP DPKVISVKSK PKKQLHEVIR PILSKYNYKM EQVQVIMRDT QVPIDLNQPV
TMADGQRLRI VMVNSDFQVG GGSSMPPKQS KPMKPLPQGH LDELTNKVFN ELLASKADAA
ASEKSRPVDL CSMKSNEAPS ETSSLFERMR RQQRDGGNIP ASKLPKLKKK STSSSQQSEE
AATTQAVADP KKPIIAKLKA GVKLQVTERV AEHQDELLEG LKRAQLARLE DQRGTEINFD
LPDFLKNKEN LSAAVSKLRK VRASLSPVSK VPATPTEIPQ PAPRLSITRS QQPVSPMKVD
QEPETDLPAA TQDQTEFAKA PPPLPPKPKV LPIKPSNWGV AQPTGNYCNK YSPSKQVPTS
PKEASKPGTF ASKIPLDLGR KSLEEAGSRC AYLDEPSSSF V
