AXO_DROME
ID AXO_DROME Reviewed; 2179 AA.
AC M9PE65; M9NF15; M9NFN0; M9PBP8; Q9VZ96;
DT 25-MAY-2022, integrated into UniProtKB/Swiss-Prot.
DT 26-JUN-2013, sequence version 1.
DT 03-AUG-2022, entry version 78.
DE RecName: Full=Axotactin {ECO:0000312|FlyBase:FBgn0262870};
DE Flags: Precursor;
GN Name=axo {ECO:0000303|PubMed:10037607, ECO:0000312|FlyBase:FBgn0262870};
GN Synonyms=CG13715 {ECO:0000312|FlyBase:FBgn0262870},
GN CG13717 {ECO:0000312|FlyBase:FBgn0262870},
GN CG18296 {ECO:0000312|FlyBase:FBgn0262870},
GN CG32234 {ECO:0000312|FlyBase:FBgn0262870},
GN CG42664 {ECO:0000312|FlyBase:FBgn0262870},
GN CT1277 {ECO:0000312|FlyBase:FBgn0262870};
GN ORFNames=CG43225 {ECO:0000312|FlyBase:FBgn0262870};
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 {ECO:0000312|Proteomes:UP000000803};
RN [1] {ECO:0000312|Proteomes:UP000000803}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [2] {ECO:0000312|Proteomes:UP000000803}
RP GENOME REANNOTATION.
RC STRAIN=Berkeley {ECO:0000312|Proteomes:UP000000803};
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 [3] {ECO:0000305}
RP FUNCTION, SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=10037607; DOI=10.1126/science.283.5406.1343;
RA Yuan L.L., Ganetzky B.;
RT "A glial-neuronal signaling pathway revealed by mutations in a neurexin-
RT related protein.";
RL Science 283:1343-1345(1999).
CC -!- FUNCTION: May have serine protease inhibitor activity (Probable). Might
CC play a role in the glial-neuronal signaling pathway that is important
CC in establishing the electrical properties of axonal membranes
CC (PubMed:10037607). {ECO:0000269|PubMed:10037607, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell projection, axon
CC {ECO:0000269|PubMed:10037607}. Membrane {ECO:0000255}; Single-pass type
CC I membrane protein {ECO:0000255}. Note=Localizes to longitudinal axon
CC tracts as well as to an axonal scaffold in the brain (PubMed:10037607).
CC A secreted form might exist (Probable). {ECO:0000269|PubMed:10037607,
CC ECO:0000305|PubMed:10037607}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=C {ECO:0000312|FlyBase:FBgn0262870}; Synonyms=G
CC {ECO:0000312|FlyBase:FBgn0262870};
CC IsoId=M9PE65-1; Sequence=Displayed;
CC Name=B {ECO:0000312|FlyBase:FBgn0262870};
CC IsoId=M9PE65-2; Sequence=VSP_061454, VSP_061461;
CC Name=D {ECO:0000312|FlyBase:FBgn0262870}; Synonyms=H
CC {ECO:0000312|FlyBase:FBgn0262870};
CC IsoId=M9PE65-3; Sequence=VSP_061456, VSP_061459;
CC Name=F {ECO:0000312|FlyBase:FBgn0262870};
CC IsoId=M9PE65-4; Sequence=VSP_061455, VSP_061460;
CC Name=I {ECO:0000312|FlyBase:FBgn0262870};
CC IsoId=M9PE65-5; Sequence=VSP_061457, VSP_061458;
CC -!- DEVELOPMENTAL STAGE: Expressed in the brain and parts of the peripheral
CC nervous system (at protein level) (PubMed:10037607). Expressed from
CC embryonic stage 13 in the differentiating nervous system in a subset of
CC glial cells, including longitudinal glia and segmental boundary cells
CC (PubMed:10037607). {ECO:0000269|PubMed:10037607}.
CC -!- DISRUPTION PHENOTYPE: Temperature-dependent loss of excitatory
CC junctional potentials in the larval neuromuscular junction.
CC {ECO:0000269|PubMed:10037607}.
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DR EMBL; AE014296; AAF47929.4; -; Genomic_DNA.
DR EMBL; AE014296; AFH04301.1; -; Genomic_DNA.
DR EMBL; AE014296; AFH04302.1; -; Genomic_DNA.
DR EMBL; AE014296; AFH04303.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94117.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94118.1; -; Genomic_DNA.
DR EMBL; AE014296; AGB94119.1; -; Genomic_DNA.
DR RefSeq; NP_001246630.1; NM_001259701.1.
DR RefSeq; NP_001246631.1; NM_001259702.1.
DR RefSeq; NP_001246632.1; NM_001259703.1.
DR RefSeq; NP_001261422.1; NM_001274493.1.
DR RefSeq; NP_001261423.1; NM_001274494.1.
DR RefSeq; NP_001261424.1; NM_001274495.1.
DR RefSeq; NP_524656.5; NM_079917.5.
DR AlphaFoldDB; M9PE65; -.
DR SMR; M9PE65; -.
DR IntAct; M9PE65; 6.
DR STRING; 7227.FBpp0305769; -.
DR MEROPS; I02.968; -.
DR PaxDb; M9PE65; -.
DR PeptideAtlas; M9PE65; -.
DR PRIDE; M9PE65; -.
DR EnsemblMetazoa; FBtr0302646; FBpp0291786; FBgn0262870. [M9PE65-2]
DR EnsemblMetazoa; FBtr0306206; FBpp0297315; FBgn0262870. [M9PE65-1]
DR EnsemblMetazoa; FBtr0306207; FBpp0297316; FBgn0262870. [M9PE65-3]
DR EnsemblMetazoa; FBtr0333591; FBpp0305768; FBgn0262870. [M9PE65-4]
DR EnsemblMetazoa; FBtr0333592; FBpp0305769; FBgn0262870. [M9PE65-1]
DR EnsemblMetazoa; FBtr0333593; FBpp0305770; FBgn0262870. [M9PE65-3]
DR EnsemblMetazoa; FBtr0333594; FBpp0305771; FBgn0262870. [M9PE65-5]
DR GeneID; 43923; -.
DR KEGG; dme:Dmel_CG43225; -.
DR CTD; 43923; -.
DR FlyBase; FBgn0262870; axo.
DR VEuPathDB; VectorBase:FBgn0262870; -.
DR eggNOG; KOG3516; Eukaryota.
DR eggNOG; KOG4295; Eukaryota.
DR HOGENOM; CLU_002286_0_0_1; -.
DR InParanoid; M9PE65; -.
DR OMA; SWHAVEL; -.
DR OrthoDB; 338397at2759; -.
DR PhylomeDB; M9PE65; -.
DR BioGRID-ORCS; 43923; 0 hits in 1 CRISPR screen.
DR GenomeRNAi; 43923; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0262870; Expressed in adult hindgut (Drosophila) and 18 other tissues.
DR ExpressionAtlas; M9PE65; baseline and differential.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0005576; C:extracellular region; ISS:FlyBase.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:UniProtKB-KW.
DR GO; GO:0009653; P:anatomical structure morphogenesis; IEA:UniProt.
DR GO; GO:0048513; P:animal organ development; IEA:UniProt.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProt.
DR GO; GO:0016043; P:cellular component organization; IEA:UniProt.
DR GO; GO:0019226; P:transmission of nerve impulse; IMP:FlyBase.
DR CDD; cd00109; KU; 1.
DR CDD; cd00110; LamG; 4.
DR Gene3D; 4.10.410.10; -; 1.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR000742; EGF-like_dom.
DR InterPro; IPR002223; Kunitz_BPTI.
DR InterPro; IPR036880; Kunitz_BPTI_sf.
DR InterPro; IPR001791; Laminin_G.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF02210; Laminin_G_2; 6.
DR SMART; SM00181; EGF; 4.
DR SMART; SM00131; KU; 1.
DR SMART; SM00282; LamG; 6.
DR SUPFAM; SSF49899; SSF49899; 6.
DR SUPFAM; SSF57362; SSF57362; 1.
DR PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 4.
DR PROSITE; PS50025; LAM_G_DOMAIN; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Disulfide bond; EGF-like domain;
KW Glycoprotein; Membrane; Protease inhibitor; Reference proteome; Repeat;
KW Serine protease inhibitor; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..2179
FT /note="Axotactin"
FT /evidence="ECO:0000255"
FT /id="PRO_5015096687"
FT TOPO_DOM 19..1816
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 1817..1837
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1838..2179
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT DOMAIN 119..170
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DOMAIN 242..438
FT /note="Laminin G-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 439..477
FT /note="EGF-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 481..664
FT /note="Laminin G-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 660..839
FT /note="Laminin G-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 841..879
FT /note="EGF-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1087..1259
FT /note="Laminin G-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1260..1297
FT /note="EGF-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1316..1526
FT /note="Laminin G-like 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DOMAIN 1527..1565
FT /note="EGF-like 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DOMAIN 1569..1765
FT /note="Laminin G-like 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT REGION 59..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 201..220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1891..2141
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2156..2179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1915..1932
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1950..1970
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1971..1987
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2005..2026
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2063..2078
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2079..2107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2163..2179
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 23
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 52
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 249
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 542
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 571
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 741
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 925
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1000
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1019
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1026
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1393
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1667
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1707
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1751
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 1782
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 119..170
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 128..152
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 144..166
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00031"
FT DISULFID 405..438
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 442..455
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 449..464
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 466..476
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 808..839
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 845..857
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 851..866
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 868..878
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1231..1259
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1263..1274
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1268..1283
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1285..1296
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1494..1526
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT DISULFID 1530..1541
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1535..1552
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1554..1564
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 1722..1765
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00122"
FT VAR_SEQ 2042..2148
FT /note="HPIQPPDAIFMPNLPQKAQQRQPQEHKSRHKATDDTEAPKQQQQQQQQQQSF
FT DVATNANGSSLPASRVKNPEEPGGKSPLVPMRQHHSKVTRPPPPPTLFLENSLLQ ->
FT QQHEMQKQLPPQRQLSQRGVGIQQQTSSKRRKPVGSGGAGGATVVGPATVRRQVSWGPP
FT IVAETDVDLANNSSGNGNGNGNGNGNRKAGGKQNGYHGVNRRATTTRN (in
FT isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_061454"
FT VAR_SEQ 2042..2147
FT /note="HPIQPPDAIFMPNLPQKAQQRQPQEHKSRHKATDDTEAPKQQQQQQQQQQSF
FT DVATNANGSSLPASRVKNPEEPGGKSPLVPMRQHHSKVTRPPPPPTLFLENSLL -> Q
FT HEMQKQLPPQRQLSQRGVGIQQQTSSKRRKPVGSGGAGGATVVGPATVRRQVSWGPPIV
FT AETDVDLANNSSGNGNGNGNGNGNRKAGGKQNGYHGVNRRATTTRN (in isoform
FT F)"
FT /evidence="ECO:0000305"
FT /id="VSP_061455"
FT VAR_SEQ 2042..2070
FT /note="HPIQPPDAIFMPNLPQKAQQRQPQEHKSR -> VSRGSQPTVNLVRMAPIAT
FT ISETNLHGLG (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_061456"
FT VAR_SEQ 2042..2047
FT /note="HPIQPP -> PNRIKP (in isoform I)"
FT /evidence="ECO:0000305"
FT /id="VSP_061457"
FT VAR_SEQ 2048..2179
FT /note="Missing (in isoform I)"
FT /evidence="ECO:0000305"
FT /id="VSP_061458"
FT VAR_SEQ 2071..2179
FT /note="Missing (in isoform D)"
FT /evidence="ECO:0000305"
FT /id="VSP_061459"
FT VAR_SEQ 2148..2179
FT /note="Missing (in isoform F)"
FT /evidence="ECO:0000305"
FT /id="VSP_061460"
FT VAR_SEQ 2149..2179
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_061461"
SQ SEQUENCE 2179 AA; 241567 MW; 7D226EF8C6FA52CE CRC64;
MAFPYIWALL PLICSASGLS LPNMTSTDAV VAGGGILPIL VAGNPGNLGS SNMSLSGGGG
LAGSSTGGQS LPDTGGGNSA GGSPAGGSSG TGGGGSNSGI SGNNSAMIQG QKSNQYEKCA
GPGDPGPCKQ YIYKWRYEPT TNECTNFIWG GCEGNPQNRF GTEAECLFHC IGGPHTLPPF
LQSTTREPST TESSMLLGLP YTQSPAQSPD GMGGAEGGDG TTPVPIEQRG PELTFAETGQ
GKTFIFAKNN TFIQMDGDII QTFQLRLCRE ISFQFRTRLP HGLLVYHNVK NPDRINLDPY
ALYVIVEKGQ LKVVHVFGKH STSVTVGESL NRDEWHSVMV RIDVHGARLI ARVDNSQEEV
YLKGLNHEYN YGVSTNLPSV VLVGGLSSEE KLHGVKYITE SFVGCIRNVV LSSGKAASDL
LPIAPLVATK HENVNEGCSD MCESRHNLCF VGSRCINHYG GISCDCFGTH YEGEHCDIYT
ATIITLRGAS YVSYRIYDWK DRVHSSTRRI SLMFRTNFDD SALFYASGES LKHQYIAASI
KNQSVHVEMD FGDNVMSTVL TDDLTRGYWH NLTILHEQRT VSIILDQQQK VLELPATASG
NMLFDPEIYF GGGPELHKKK GLASHNNFVG SLKYVYYNDI SILYELQRGN PKVHYHGVLE
AEFVENEVNV IPITYPFATS HIWWPINHAE EFNIKFDFRS SRPGAVLAYS DVTTSAGNGF
WEIRLTSDKL SFDLVPDVNN NVTHSTTIKI NRATSWHSVE LDYKLGEIRF TVDYRHTLSQ
MYGLTFNIGD KLIIGSSLKS AAMGLVGCIR DIEINGHLIE PRHVVKTERV VGEVALDNCN
YIDPCKRPNT CEHGGKCFVK DDRVTCDCKH TGYIGKNCHF TKYRKTCEEL ALLGFTKSDV
YLIDIDGNGV FPPAHVKCDF QSLENATKTI VEHNLPSQVD VRSARESDFS FNIRYREFSP
HMLQELISHS LYCTQYIKYD CYRAQLELHS ATWFTSSAKN LTVDFLGNVK RGACPCSVNK
TCVDPNQSCN CDVKENKWNS DEGYYQDPQS LGITNMYFLQ QKDMDDEAQG RITLGPLECV
ETNTQKYVVT FTTSQSYIEV PGWRKGDIAF SFRTTGEKAI LLFQPPIRPH YPSFMVALTG
DDQLTFTFTL STGTTRELVI NSHRRLNGGE WHKIWIDYNQ YHVRFMINTD YQMLDLLPEE
EFGPFEGSMY IGGATFDLLK KLSVKAGLIG CFRGLVVNGE ILDIYSYMSV HLSEIIKDCK
PSCVPSPCRN GAQCKELWSS FKCVCNNPWA HIGEFCETNI NEKALTFINR ESFLMRNYLS
VGATPVILMH GINGERDVLK GILNQDLLIN LRTYDTNALV LYANDHYNNF VHLYISLNRE
IVFLYNYGDE IVNLTLLDDT LMASLKSIQV AIVRGEQETR MHVNEHSVSI DRGTLLLDEY
ANKPWSNPEK EVLSPHRPPA PPTEYFQFHV GGYDPANLLR PNVDAPALEG YIGCVRGLKI
GAQLIDLADI NERNIAPTQE GVLPNCQIKC DAEPCKNGGT CQEHFAEQLS TCDCEHTSFL
GEFCSEEKGA DFSGESTLQR KFELPGTGRV DYVRLQLAFS SFDLRRANRI MLLMQTEAER
SYYLLLAITS DGYLQLEEDR DNGQTVGARI DRNFLNSARH SVYYVRNGTQ SQLFIDREQV
PLSEFAARVL TTGGDAGSNR VQIGGINSTD SRFAVFKSYS GCLSNIYIQV NGHVMKPLEE
YMLFTKSGAD NITVINPQGV RSAQCNAKFD VSEQPTQEPM VNVSMIPEPW VEEPPARVPY
IPRFVYDENK QEDSTQVVFL TLTSVFVIIV ICCLLEVYRS HLAYKKRIER ETDEDIIWSK
EQATKMHESP GVKAGLLGGV TAGSGNGLPP YTYKALPQED KKPGNGAPLV GILKNGSATP
SQPGTPTALS KNGDIASRIE EEEEEEDEAP AQKAAEKSGE NEEPPAKDTT ASEIKESQAQ
PPEQLAKDTT DASAAPKASK ETEAQAEPSE PSSQLNSAQN GQLAQMEQAA RGDEVQVPSL
PHPIQPPDAI FMPNLPQKAQ QRQPQEHKSR HKATDDTEAP KQQQQQQQQQ QSFDVATNAN
GSSLPASRVK NPEEPGGKSP LVPMRQHHSK VTRPPPPPTL FLENSLLQRQ FANPISYLGG
PRLQPRSNRT SIDSILSLD
