PTRO_DROME
ID PTRO_DROME Reviewed; 1630 AA.
AC A1ZAU8; A1ZAU9; A1ZAV0; Q86NU5; Q8MSU7;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Patronin;
DE AltName: Full=Short spindle protein 4;
GN Name=Patronin; Synonyms=l(2)k07433, ssp4; ORFNames=CG33130;
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 [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 [2]
RP GENOME REANNOTATION, AND ALTERNATIVE SPLICING.
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Testis;
RA Stapleton M., Brokstein P., Hong L., Agbayani A., Carlson J.W., Champe M.,
RA Chavez C., Dorsett V., Dresnek D., Farfan D., Frise E., George R.A.,
RA Gonzalez M., Guarin H., Kronmiller B., Li P.W., Liao G., Miranda A.,
RA Mungall C.J., Nunoo J., Pacleb J.M., Paragas V., Park S., Patel S.,
RA Phouanenavong S., Wan K.H., Yu C., Lewis S.E., Rubin G.M., Celniker S.E.;
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 941-1630 (ISOFORM B).
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-322; SER-422; SER-431;
RP SER-441; SER-460; SER-463; SER-466; THR-492; SER-494; SER-496; SER-513;
RP SER-530; SER-1034; SER-1035; SER-1036; SER-1219; SER-1228; SER-1398;
RP SER-1399 AND SER-1400, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Embryo;
RX PubMed=18327897; DOI=10.1021/pr700696a;
RA Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
RT "Phosphoproteome analysis of Drosophila melanogaster embryos.";
RL J. Proteome Res. 7:1675-1682(2008).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-460 AND SER-1067, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=17372656; DOI=10.1039/b617545g;
RA Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D., Juenger M.A.,
RA Eng J.K., Aebersold R., Tao W.A.;
RT "An integrated chemical, mass spectrometric and computational strategy for
RT (quantitative) phosphoproteomics: application to Drosophila melanogaster
RT Kc167 cells.";
RL Mol. Biosyst. 3:275-286(2007).
RN [7]
RP FUNCTION.
RX PubMed=17412918; DOI=10.1126/science.1141314;
RA Goshima G., Wollman R., Goodwin S.S., Zhang N., Scholey J.M., Vale R.D.,
RA Stuurman N.;
RT "Genes required for mitotic spindle assembly in Drosophila S2 cells.";
RL Science 316:417-421(2007).
RN [8]
RP FUNCTION, ASSOCIATION WITH MICROTUBULES, SUBUNIT, AND SUBCELLULAR LOCATION.
RX PubMed=20946984; DOI=10.1016/j.cell.2010.09.022;
RA Goodwin S.S., Vale R.D.;
RT "Patronin regulates the microtubule network by protecting microtubule minus
RT ends.";
RL Cell 143:263-274(2010).
RN [9]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=24100293; DOI=10.1083/jcb.201306001;
RA Wang H., Brust-Mascher I., Civelekoglu-Scholey G., Scholey J.M.;
RT "Patronin mediates a switch from kinesin-13-dependent poleward flux to
RT anaphase B spindle elongation.";
RL J. Cell Biol. 203:35-46(2013).
RN [10]
RP FUNCTION.
RX PubMed=26246606; DOI=10.1091/mbc.e15-02-0113;
RA Carvalhal S., Ribeiro S.A., Arocena M., Kasciukovic T., Temme A.,
RA Koehler K., Huebner A., Griffis E.R.;
RT "The nucleoporin ALADIN regulates Aurora A localization to ensure robust
RT mitotic spindle formation.";
RL Mol. Biol. Cell 26:3424-3438(2015).
RN [11]
RP FUNCTION.
RX PubMed=26659188; DOI=10.1038/nature16443;
RA Derivery E., Seum C., Daeden A., Loubery S., Holtzer L., Juelicher F.,
RA Gonzalez-Gaitan M.;
RT "Polarized endosome dynamics by spindle asymmetry during asymmetric cell
RT division.";
RL Nature 528:280-285(2015).
CC -!- FUNCTION: Involved in mitotic spindle assembly (PubMed:17412918,
CC PubMed:26246606). Regulates microtubule (MT) severing
CC (PubMed:17412918). Antagonizes the activity of the kinesin-13
CC depolymerase Klp10A thereby switching off the depolymerization of the
CC MTs at their pole-associated minus ends, which turns off poleward flux
CC and induces anaphase B spindle elongation (PubMed:20946984,
CC PubMed:24100293). Involved in asymmetric cell division of sensory organ
CC precursor (SOP) cells by playing a role in the asymmetric localization
CC of Sara-expressing endosomes to the pIIa daughter cell but not to the
CC pIIb cell. Klp98A targets Sara-expressing endosomes to the central
CC spindle which is symmetrically arranged in early cell division. During
CC late cytokinesis, central spindle asymmetry is generated by enrichment
CC of Patronin on the pIIb side which protects microtubules from
CC depolymerization by Klp10A while unprotected microtubules on the pIIa
CC side are disassembled by Klp10A, leading to the asymmetric delivery of
CC Sara-expressing endosomes to the pIIa daughter cell (PubMed:26659188).
CC {ECO:0000269|PubMed:17412918, ECO:0000269|PubMed:20946984,
CC ECO:0000269|PubMed:24100293, ECO:0000269|PubMed:26246606,
CC ECO:0000269|PubMed:26659188}.
CC -!- SUBUNIT: Associates with the minus end of the microtubules.
CC {ECO:0000269|PubMed:20946984}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, microtubule organizing
CC center, spindle pole body. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome. Note=Localizes to centrosomes in
CC prophase, to the midbody during cytokinesis, diffusely throughout the
CC metaphase spindle and to punctae in interphase that often overlap with
CC MTs. Colocalizes with Sas-4 and SAK at the microtubule organizing
CC center.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=C;
CC IsoId=A1ZAU8-1; Sequence=Displayed;
CC Name=A;
CC IsoId=A1ZAU8-2; Sequence=VSP_037213, VSP_037214, VSP_037215;
CC Name=B;
CC IsoId=A1ZAU8-3; Sequence=VSP_037213, VSP_037214, VSP_037216;
CC -!- DOMAIN: The CKK domain binds microtubules. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
CC -!- SIMILARITY: Belongs to the CAMSAP1 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00841}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAM49943.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE013599; AAO41362.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64821.1; -; Genomic_DNA.
DR EMBL; AE013599; AAS64822.1; -; Genomic_DNA.
DR EMBL; BT003634; AAO39638.1; -; mRNA.
DR EMBL; AY118574; AAM49943.1; ALT_INIT; mRNA.
DR RefSeq; NP_788398.1; NM_176218.3. [A1ZAU8-2]
DR RefSeq; NP_995875.1; NM_206153.3. [A1ZAU8-1]
DR RefSeq; NP_995876.1; NM_206154.3. [A1ZAU8-3]
DR AlphaFoldDB; A1ZAU8; -.
DR SMR; A1ZAU8; -.
DR BioGRID; 62669; 21.
DR IntAct; A1ZAU8; 4.
DR STRING; 7227.FBpp0304550; -.
DR iPTMnet; A1ZAU8; -.
DR PRIDE; A1ZAU8; -.
DR EnsemblMetazoa; FBtr0086948; FBpp0086104; FBgn0263197. [A1ZAU8-2]
DR EnsemblMetazoa; FBtr0086949; FBpp0086105; FBgn0263197. [A1ZAU8-3]
DR EnsemblMetazoa; FBtr0086950; FBpp0086106; FBgn0263197. [A1ZAU8-1]
DR GeneID; 36978; -.
DR KEGG; dme:Dmel_CG33130; -.
DR UCSC; CG33130-RA; d. melanogaster.
DR UCSC; CG33130-RB; d. melanogaster.
DR UCSC; CG33130-RC; d. melanogaster. [A1ZAU8-1]
DR CTD; 36978; -.
DR FlyBase; FBgn0263197; Patronin.
DR VEuPathDB; VectorBase:FBgn0263197; -.
DR eggNOG; KOG3654; Eukaryota.
DR GeneTree; ENSGT00950000182975; -.
DR InParanoid; A1ZAU8; -.
DR SignaLink; A1ZAU8; -.
DR BioGRID-ORCS; 36978; 0 hits in 3 CRISPR screens.
DR GenomeRNAi; 36978; -.
DR PRO; PR:A1ZAU8; -.
DR Proteomes; UP000000803; Chromosome 2R.
DR Bgee; FBgn0263197; Expressed in cleaving embryo and 24 other tissues.
DR ExpressionAtlas; A1ZAU8; baseline and differential.
DR Genevisible; A1ZAU8; DM.
DR GO; GO:0061802; C:anterior cell cortex; IDA:FlyBase.
DR GO; GO:0005813; C:centrosome; IDA:FlyBase.
DR GO; GO:0097575; C:lateral cell cortex; IDA:FlyBase.
DR GO; GO:0005874; C:microtubule; IDA:FlyBase.
DR GO; GO:0030496; C:midbody; IDA:FlyBase.
DR GO; GO:0072686; C:mitotic spindle; IDA:FlyBase.
DR GO; GO:0005819; C:spindle; IDA:FlyBase.
DR GO; GO:0120219; C:subapical part of cell; IDA:FlyBase.
DR GO; GO:0005516; F:calmodulin binding; IEA:InterPro.
DR GO; GO:0008017; F:microtubule binding; ISS:FlyBase.
DR GO; GO:0051011; F:microtubule minus-end binding; IDA:FlyBase.
DR GO; GO:0030507; F:spectrin binding; IEA:InterPro.
DR GO; GO:0045167; P:asymmetric protein localization involved in cell fate determination; IMP:FlyBase.
DR GO; GO:0051298; P:centrosome duplication; IMP:FlyBase.
DR GO; GO:0043622; P:cortical microtubule organization; IMP:FlyBase.
DR GO; GO:0031122; P:cytoplasmic microtubule organization; IBA:GO_Central.
DR GO; GO:0061867; P:establishment of mitotic spindle asymmetry; IMP:FlyBase.
DR GO; GO:0000226; P:microtubule cytoskeleton organization; IMP:FlyBase.
DR GO; GO:0007052; P:mitotic spindle organization; IMP:FlyBase.
DR GO; GO:0035331; P:negative regulation of hippo signaling; IGI:FlyBase.
DR GO; GO:0007026; P:negative regulation of microtubule depolymerization; IMP:FlyBase.
DR GO; GO:0031175; P:neuron projection development; IEA:InterPro.
DR Gene3D; 3.10.20.360; -; 1.
DR InterPro; IPR032940; CAMSAP.
DR InterPro; IPR022613; CAMSAP-like_CH_dom.
DR InterPro; IPR031372; CAMSAP_CC1.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR038209; CKK_dom_sf.
DR InterPro; IPR014797; CKK_domain.
DR InterPro; IPR011033; PRC_barrel-like_sf.
DR PANTHER; PTHR21595; PTHR21595; 2.
DR Pfam; PF17095; CAMSAP_CC1; 1.
DR Pfam; PF11971; CAMSAP_CH; 1.
DR Pfam; PF08683; CAMSAP_CKK; 1.
DR SMART; SM01051; CAMSAP_CKK; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR SUPFAM; SSF50346; SSF50346; 1.
DR PROSITE; PS50021; CH; 1.
DR PROSITE; PS51508; CKK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell cycle; Coiled coil; Cytoplasm; Cytoskeleton;
KW Microtubule; Phosphoprotein; Reference proteome.
FT CHAIN 1..1630
FT /note="Patronin"
FT /id="PRO_0000372861"
FT DOMAIN 156..288
FT /note="Calponin-homology (CH)"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 1489..1623
FT /note="CKK"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00841"
FT REGION 311..333
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 355..446
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 486..589
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 726..753
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 872..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1005..1042
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1055..1186
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1200..1241
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1284..1315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1335..1459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 601..639
FT /evidence="ECO:0000255"
FT COILED 1277..1343
FT /evidence="ECO:0000255"
FT COMPBIAS 355..397
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..427
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 494..509
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 510..529
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 545..585
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 872..890
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 919..953
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1055..1076
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1093..1124
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1216..1241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1335..1349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1350..1365
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1384..1446
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 322
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 422
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 441
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 460
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656,
FT ECO:0000269|PubMed:18327897"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 466
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 492
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 494
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 513
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 530
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1034
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1035
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1036
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1067
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:17372656"
FT MOD_RES 1219
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1228
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1398
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1399
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT MOD_RES 1400
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18327897"
FT VAR_SEQ 418
FT /note="R -> RGDFVAAGRPSNWEQSRRPSFA (in isoform A and
FT isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.3"
FT /id="VSP_037213"
FT VAR_SEQ 671..719
FT /note="Missing (in isoform A and isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569, ECO:0000303|Ref.3"
FT /id="VSP_037214"
FT VAR_SEQ 1404..1488
FT /note="Missing (in isoform A)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_037215"
FT VAR_SEQ 1404..1488
FT /note="GYGQLSSNSMKRDYYRGSQDSLTVKESPDDYPSTSSTPIGRRGSYKTSREPA
FT GVERGRTLSRISVAKGSTLNFRGRKSNSLMNLC -> DSGLGRATPPRRAPSPGMGMGA
FT S (in isoform B)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_037216"
FT CONFLICT 805
FT /note="T -> A (in Ref. 3; AAO39638)"
FT /evidence="ECO:0000305"
FT CONFLICT 1170
FT /note="N -> S (in Ref. 3; AAO39638)"
FT /evidence="ECO:0000305"
FT CONFLICT 1177
FT /note="P -> H (in Ref. 3; AAO39638)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1630 AA; 183622 MW; B8182F1FCEBF51DF CRC64;
MDVETQEIRQ ARQRASVKWL LSKAFNNRVP DNLKEPFYRD HENQERLKPQ IIVELGNATL
YCQTLANLYS DPNYQSMNHW SIIQTLARKG VPVAESADMP ITETVLIQTN PLRINAHMSV
IESLMVLYAK EISSGDRVMA AIRRISGNNY QAPTGQSYEQ ALLGWISHAC AALKKRIIKE
VDAGLPDDNG SRLQTPDIPP VRDFQDLCDG ICLALLISYY CPKVVPWTSV RINYLPAVED
SIHNILLVCN FSQKHLPYTV MHMTPEDVTY MRGSMKLNLV VLLTDLFNLF EIHPAKCVCY
PGMDGQVPHS NSFGGGLNRR STPPNEYQTV QSNNFDGNHA EAFVVHKSRG ITTLASMHSQ
QQQQLHQQQQ HQQQYHQQPL QQHPSQSQLQ IQQQEPLVPA RLRQAKEKTN VESKADERGR
RSRRNSSSED SQLTIENFGG SQDQLNTLGR YERDRERKLS NTSVGSYPVE PAVAVRSSIA
DARGTLQLGY DTDSGSEKQD RETEKYSMRR QVSVDNVPTV SSHNLSNAGS PLPVARHKQH
SSDKDYSSNS GMTPDAYNDS RSTSGYDPES TPVRKSSTSS MPASPAAWQL DVGDDDMRSL
ENASKLSTIR MKLEEKRRRI EQDKRKIEMA LLRHQEKEDL ESCPDVMKWE TMSNESKRTP
DMDPVDLDKY QQSIAIMNMN LQDIQQDIHR LATQQSQMQA QHLQAQQLMQ AQQIANMLNQ
AYNAPVSAYS SRPPSRDPYQ QQLHHQQQQP MPMPQPMQYV NEHGQYMSPP QPAHYMPQQA
QQPQSIYSDN GAAYNHSNHS PYGGTPQYRS SVVYDDYGQP TNHFYLHESS PQPQAHQHPQ
RRTWAHSAAA AAYEQQQQIQ PSLVDVNAWQ TQQHQKQKQT WMNRPPSSAG APSPGSFMLH
QNGGGGGGGG GGGELQHLFQ VQASPQHGQR QVSGSNGVQR QQSLTNLRDN RSPKAPQNMG
MPMGMPMQQE DMMAPQSICF IGDEEDVDEL ERNIIESMQS THISDFVHQQ QQQHQHQQQL
QQQQRLQGHS GRGSSSEDYD SGEMISNKLN ITSGNLTYRI PSPSRPSIQA NSFQDPRAMA
AASGGEDQPP EKGFYISFDD EQPKRPKPPL RAKRSPKKES PPGSRDSVDN QATLKRESLS
HLHNNNNIGF GNDDVNSKPV TRHSIHGLNN SNSVKSPGNA TYNKYTDEPP IQLRQLAVSG
AMSPTSNERH HLDDVSNQSP QQTQQPMSPT RLQQSSNNAE AAKNKALVIG ADSTNLDPES
VDEMERRKEK IMLLSLQRRQ QQEEAKARKE IEASQKREKE REKEEERARK KEEQMARRAA
ILEQHRLKKA IEEAEREGKT LDRPDLHVKL QSHSSTSTTP RLRQQRTTRP RPKTIHVDDA
SVDISEASSI SSRGKKGSSS NLTGYGQLSS NSMKRDYYRG SQDSLTVKES PDDYPSTSST
PIGRRGSYKT SREPAGVERG RTLSRISVAK GSTLNFRGRK SNSLMNLCGP KLYKQPAAKS
NRGIILNAVE YCVFPGVVNR EAKQKVLEKI ARSEAKHFLV LFRDAGCQFR ALYSYQPETD
QVTKLYGTGP SQVEEVMFDK FFKYNSGGKC FSQVHTKHLT VTIDAFTIHN SLWQGKRVQL
PSKKDMALVI
