PAN1_YEAST
ID PAN1_YEAST Reviewed; 1480 AA.
AC P32521; D6VVT6;
DT 01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 2.
DT 03-AUG-2022, entry version 197.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein PAN1;
DE AltName: Full=Mitochondrial distribution of proteins protein 3;
GN Name=PAN1; Synonyms=DIM2, MDP3, MIP3; OrderedLocusNames=YIR006C;
GN ORFNames=YIB6C;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 320-344; 352-375
RP AND 899-906.
RX PubMed=1339314; DOI=10.1016/0092-8674(92)90246-9;
RA Sachs A.B., Deardorff J.A.;
RT "Translation initiation requires the PAB-dependent poly(A) ribonuclease in
RT yeast.";
RL Cell 70:961-973(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=7762303; DOI=10.1002/yea.320110109;
RA Voss H., Tamames J., Teodoru C., Valencia A., Sensen C., Wiemann S.,
RA Schwager C., Zimmermann J., Sander C., Ansorge W.;
RT "Nucleotide sequence and analysis of the centromeric region of yeast
RT chromosome IX.";
RL Yeast 11:61-78(1995).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169870;
RA Churcher C.M., Bowman S., Badcock K., Bankier A.T., Brown D.,
RA Chillingworth T., Connor R., Devlin K., Gentles S., Hamlin N., Harris D.E.,
RA Horsnell T., Hunt S., Jagels K., Jones M., Lye G., Moule S., Odell C.,
RA Pearson D., Rajandream M.A., Rice P., Rowley N., Skelton J., Smith V.,
RA Walsh S.V., Whitehead S., Barrell B.G.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IX.";
RL Nature 387:84-87(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP FUNCTION.
RX PubMed=8524255; DOI=10.1128/mcb.15.12.6884;
RA Zoladek T., Vaduva G., Hunter L.A., Boguta M., Go B.D., Martin N.C.,
RA Hopper A.K.;
RT "Mutations altering the mitochondrial-cytoplasmic distribution of Mod5p
RT implicate the actin cytoskeleton and mRNA 3' ends and/or protein synthesis
RT in mitochondrial delivery.";
RL Mol. Cell. Biol. 15:6884-6894(1995).
RN [6]
RP FUNCTION, AND DOMAIN.
RX PubMed=8978817; DOI=10.1083/jcb.135.6.1485;
RA Wendland B., McCaffery J.M., Xiao Q., Emr S.D.;
RT "A novel fluorescence-activated cell sorter-based screen for yeast
RT endocytosis mutants identifies a yeast homologue of mammalian eps15.";
RL J. Cell Biol. 135:1485-1500(1996).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=8756649; DOI=10.1128/mcb.16.9.4897;
RA Tang H.-Y., Cai M.;
RT "The EH-domain-containing protein Pan1 is required for normal organization
RT of the actin cytoskeleton in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 16:4897-4914(1996).
RN [8]
RP IDENTIFICATION IN THE PAN1 COMPLEX, FUNCTION OF THE PAN1 COMPLEX, AND
RP SUBCELLULAR LOCATION.
RX PubMed=9234686; DOI=10.1128/mcb.17.8.4294;
RA Tang H.-Y., Munn A., Cai M.;
RT "EH domain proteins Pan1p and End3p are components of a complex that plays
RT a dual role in organization of the cortical actin cytoskeleton and
RT endocytosis in Saccharomyces cerevisiae.";
RL Mol. Cell. Biol. 17:4294-4304(1997).
RN [9]
RP EH DOMAINS.
RX PubMed=9822599; DOI=10.1093/emboj/17.22.6541;
RA Paoluzi S., Castagnoli L., Lauro I., Salcini A.E., Coda L., Fre' S.,
RA Confalonieri S., Pelicci P.G., Di Fiore P.P., Cesareni G.;
RT "Recognition specificity of individual EH domains of mammals and yeast.";
RL EMBO J. 17:6541-6550(1998).
RN [10]
RP FUNCTION, AND INTERACTION WITH YAP1801 AND YAP1802.
RX PubMed=9531549; DOI=10.1083/jcb.141.1.71;
RA Wendland B., Emr S.D.;
RT "Pan1p, yeast eps15, functions as a multivalent adaptor that coordinates
RT protein-protein interactions essential for endocytosis.";
RL J. Cell Biol. 141:71-84(1998).
RN [11]
RP PHOSPHORYLATION BY PRK1, AND INTERACTION WITH END3.
RX PubMed=9885245; DOI=10.1083/jcb.144.1.71;
RA Zeng G., Cai M.;
RT "Regulation of the actin cytoskeleton organization in yeast by a novel
RT serine/threonine kinase Prk1p.";
RL J. Cell Biol. 144:71-82(1999).
RN [12]
RP FUNCTION.
RX PubMed=10954428; DOI=10.1242/jcs.113.18.3309;
RA Gagny B., Wiederkehr A., Dumoulin P., Winsor B., Riezman H.,
RA Haguenauer-Tsapis R.;
RT "A novel EH domain protein of Saccharomyces cerevisiae, Ede1p, involved in
RT endocytosis.";
RL J. Cell Sci. 113:3309-3319(2000).
RN [13]
RP FUNCTION, AND IDENTIFICATION IN THE PAN1 COMPLEX.
RX PubMed=10594004; DOI=10.1128/mcb.20.1.12-25.2000;
RA Tang H.-Y., Xu J., Cai M.;
RT "Pan1p, End3p, and Sla1p, three yeast proteins required for normal cortical
RT actin cytoskeleton organization, associate with each other and play
RT essential roles in cell wall morphogenesis.";
RL Mol. Cell. Biol. 20:12-25(2000).
RN [14]
RP IDENTIFICATION IN THE PAN1 COMPLEX, FUNCTION OF THE PAN1 COMPLEX,
RP SUBCELLULAR LOCATION, AND PHOSPHORYLATION BY PRK1.
RX PubMed=11739778; DOI=10.1091/mbc.12.12.3759;
RA Zeng G., Yu X., Cai M.;
RT "Regulation of yeast actin cytoskeleton-regulatory complex
RT Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p.";
RL Mol. Biol. Cell 12:3759-3772(2001).
RN [15]
RP FUNCTION.
RX PubMed=11957109; DOI=10.1007/s10142-001-0043-1;
RA Bidlingmaier S., Snyder M.A.;
RT "Large-scale identification of genes important for apical growth in
RT Saccharomyces cerevisiae by directed allele replacement technology (DART)
RT screening.";
RL Funct. Integr. Genomics 1:345-356(2002).
RN [16]
RP SUBCELLULAR LOCATION.
RX PubMed=14622601; DOI=10.1016/s0092-8674(03)00883-3;
RA Kaksonen M., Sun Y., Drubin D.G.;
RT "A pathway for association of receptors, adaptors, and actin during
RT endocytic internalization.";
RL Cell 115:475-487(2003).
RN [17]
RP INTERACTION WITH ENT1.
RX PubMed=12529323; DOI=10.1074/jbc.m211622200;
RA Aguilar R.C., Watson H.A., Wendland B.;
RT "The yeast Epsin Ent1 is recruited to membranes through multiple
RT independent interactions.";
RL J. Biol. Chem. 278:10737-10743(2003).
RN [18]
RP FUNCTION, SUBCELLULAR LOCATION, DOMAINS, AND SUBUNIT.
RX PubMed=15522098; DOI=10.1111/j.1600-0854.2004.00238.x;
RA Miliaras N.B., Park J.-H., Wendland B.;
RT "The function of the endocytic scaffold protein Pan1p depends on multiple
RT domains.";
RL Traffic 5:963-978(2004).
RN [19]
RP FUNCTION.
RX PubMed=16171804; DOI=10.1016/j.yexcr.2005.08.018;
RA Kaminska J., Wysocka-Kapcinska M., Smaczynska-de Rooij I., Rytka J.,
RA Zoladek T.;
RT "Pan1p, an actin cytoskeleton-associated protein, is required for growth of
RT yeast on oleate medium.";
RL Exp. Cell Res. 310:482-492(2005).
RN [20]
RP FUNCTION.
RX PubMed=16183906; DOI=10.1534/genetics.105.040634;
RA D'Agostino J.L., Goode B.L.;
RT "Dissection of Arp2/3 complex actin nucleation mechanism and distinct roles
RT for its nucleation-promoting factors in Saccharomyces cerevisiae.";
RL Genetics 171:35-47(2005).
RN [21]
RP INTERACTION WITH SPA2, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16030260; DOI=10.1091/mbc.e05-02-0108;
RA Shih J.L., Reck-Peterson S.L., Newitt R., Mooseker M.S., Aebersold R.,
RA Herskowitz I.;
RT "Cell polarity protein Spa2P associates with proteins involved in actin
RT function in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 16:4595-4608(2005).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-995; SER-1003 AND SER-1281,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ADR376;
RX PubMed=17330950; DOI=10.1021/pr060559j;
RA Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
RA Elias J.E., Gygi S.P.;
RT "Large-scale phosphorylation analysis of alpha-factor-arrested
RT Saccharomyces cerevisiae.";
RL J. Proteome Res. 6:1190-1197(2007).
RN [23]
RP IDENTIFICATION IN THE PAN1 COMPLEX, INTERACTION WITH SLA2, AND FUNCTION.
RX PubMed=17151356; DOI=10.1091/mbc.e06-09-0788;
RA Toshima J., Toshima J.Y., Duncan M.C., Cope M.J.T.V., Sun Y., Martin A.C.,
RA Anderson S., Yates J.R. III, Mizuno K., Drubin D.G.;
RT "Negative regulation of yeast Eps15-like Arp2/3 complex activator, Pan1p,
RT by the Hip1R-related protein, Sla2p, during endocytosis.";
RL Mol. Biol. Cell 18:658-668(2007).
RN [24]
RP INTERACTION WITH SCD5.
RX PubMed=17898076; DOI=10.1091/mbc.e07-06-0607;
RA Zeng G., Huang B., Neo S.P., Wang J., Cai M.;
RT "Scd5p mediates phosphoregulation of actin and endocytosis by the type 1
RT phosphatase Glc7p in yeast.";
RL Mol. Biol. Cell 18:4885-4898(2007).
RN [25]
RP PHOSPHORYLATION BY ARK1.
RX PubMed=17978096; DOI=10.1091/mbc.e07-06-0530;
RA Jin M., Cai M.;
RT "A novel function of Arp2p in mediating Prk1p-specific regulation of actin
RT and endocytosis in yeast.";
RL Mol. Biol. Cell 19:297-307(2008).
RN [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-241; THR-570; SER-747;
RP SER-757; THR-995; SER-1250 AND THR-1321, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=18407956; DOI=10.1074/mcp.m700468-mcp200;
RA Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
RT "A multidimensional chromatography technology for in-depth phosphoproteome
RT analysis.";
RL Mol. Cell. Proteomics 7:1389-1396(2008).
RN [27]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-570; SER-757; THR-993;
RP THR-995; SER-1003; SER-1180; SER-1250; SER-1253 AND SER-1281, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19779198; DOI=10.1126/science.1172867;
RA Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
RT "Global analysis of Cdk1 substrate phosphorylation sites provides insights
RT into evolution.";
RL Science 325:1682-1686(2009).
CC -!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory complex
CC required for the internalization of endosomes during actin-coupled
CC endocytosis. The complex links the site of endocytosis to the cell
CC membrane-associated actin cytoskeleton. Mediates uptake of external
CC molecules and vacuolar degradation of plasma membrane proteins. Plays a
CC role in the proper organization of the cell membrane-associated actin
CC cytoskeleton and promotes its destabilization. Required for the bipolar
CC budding of diploid cells and the correct distribution of chitin at the
CC cell surface. {ECO:0000269|PubMed:10594004,
CC ECO:0000269|PubMed:10954428, ECO:0000269|PubMed:11739778,
CC ECO:0000269|PubMed:11957109, ECO:0000269|PubMed:15522098,
CC ECO:0000269|PubMed:16171804, ECO:0000269|PubMed:16183906,
CC ECO:0000269|PubMed:17151356, ECO:0000269|PubMed:8524255,
CC ECO:0000269|PubMed:8756649, ECO:0000269|PubMed:8978817,
CC ECO:0000269|PubMed:9234686, ECO:0000269|PubMed:9531549}.
CC -!- SUBUNIT: Forms homooligomers. Component of the PAN1 actin cytoskeleton-
CC regulatory complex composed of at least END3, PAN1, and SLA1. Interacts
CC directly with END3, and with ENT1, SCD5, SLA2, YAP1801 and YAP1802.
CC {ECO:0000269|PubMed:10594004, ECO:0000269|PubMed:11739778,
CC ECO:0000269|PubMed:12529323, ECO:0000269|PubMed:15522098,
CC ECO:0000269|PubMed:16030260, ECO:0000269|PubMed:17151356,
CC ECO:0000269|PubMed:17898076, ECO:0000269|PubMed:9234686,
CC ECO:0000269|PubMed:9531549, ECO:0000269|PubMed:9885245}.
CC -!- INTERACTION:
CC P32521; P39013: END3; NbExp=9; IntAct=EBI-12875, EBI-6460;
CC P32521; Q04439: MYO5; NbExp=2; IntAct=EBI-12875, EBI-11687;
CC P32521; P32790: SLA1; NbExp=5; IntAct=EBI-12875, EBI-17313;
CC P32521; P38856: YAP1801; NbExp=4; IntAct=EBI-12875, EBI-24811;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein;
CC Cytoplasmic side. Endosome membrane; Peripheral membrane protein;
CC Cytoplasmic side. Cytoplasm, cytoskeleton, actin patch.
CC Note=Cytoplasmic and cortical actin patches.
CC -!- PTM: The N-terminus is blocked.
CC -!- PTM: Phosphorylated by PRK1 on threonine residues in the L-x-x-Q-x-T-G
CC motif of repeats 1-6 to 1-15 (PubMed:9885245, PubMed:11739778,
CC PubMed:17978096). Phosphorylated by ARK1 (PubMed:17978096).
CC {ECO:0000269|PubMed:11739778, ECO:0000269|PubMed:17978096,
CC ECO:0000269|PubMed:9885245}.
CC -!- SIMILARITY: Belongs to the PAN1 family. {ECO:0000305}.
CC -!- CAUTION: Was originally thought to be a subunit of PAB-dependent
CC poly(A)-specific ribonuclease. {ECO:0000305|PubMed:1339314}.
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DR EMBL; Z38062; CAA86208.1; -; Genomic_DNA.
DR EMBL; X79743; CAB38097.1; -; Genomic_DNA.
DR EMBL; M90688; AAA34841.1; -; Genomic_DNA.
DR EMBL; BK006942; DAA08552.1; -; Genomic_DNA.
DR PIR; S48440; S48440.
DR RefSeq; NP_012271.3; NM_001179528.3.
DR AlphaFoldDB; P32521; -.
DR SMR; P32521; -.
DR BioGRID; 34997; 651.
DR ComplexPortal; CPX-426; PAN1 actin cytoskeleton-regulatory complex.
DR DIP; DIP-1340N; -.
DR IntAct; P32521; 22.
DR MINT; P32521; -.
DR STRING; 4932.YIR006C; -.
DR iPTMnet; P32521; -.
DR MaxQB; P32521; -.
DR PaxDb; P32521; -.
DR PRIDE; P32521; -.
DR TopDownProteomics; P32521; -.
DR EnsemblFungi; YIR006C_mRNA; YIR006C; YIR006C.
DR GeneID; 854822; -.
DR KEGG; sce:YIR006C; -.
DR SGD; S000001445; PAN1.
DR VEuPathDB; FungiDB:YIR006C; -.
DR eggNOG; KOG0998; Eukaryota.
DR HOGENOM; CLU_006042_0_0_1; -.
DR InParanoid; P32521; -.
DR OMA; PQRTGMQ; -.
DR BioCyc; YEAST:G3O-31427-MON; -.
DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-SCE-9013420; RHOU GTPase cycle.
DR PRO; PR:P32521; -.
DR Proteomes; UP000002311; Chromosome IX.
DR RNAct; P32521; protein.
DR GO; GO:0030479; C:actin cortical patch; IDA:SGD.
DR GO; GO:1990964; C:actin cytoskeleton-regulatory complex; IDA:SGD.
DR GO; GO:0005935; C:cellular bud neck; HDA:SGD.
DR GO; GO:0005737; C:cytoplasm; IDA:SGD.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0043332; C:mating projection tip; HDA:SGD.
DR GO; GO:0005634; C:nucleus; IDA:SGD.
DR GO; GO:0005886; C:plasma membrane; HDA:SGD.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0071933; F:Arp2/3 complex binding; IDA:SGD.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0000147; P:actin cortical patch assembly; IMP:SGD.
DR GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR GO; GO:0007120; P:axial cellular bud site selection; IMP:SGD.
DR GO; GO:0007121; P:bipolar cellular bud site selection; IMP:SGD.
DR GO; GO:0071555; P:cell wall organization; IMP:ComplexPortal.
DR GO; GO:0006897; P:endocytosis; IMP:SGD.
DR GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR GO; GO:2000601; P:positive regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
DR CDD; cd00052; EH; 2.
DR DisProt; DP02220; -.
DR InterPro; IPR013182; DUF1720.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR000261; EH_dom.
DR Pfam; PF08226; DUF1720; 3.
DR Pfam; PF12763; EF-hand_4; 2.
DR SMART; SM00054; EFh; 3.
DR SMART; SM00027; EH; 2.
DR SUPFAM; SSF47473; SSF47473; 2.
DR PROSITE; PS50222; EF_HAND_2; 3.
DR PROSITE; PS50031; EH; 2.
PE 1: Evidence at protein level;
KW Actin-binding; Calcium; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoskeleton; Direct protein sequencing; Endocytosis; Endosome; Membrane;
KW Metal-binding; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1480
FT /note="Actin cytoskeleton-regulatory complex protein PAN1"
FT /id="PRO_0000058221"
FT REPEAT 142..153
FT /note="1-1"
FT REPEAT 164..175
FT /note="1-2"
FT REPEAT 188..199
FT /note="1-3"
FT REPEAT 215..226
FT /note="1-4"
FT REPEAT 235..246
FT /note="1-5"
FT DOMAIN 269..304
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 270..359
FT /note="EH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 306..338
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 328..350
FT /note="2-1"
FT REPEAT 392..403
FT /note="1-6"
FT REPEAT 409..420
FT /note="1-7"
FT REPEAT 422..433
FT /note="1-8"
FT REPEAT 446..457
FT /note="1-9"
FT REPEAT 467..478
FT /note="1-10"
FT REPEAT 498..509
FT /note="1-11"
FT REPEAT 510..518
FT /note="1-12"
FT REPEAT 538..548
FT /note="1-13"
FT REPEAT 549..556
FT /note="1-14"
FT REPEAT 564..575
FT /note="1-15"
FT DOMAIN 600..689
FT /note="EH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00077"
FT DOMAIN 633..668
FT /note="EF-hand 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT REPEAT 658..680
FT /note="2-2"
FT REPEAT 1084..1089
FT /note="3-1"
FT REPEAT 1090..1095
FT /note="3-2"
FT REPEAT 1096..1101
FT /note="3-3"
FT REPEAT 1102..1107
FT /note="3-4"
FT REPEAT 1108..1113
FT /note="3-5"
FT REPEAT 1114..1119
FT /note="3-6"
FT REPEAT 1120..1125
FT /note="3-7"
FT REPEAT 1315..1320
FT /note="4-1"
FT REPEAT 1321..1326
FT /note="4-2"
FT REPEAT 1327..1332
FT /note="4-3"
FT REPEAT 1340..1345
FT /note="4-4"
FT REPEAT 1346..1350
FT /note="4-5"
FT REPEAT 1355..1360
FT /note="4-6"
FT REPEAT 1361..1366
FT /note="4-7"
FT REPEAT 1372..1377
FT /note="4-8"
FT REGION 1..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 142..575
FT /note="15 X 12 AA tandem repeats of [SPNAG]-[IL]-[QKNGT]-
FT [PSA]-[QT]-[GQAPISTLYK]-T-G-[YFGML]-[YVMGAQL]-[QVLNPAG]-
FT [ASQPN]"
FT REGION 185..214
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 328..680
FT /note="2 X 23 AA repeats of F-A-L-[AG]-M-H-L-[IV]-[NY]-
FT [DG]-[VK]-L-[QN]-G-[DK]-[TP]-I-P-[YN]-[EV]-L-[DP]-S"
FT REGION 737..766
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 888..909
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 977..1147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1084..1125
FT /note="7 X 6 AA tandem repeats of Q-[PS]-T-Q-P-V"
FT REGION 1169..1480
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1315..1377
FT /note="8 X 6 AA repeats of [ATVSP]-P-[LVI]-P-[SPQILA]-
FT [VAS]"
FT COILED 1131..1190
FT /evidence="ECO:0000255"
FT COMPBIAS 1..126
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 740..766
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 977..1010
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1014..1040
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1041..1070
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1098
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1119
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1169..1189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1205..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1230..1260
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1284..1305
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1315..1329
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1342..1371
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 646
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 648
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 650
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 652
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT BINDING 657
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT MOD_RES 241
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 570
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT MOD_RES 757
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 993
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 995
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:18407956, ECO:0007744|PubMed:19779198"
FT MOD_RES 1003
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1250
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18407956,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1253
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19779198"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17330950,
FT ECO:0007744|PubMed:19779198"
FT MOD_RES 1321
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18407956"
FT CONFLICT 235
FT /note="P -> T (in Ref. 1; AAA34841)"
FT /evidence="ECO:0000305"
FT CONFLICT 266..273
FT /note="ITAQDQAK -> YYCPRSGKN (in Ref. 1; AAA34841)"
FT /evidence="ECO:0000305"
FT CONFLICT 474..487
FT /note="Missing (in Ref. 1; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 653..657
FT /note="Missing (in Ref. 1; AAA34841)"
FT /evidence="ECO:0000305"
FT CONFLICT 1291
FT /note="A -> R (in Ref. 1; AAA34841)"
FT /evidence="ECO:0000305"
FT CONFLICT 1396..1480
FT /note="GGVLPPPPPLPTQQASTSEPIIAHVDNYNGAEKGTGAYGSDSDDDVLSIPES
FT VGTDEEEEGAQPVSTAGIPSIPPAGIPPPPPLP -> EAFCLHPHLYQLNKLPLQNLLS
FT LTLITTMVLKKARAHMDPILMMTFYRFLNQLVQMKRKKGHNQFLLQVSHQFHLQVFLHP
FT HPFHEDLICFL (in Ref. 1; AAA34841)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1480 AA; 160267 MW; F3518495FF759553 CRC64;
MYNPYQQQGM GYQQQQQQQQ QQPNGFYPQQ QQGQSSNQPQ GQPQPQQQMA FNQPQATGIG
GMPQSFGNSF SSMPQQPQTG YNNNGNNGSV YGNGNFGQQP QQQQQQAKPQ HTGYVPNSSM
PMMNTTGTMP PPNPAQQPQL QSIQPQGTGY YQAANTANVH SVQPLQSQGT GYYVSTPNLI
SSNQTQQPLQ AQGTGYYQSQ PQQVPPPQQA QSLQPLKPQQ TGFYLQPQNQ APLEPLKPTA
TGFVNSFANN GLNNDIKIPA IRLSFITAQD QAKFETLFRS IVTNGSNTVS GANCRKILMR
SGLPPSQLAR IWTLCDTSKA GELLFPEFAL AMHLINDVLQ GDTIPYELDS KTKNEVSSFI
DAINLSIANQ DSSANDAPKT PFDEFITAGV QNLQPQPTGY MPQTSFGIPL QSQITGGGVA
SALNPQSTGF MAPTTFNMSM NTGTPGLNPQ ITGGAPASMQ PNITGNALQP QTTGMMPQTT
GMMPQTTGMM PQTSFGVNLG PQLTGGALQS QYTGGYGSVM PQQSGPASMP NLSFNQQGLQ
SQLTGLQPQP TGFLPPSNFS ATMPLTAQKT GFGNNEIYTK SNFNNNLIDN SSQDKISTEE
KSLFYKIFET FDTQNKGLLD SPTAVEIFRK SGLNRADLEQ IWNLCDINNT GQLNKQEFAL
GMHLVYGKLN GKPIPNVLPS SLIPSSTKLL DNLKNQLKTE PTTTKEKPSF GKIDALSYKN
NDDDVLPNYR NRRKVYSAKN EEQSSFSSPS AKSVNHSSST LQTDDISVDK TVEKKTAKPK
YAGFSREINL KNIASLENEI KNISNPENCY DSSIPSDLTS RFDAIIAKLP NLFNEISTID
NEITNAKIQL YRKKNPSSII GSGPNGEITE NDRKKAKSRA LLRARMSALT GKSTESEDSL
SMEDEQQSAE IKRIQQENGK NQEIIKDIRS SISDISASLK STMTGSNMIS NQEFERWEFG
IGLEDGVREF LDDLKSNSNK SVTESSPFVP SSTPTPVDDR SSSPSYSQFK TAEERAAYLK
EQAKKRMKEK LAKFDKNRRN VTQSSRSISS ENSREQPQQI AGSSNLVEPR ATPFQEEKYV
EVAQPTQPVQ STQPVQPTQP VQPTQPVQPT QPVQPTQPVQ PTQPVQNVYN AKQESDDEDE
DDEEKRLQEE LKRLKLKKKA DKEKRLAALR KQIEDAQNES DEEETNGKDN FGGHVNVPQA
APVAPSAAFS QNSTNAPRSV HAAVTPAAGK NSTGLPSTTM GHNPYFKDAS ASSTSTFDAR
AAEMQRRIQR GLDEDEDDGW SDEDESNNRV AVDNKVEEAK IGHPDHARAP PVTAAPLPSV
TPVPPAVPVP QANTSNEKSS PIPIAPIPPS VTQEPPVPLA PPLPAVDGFQ EPPIPSAPAI
ATAVQKSGSS TPALAGGVLP PPPPLPTQQA STSEPIIAHV DNYNGAEKGT GAYGSDSDDD
VLSIPESVGT DEEEEGAQPV STAGIPSIPP AGIPPPPPLP
