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 27-MAR-2024, entry version 205. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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; 661. 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 GlyGen; P32521; 18 sites, 1 O-linked glycan (18 sites). DR iPTMnet; P32521; -. DR MaxQB; P32521; -. DR PaxDb; 4932-YIR006C; -. DR PeptideAtlas; P32521; -. DR TopDownProteomics; P32521; -. DR EnsemblFungi; YIR006C_mRNA; YIR006C; YIR006C. DR GeneID; 854822; -. DR KEGG; sce:YIR006C; -. DR AGR; SGD:S000001445; -. 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 OrthoDB; 2734911at2759; -. DR BioCyc; YEAST:G3O-31427-MONOMER; -. DR Reactome; R-SCE-8856825; Cargo recognition for clathrin-mediated endocytosis. DR Reactome; R-SCE-8856828; Clathrin-mediated endocytosis. DR BioGRID-ORCS; 854822; 10 hits in 10 CRISPR screens. 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: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 Gene3D; 1.10.238.10; EF-hand; 2. 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 PANTHER; PTHR11216:SF177; ACTIN CYTOSKELETON-REGULATORY COMPLEX PROTEIN PAN1; 1. DR PANTHER; PTHR11216; EH DOMAIN; 1. DR Pfam; PF08226; DUF1720; 4. DR Pfam; PF12763; EF-hand_4; 2. DR SMART; SM00054; EFh; 3. DR SMART; SM00027; EH; 2. DR SUPFAM; SSF47473; EF-hand; 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 //