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Actin cytoskeleton-regulatory complex protein SLA1

 SLA1_YEAST              Reviewed;        1244 AA.
P32790; D6VPZ3;
01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
01-OCT-1993, sequence version 1.
20-DEC-2017, entry version 181.
RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1;
Name=SLA1; OrderedLocusNames=YBL007C; ORFNames=YBL0321;
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Saccharomyces.
NCBI_TaxID=559292;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
STRAIN=DDY 228;
PubMed=8335689; DOI=10.1083/jcb.122.3.635;
Holtzman D.A., Yang S., Drubin D.G.;
"Synthetic-lethal interactions identify two novel genes, SLA1 and
SLA2, that control membrane cytoskeleton assembly in Saccharomyces
cerevisiae.";
J. Cell Biol. 122:635-644(1993).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=1441753; DOI=10.1002/yea.320080909;
Delaveau T., Jacq C., Perea J.;
"Sequence of a 12.7 kb segment of yeast chromosome II identifies a
PDR-like gene and several new open reading frames.";
Yeast 8:761-768(1992).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC 204508 / S288c;
PubMed=7813418;
Feldmann H., Aigle M., Aljinovic G., Andre B., Baclet M.C., Barthe C.,
Baur A., Becam A.-M., Biteau N., Boles E., Brandt T., Brendel M.,
Brueckner M., Bussereau F., Christiansen C., Contreras R., Crouzet M.,
Cziepluch C., Demolis N., Delaveau T., Doignon F., Domdey H.,
Duesterhus S., Dubois E., Dujon B., El Bakkoury M., Entian K.-D.,
Feuermann M., Fiers W., Fobo G.M., Fritz C., Gassenhuber J.,
Glansdorff N., Goffeau A., Grivell L.A., de Haan M., Hein C.,
Herbert C.J., Hollenberg C.P., Holmstroem K., Jacq C., Jacquet M.,
Jauniaux J.-C., Jonniaux J.-L., Kallesoee T., Kiesau P., Kirchrath L.,
Koetter P., Korol S., Liebl S., Logghe M., Lohan A.J.E., Louis E.J.,
Li Z.Y., Maat M.J., Mallet L., Mannhaupt G., Messenguy F., Miosga T.,
Molemans F., Mueller S., Nasr F., Obermaier B., Perea J., Pierard A.,
Piravandi E., Pohl F.M., Pohl T.M., Potier S., Proft M., Purnelle B.,
Ramezani Rad M., Rieger M., Rose M., Schaaff-Gerstenschlaeger I.,
Scherens B., Schwarzlose C., Skala J., Slonimski P.P., Smits P.H.M.,
Souciet J.-L., Steensma H.Y., Stucka R., Urrestarazu L.A.,
van der Aart Q.J.M., Van Dyck L., Vassarotti A., Vetter I.,
Vierendeels F., Vissers S., Wagner G., de Wergifosse P., Wolfe K.H.,
Zagulski M., Zimmermann F.K., Mewes H.-W., Kleine K.;
"Complete DNA sequence of yeast chromosome II.";
EMBO J. 13:5795-5809(1994).
[4]
GENOME REANNOTATION.
STRAIN=ATCC 204508 / S288c;
PubMed=24374639; DOI=10.1534/g3.113.008995;
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M.,
Cherry J.M.;
"The reference genome sequence of Saccharomyces cerevisiae: Then and
now.";
G3 (Bethesda) 4:389-398(2014).
[5]
FUNCTION.
PubMed=8756649; DOI=10.1128/MCB.16.9.4897;
Tang H.-Y., Cai M.;
"The EH-domain-containing protein Pan1 is required for normal
organization of the actin cytoskeleton in Saccharomyces cerevisiae.";
Mol. Cell. Biol. 16:4897-4914(1996).
[6]
FUNCTION.
PubMed=9008707; DOI=10.1083/jcb.136.1.111;
Yang S., Ayscough K.R., Drubin D.G.;
"A role for the actin cytoskeleton of Saccharomyces cerevisiae in
bipolar bud-site selection.";
J. Cell Biol. 136:111-123(1997).
[7]
INTERACTION WITH LAS17.
PubMed=9024694; DOI=10.1083/jcb.136.3.649;
Li R.;
"Bee1, a yeast protein with homology to Wiscott-Aldrich syndrome
protein, is critical for the assembly of cortical actin
cytoskeleton.";
J. Cell Biol. 136:649-658(1997).
[8]
FUNCTION.
PubMed=9128251; DOI=10.1083/jcb.137.2.399;
Ayscough K.R., Stryker J., Pokala N., Sanders M., Crews P.,
Drubin D.G.;
"High rates of actin filament turnover in budding yeast and roles for
actin in establishment and maintenance of cell polarity revealed using
the actin inhibitor latrunculin-A.";
J. Cell Biol. 137:399-416(1997).
[9]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=10198057; DOI=10.1091/mbc.10.4.1061;
Ayscough K.R., Eby J.J., Lila T., Dewar H., Kozminski K.G.,
Drubin D.G.;
"Sla1p is a functionally modular component of the yeast cortical actin
cytoskeleton required for correct localization of both Rho1p-GTPase
and Sla2p, a protein with talin homology.";
Mol. Biol. Cell 10:1061-1075(1999).
[10]
FUNCTION, AND IDENTIFICATION IN THE PAN1 COMPLEX.
PubMed=10594004; DOI=10.1128/MCB.20.1.12-25.2000;
Tang H.-Y., Xu J., Cai M.;
"Pan1p, End3p, and Sla1p, three yeast proteins required for normal
cortical actin cytoskeleton organization, associate with each other
and play essential roles in cell wall morphogenesis.";
Mol. Cell. Biol. 20:12-25(2000).
[11]
IDENTIFICATION IN THE PAN1 COMPLEX, PHOSPHORYLATION BY PRK1, AND
SUBCELLULAR LOCATION.
PubMed=11739778; DOI=10.1091/mbc.12.12.3759;
Zeng G., Yu X., Cai M.;
"Regulation of yeast actin cytoskeleton-regulatory complex
Pan1p/Sla1p/End3p by serine/threonine kinase Prk1p.";
Mol. Biol. Cell 12:3759-3772(2001).
[12]
FUNCTION.
PubMed=11940605; DOI=10.1083/jcb.200110027;
Howard J.P., Hutton J.L., Olson J.M., Payne G.S.;
"Sla1p serves as the targeting signal recognition factor for
NPFX(1,2)D-mediated endocytosis.";
J. Cell Biol. 157:315-326(2002).
[13]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH ABP1 AND LAS17.
PubMed=11950888;
Warren D.T., Andrews P.D., Gourlay C.W., Ayscough K.R.;
"Sla1p couples the yeast endocytic machinery to proteins regulating
actin dynamics.";
J. Cell Sci. 115:1703-1715(2002).
[14]
FUNCTION, AND INTERACTION WITH LSB5 AND YSC84.
PubMed=12388763; DOI=10.1091/mbc.E02-05-0262;
Dewar H., Warren D.T., Gardiner F.C., Gourlay C.G., Satish N.,
Richardson M.R., Andrews P.D., Ayscough K.R.;
"Novel proteins linking the actin cytoskeleton to the endocytic
machinery in Saccharomyces cerevisiae.";
Mol. Biol. Cell 13:3646-3661(2002).
[15]
FUNCTION, AND INTERACTION WITH KRE6.
PubMed=12237851; DOI=10.1002/yea.904;
Li H., Page N., Bussey H.;
"Actin patch assembly proteins Las17p and Sla1p restrict cell wall
growth to daughter cells and interact with cis-Golgi protein Kre6p.";
Yeast 19:1097-1112(2002).
[16]
FUNCTION.
PubMed=12814545; DOI=10.1016/S0960-9822(03)00383-X;
Rodal A.A., Manning A.L., Goode B.L., Drubin D.G.;
"Negative regulation of yeast WASp by two SH3 domain-containing
proteins.";
Curr. Biol. 13:1000-1008(2003).
[17]
FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH SLA2.
PubMed=12734398; DOI=10.1242/jcs.00454;
Gourlay C.W., Dewar H., Warren D.T., Costa R., Satish N.,
Ayscough K.R.;
"An interaction between Sla1p and Sla2p plays a role in regulating
actin dynamics and endocytosis in budding yeast.";
J. Cell Sci. 116:2551-2564(2003).
[18]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=14562095; DOI=10.1038/nature02026;
Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
Weissman J.S., O'Shea E.K.;
"Global analysis of protein localization in budding yeast.";
Nature 425:686-691(2003).
[19]
LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
PubMed=14562106; DOI=10.1038/nature02046;
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
Dephoure N., O'Shea E.K., Weissman J.S.;
"Global analysis of protein expression in yeast.";
Nature 425:737-741(2003).
[20]
FUNCTION, AND INTERACTION WITH RSP5 AND RVS167.
PubMed=14761940; DOI=10.1074/jbc.M313479200;
Stamenova S.D., Dunn R., Adler A.S., Hicke L.;
"The Rsp5 ubiquitin ligase binds to and ubiquitinates members of the
yeast CIN85-endophilin complex, Sla1-Rvs167.";
J. Biol. Chem. 279:16017-16025(2004).
[21]
INTERACTION WITH LSB5.
PubMed=15651983; DOI=10.1042/BJ20041729;
Costa R., Warren D.T., Ayscough K.R.;
"Lsb5p interacts with actin regulators Sla1p and Las17p, ubiquitin and
Arf3p to couple actin dynamics to membrane trafficking processes.";
Biochem. J. 387:649-658(2005).
[22]
INTERACTION WITH VPS1.
PubMed=15265985; DOI=10.1242/jcs.01239;
Yu X., Cai M.;
"The yeast dynamin-related GTPase Vps1p functions in the organization
of the actin cytoskeleton via interaction with Sla1p.";
J. Cell Sci. 117:3839-3853(2004).
[23]
FUNCTION.
PubMed=15525671; DOI=10.1091/mbc.E04-08-0734;
Rodal A.A., Kozubowski L., Goode B.L., Drubin D.G., Hartwig J.H.;
"Actin and septin ultrastructures at the budding yeast cell cortex.";
Mol. Biol. Cell 16:372-384(2005).
[24]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
STRAIN=ADR376;
PubMed=17330950; DOI=10.1021/pr060559j;
Li X., Gerber S.A., Rudner A.D., Beausoleil S.A., Haas W., Villen J.,
Elias J.E., Gygi S.P.;
"Large-scale phosphorylation analysis of alpha-factor-arrested
Saccharomyces cerevisiae.";
J. Proteome Res. 6:1190-1197(2007).
[25]
SUBCELLULAR LOCATION, AND FUNCTION.
PubMed=17286805; DOI=10.1111/j.1600-0854.2007.00534.x;
Gardiner F.C., Costa R., Ayscough K.R.;
"Nucleocytoplasmic trafficking is required for functioning of the
adaptor protein Sla1p in endocytosis.";
Traffic 8:347-358(2007).
[26]
PHOSPHORYLATION BY ARK1.
PubMed=17978096; DOI=10.1091/mbc.E07-06-0530;
Jin M., Cai M.;
"A novel function of Arp2p in mediating Prk1p-specific regulation of
actin and endocytosis in yeast.";
Mol. Biol. Cell 19:297-307(2008).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799; THR-831; THR-858;
THR-887; THR-904; THR-984 AND SER-996, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=18407956; DOI=10.1074/mcp.M700468-MCP200;
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
"A multidimensional chromatography technology for in-depth
phosphoproteome analysis.";
Mol. Cell. Proteomics 7:1389-1396(2008).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-447; SER-449; SER-454;
THR-887; THR-904; THR-984; THR-993; SER-996 AND THR-1075, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19779198; DOI=10.1126/science.1172867;
Holt L.J., Tuch B.B., Villen J., Johnson A.D., Gygi S.P., Morgan D.O.;
"Global analysis of Cdk1 substrate phosphorylation sites provides
insights into evolution.";
Science 325:1682-1686(2009).
[29]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[30]
UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-471 AND LYS-548, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22106047; DOI=10.1002/pmic.201100166;
Starita L.M., Lo R.S., Eng J.K., von Haller P.D., Fields S.;
"Sites of ubiquitin attachment in Saccharomyces cerevisiae.";
Proteomics 12:236-240(2012).
[31]
STRUCTURE BY NMR OF 495-560, AND DOMAIN.
PubMed=17363896; DOI=10.1038/sj.emboj.7601646;
Mahadev R.K., Di Pietro S.M., Olson J.M., Piao H.L., Payne G.S.,
Overduin M.;
"Structure of Sla1p homology domain 1 and interaction with the NPFxD
endocytic internalization motif.";
EMBO J. 26:1963-1971(2007).
[32]
STRUCTURE BY NMR OF 350-420, AND DOMAIN.
PubMed=17765920; DOI=10.1016/j.jmb.2007.07.074;
He Y., Hicke L., Radhakrishnan I.;
"Structural basis for ubiquitin recognition by SH3 domains.";
J. Mol. Biol. 373:190-196(2007).
-!- FUNCTION: Component of the PAN1 actin cytoskeleton-regulatory
complex required for the internalization of endosomes during
actin-coupled endocytosis. The complex links the site of
endocytosis to the cell membrane-associated actin cytoskeleton.
Mediates uptake of external molecules and vacuolar degradation of
plasma membrane proteins. Plays a role in the proper organization
of the cell membrane-associated actin cytoskeleton and promotes
its destabilization. {ECO:0000269|PubMed:10198057,
ECO:0000269|PubMed:10594004, ECO:0000269|PubMed:11940605,
ECO:0000269|PubMed:11950888, ECO:0000269|PubMed:12237851,
ECO:0000269|PubMed:12388763, ECO:0000269|PubMed:12734398,
ECO:0000269|PubMed:12814545, ECO:0000269|PubMed:14761940,
ECO:0000269|PubMed:15525671, ECO:0000269|PubMed:17286805,
ECO:0000269|PubMed:8335689, ECO:0000269|PubMed:8756649,
ECO:0000269|PubMed:9008707, ECO:0000269|PubMed:9128251}.
-!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory
complex. Interacts with ABP1, KRE6, LAS17, LSB5, RSP5, RVS167,
VPS1 and YSC84. {ECO:0000269|PubMed:10594004,
ECO:0000269|PubMed:11739778, ECO:0000269|PubMed:11950888,
ECO:0000269|PubMed:12237851, ECO:0000269|PubMed:12388763,
ECO:0000269|PubMed:12734398, ECO:0000269|PubMed:14761940,
ECO:0000269|PubMed:15265985, ECO:0000269|PubMed:15651983,
ECO:0000269|PubMed:9024694}.
-!- INTERACTION:
Self; NbExp=10; IntAct=EBI-17313, EBI-17313;
P15891:ABP1; NbExp=4; IntAct=EBI-17313, EBI-2036;
P40563:AIM21; NbExp=4; IntAct=EBI-17313, EBI-25376;
P53933:APP1; NbExp=4; IntAct=EBI-17313, EBI-28798;
Q06604:BSP1; NbExp=5; IntAct=EBI-17313, EBI-37047;
P22137:CHC1; NbExp=4; IntAct=EBI-17313, EBI-4766;
P32525:ECM25; NbExp=4; IntAct=EBI-17313, EBI-26215;
P39013:END3; NbExp=4; IntAct=EBI-17313, EBI-6460;
P13134:KEX2; NbExp=16; IntAct=EBI-17313, EBI-9658;
Q12446:LAS17; NbExp=7; IntAct=EBI-17313, EBI-10022;
P43603:LSB3; NbExp=7; IntAct=EBI-17313, EBI-22980;
P25369:LSB5; NbExp=5; IntAct=EBI-17313, EBI-10218;
P54199:MPS1; NbExp=2; IntAct=EBI-17313, EBI-11224;
P32521:PAN1; NbExp=5; IntAct=EBI-17313, EBI-12875;
P25368:RRP7; NbExp=3; IntAct=EBI-17313, EBI-16019;
Q02794:STD1; NbExp=3; IntAct=EBI-17313, EBI-18344;
P32793:YSC84; NbExp=7; IntAct=EBI-17313, EBI-24460;
P54786:ZDS2; NbExp=3; IntAct=EBI-17313, EBI-29637;
-!- SUBCELLULAR LOCATION: Nucleus. Cell membrane; Peripheral membrane
protein; Cytoplasmic side. Endosome membrane; Peripheral membrane
protein; Cytoplasmic side. Cytoplasm, cytoskeleton, actin patch.
Note=Cytoplasmic and cortical actin patches. Is associated with
cortical actin patches in its dephosphorylated form and
dissociates upon phosphorylation by PRK1.
-!- PTM: Phosphorylated by PRK1. {ECO:0000269|PubMed:11739778,
ECO:0000269|PubMed:17978096}.
-!- MISCELLANEOUS: Present with 952 molecules/cell in log phase SD
medium. {ECO:0000269|PubMed:14562106}.
-!- SIMILARITY: Belongs to the SLA1 family. {ECO:0000305}.
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EMBL; Z22810; CAA80463.1; -; Genomic_DNA.
EMBL; Z35768; CAA84826.1; -; Genomic_DNA.
EMBL; S47695; AAB23985.1; -; Genomic_DNA.
EMBL; BK006936; DAA07113.1; -; Genomic_DNA.
PIR; S25327; S25327.
RefSeq; NP_009546.1; NM_001178247.1.
PDB; 1SSH; X-ray; 1.40 A; B=191-202.
PDB; 1Z9Z; X-ray; 1.95 A; A/B=357-413.
PDB; 2HBP; NMR; -; A=495-560.
PDB; 2JT4; NMR; -; A=350-420.
PDB; 2V1Q; X-ray; 1.20 A; A/B=357-413.
PDB; 3IDW; X-ray; 1.85 A; A=653-724.
PDBsum; 1SSH; -.
PDBsum; 1Z9Z; -.
PDBsum; 2HBP; -.
PDBsum; 2JT4; -.
PDBsum; 2V1Q; -.
PDBsum; 3IDW; -.
ProteinModelPortal; P32790; -.
SMR; P32790; -.
BioGrid; 32692; 679.
DIP; DIP-695N; -.
IntAct; P32790; 156.
MINT; MINT-410065; -.
STRING; 4932.YBL007C; -.
iPTMnet; P32790; -.
MaxQB; P32790; -.
PRIDE; P32790; -.
EnsemblFungi; YBL007C; YBL007C; YBL007C.
GeneID; 852276; -.
KEGG; sce:YBL007C; -.
EuPathDB; FungiDB:YBL007C; -.
SGD; S000000103; SLA1.
GeneTree; ENSGT00730000114400; -.
HOGENOM; HOG000157527; -.
InParanoid; P32790; -.
KO; K20046; -.
OMA; NTRKGRP; -.
OrthoDB; EOG092C14N7; -.
BioCyc; YEAST:G3O-28913-MONOMER; -.
EvolutionaryTrace; P32790; -.
PRO; PR:P32790; -.
Proteomes; UP000002311; Chromosome II.
GO; GO:0030479; C:actin cortical patch; IDA:SGD.
GO; GO:0005938; C:cell cortex; IDA:SGD.
GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; IDA:SGD.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
GO; GO:0098748; F:endocytic adaptor activity; IMP:SGD.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0043130; F:ubiquitin binding; IDA:SGD.
GO; GO:0000147; P:actin cortical patch assembly; IMP:SGD.
GO; GO:0007015; P:actin filament organization; IEA:InterPro.
GO; GO:0006897; P:endocytosis; IMP:SGD.
GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:SGD.
CDD; cd11773; SH3_Sla1p_1; 1.
CDD; cd11775; SH3_Sla1p_3; 1.
InterPro; IPR036028; SH3-like_dom_sf.
InterPro; IPR001452; SH3_domain.
InterPro; IPR007131; SHD1.
InterPro; IPR029922; Sla1.
InterPro; IPR035800; Sla1_SH3_1.
InterPro; IPR035821; Sla1_SH3_3.
PANTHER; PTHR11216:SF55; PTHR11216:SF55; 2.
Pfam; PF00018; SH3_1; 2.
Pfam; PF14604; SH3_9; 1.
Pfam; PF03983; SHD1; 1.
PRINTS; PR00452; SH3DOMAIN.
SMART; SM00326; SH3; 3.
SUPFAM; SSF50044; SSF50044; 3.
PROSITE; PS50002; SH3; 3.
1: Evidence at protein level;
3D-structure; Actin-binding; Cell membrane; Complete proteome;
Cytoplasm; Cytoskeleton; Endocytosis; Endosome; Isopeptide bond;
Membrane; Nucleus; Phosphoprotein; Reference proteome; Repeat;
SH3 domain; Ubl conjugation.
CHAIN 1 1244 Actin cytoskeleton-regulatory complex
protein SLA1.
/FTId=PRO_0000071943.
DOMAIN 3 68 SH3 1. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 69 132 SH3 2. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 353 415 SH3 3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
REPEAT 868 874 1.
REPEAT 877 883 2.
REPEAT 887 893 3.
REPEAT 923 929 4.
REPEAT 945 951 5.
REPEAT 1003 1009 6.
REPEAT 1020 1026 7.
REPEAT 1031 1037 8.
REPEAT 1048 1054 9.
REPEAT 1065 1071 10.
REPEAT 1084 1090 11.
REPEAT 1129 1135 12.
REPEAT 1155 1161 13.
REPEAT 1170 1176 14.
REPEAT 1185 1191 15.
REPEAT 1200 1206 16.
REGION 868 1205 16 X 7 AA approximate repeats of T-G-G-A-
M-M-P.
MOD_RES 447 447 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 449 449 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 454 454 Phosphoserine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 799 799 Phosphoserine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 831 831 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 858 858 Phosphothreonine.
{ECO:0000244|PubMed:18407956}.
MOD_RES 887 887 Phosphothreonine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 904 904 Phosphothreonine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 984 984 Phosphothreonine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 993 993 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
MOD_RES 996 996 Phosphoserine.
{ECO:0000244|PubMed:18407956,
ECO:0000244|PubMed:19779198}.
MOD_RES 1075 1075 Phosphothreonine.
{ECO:0000244|PubMed:19779198}.
CROSSLNK 471 471 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
CROSSLNK 548 548 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in ubiquitin).
{ECO:0000244|PubMed:22106047}.
STRAND 357 360 {ECO:0000244|PDB:2V1Q}.
STRAND 379 387 {ECO:0000244|PDB:2V1Q}.
STRAND 389 396 {ECO:0000244|PDB:2V1Q}.
TURN 397 399 {ECO:0000244|PDB:2V1Q}.
STRAND 402 406 {ECO:0000244|PDB:2V1Q}.
HELIX 407 409 {ECO:0000244|PDB:2V1Q}.
STRAND 410 412 {ECO:0000244|PDB:2V1Q}.
TURN 413 415 {ECO:0000244|PDB:2JT4}.
STRAND 497 505 {ECO:0000244|PDB:2HBP}.
STRAND 508 517 {ECO:0000244|PDB:2HBP}.
STRAND 520 524 {ECO:0000244|PDB:2HBP}.
STRAND 530 534 {ECO:0000244|PDB:2HBP}.
HELIX 540 550 {ECO:0000244|PDB:2HBP}.
HELIX 555 557 {ECO:0000244|PDB:2HBP}.
HELIX 657 663 {ECO:0000244|PDB:3IDW}.
HELIX 668 680 {ECO:0000244|PDB:3IDW}.
HELIX 685 690 {ECO:0000244|PDB:3IDW}.
HELIX 693 698 {ECO:0000244|PDB:3IDW}.
HELIX 703 716 {ECO:0000244|PDB:3IDW}.
SEQUENCE 1244 AA; 135848 MW; 7FD85AA776407624 CRC64;
MTVFLGIYRA VYAYEPQTPE ELAIQEDDLL YLLQKSDIDD WWTVKKRVIG SDSEEPVGLV
PSTYIEEAPV LKKVRAIYDY EQVQNADEEL TFHENDVFDV FDDKDADWLL VKSTVSNEFG
FIPGNYVEPE NGSTSKQEQA PAAAEAPAAT PAAAPASAAV LPTNFLPPPQ HNDRARMMQS
KEDQAPDEDE EGPPPAMPAR PTATTETTDA TAAAVRSRTR LSYSDNDNDD EEDDYYYNSN
SNNVGNHEYN TEYHSWNVTE IEGRKKKKAK LSIGNNKINF IPQKGTPHEW SIDKLVSYDN
EKKHMFLEFV DPYRSLELHT GNTTTCEEIM NIIGEYKGAS RDPGLREVEM ASKSKKRGIV
QYDFMAESQD ELTIKSGDKV YILDDKKSKD WWMCQLVDSG KSGLVPAQFI EPVRDKKHTE
STASGIIKSI KKNFTKSPSR SRSRSRSKSN ANASWKDDEL QNDVVGSAAG KRSRKSSLSS
HKKNSSATKD FPNPKKSRLW VDRSGTFKVD AEFIGCAKGK IHLHKANGVK IAVAADKLSN
EDLAYVEKIT GFSLEKFKAN DGSSSRGTDS RDSERERRRR LKEQEEKERD RRLKERELYE
LKKARELLDE ERSRLQEKEL PPIKPPRPTS TTSVPNTTSV PPAESSNNNN SSNKYDWFEF
FLNCGVDVSN CQRYTINFDR EQLTEDMMPD INNSMLRTLG LREGDIVRVM KHLDKKFGRE
NIASIPTNAT GNMFSQPDGS LNVATSPETS LPQQLLPQTT SPAQTAPSTS AETDDAWTVK
PASKSESNLL SKKSEFTGSM QDLLDLQPLE PKKAAASTPE PNLKDLEPVK TGGTTVPAAP
VSSAPVSSAP APLDPFKTGG NNILPLSTGF VMMPMITGGD MLPMQRTGGF VVPQTTFGMQ
SQVTGGILPV QKTGNGLIPI SNTGGAMMPQ TTFGAAATVL PLQKTGGGLI PIATTGGAQF
PQTSFNVQGQ QQLPTGSILP VQKTANGLIS ANTGVSMPTV QRTGGTMIPQ TSFGVSQQLT
GGAMMTQPQN TGSAMMPQTS FNAVPQITGG AMMPQTSFNA LPQVTGGAMM PLQRTGGALN
TFNTGGAMIP QTSFSSQAQN TGGFRPQSQF GLTLQKTGGI APLNQNQFTG GAMNTLSTGG
VLQQQQPQTM NTFNTGGVMQ ELQMMTTFNT GGAMQQPQMM NTFNTDGIMQ QPQMMNTFNT
GGAMQQPQQQ ALQNQPTGFG FGNGPQQSRQ ANIFNATASN PFGF


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