ID   SLA1_USTMA              Reviewed;        1207 AA.
AC   Q4P3H6; A0A0D1DQT8;
DT   02-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2005, sequence version 1.
DT   25-MAY-2022, entry version 102.
DE   RecName: Full=Actin cytoskeleton-regulatory complex protein SLA1;
GN   Name=SLA1; ORFNames=UMAG_05337;
OS   Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC   Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX   NCBI_TaxID=237631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=521 / FGSC 9021;
RX   PubMed=17080091; DOI=10.1038/nature05248;
RA   Kaemper J., Kahmann R., Boelker M., Ma L.-J., Brefort T., Saville B.J.,
RA   Banuett F., Kronstad J.W., Gold S.E., Mueller O., Perlin M.H.,
RA   Woesten H.A.B., de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G.,
RA   Snetselaar K., McCann M., Perez-Martin J., Feldbruegge M., Basse C.W.,
RA   Steinberg G., Ibeas J.I., Holloman W., Guzman P., Farman M.L.,
RA   Stajich J.E., Sentandreu R., Gonzalez-Prieto J.M., Kennell J.C., Molina L.,
RA   Schirawski J., Mendoza-Mendoza A., Greilinger D., Muench K., Roessel N.,
RA   Scherer M., Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B.,
RA   Meng S., Ho E.C.H., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J.,
RA   Deelstra H.J., Ortiz-Castellanos L., Li W., Sanchez-Alonso P.,
RA   Schreier P.H., Haeuser-Hahn I., Vaupel M., Koopmann E., Friedrich G.,
RA   Voss H., Schlueter T., Margolis J., Platt D., Swimmer C., Gnirke A.,
RA   Chen F., Vysotskaia V., Mannhaupt G., Gueldener U., Muensterkoetter M.,
RA   Haase D., Oesterheld M., Mewes H.-W., Mauceli E.W., DeCaprio D., Wade C.M.,
RA   Butler J., Young S.K., Jaffe D.B., Calvo S.E., Nusbaum C., Galagan J.E.,
RA   Birren B.W.;
RT   "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT   maydis.";
RL   Nature 444:97-101(2006).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=521 / FGSC 9021;
RA   Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL   Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Component of the PAN1 actin cytoskeleton-regulatory complex.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC       protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Endosome
CC       membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250};
CC       Cytoplasmic side {ECO:0000250}. Cytoplasm, cytoskeleton, actin patch
CC       {ECO:0000250}. Note=Cytoplasmic and cortical actin patches.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SLA1 family. {ECO:0000305}.
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DR   EMBL; CM003158; KIS66336.1; -; Genomic_DNA.
DR   RefSeq; XP_011392040.1; XM_011393738.1.
DR   AlphaFoldDB; Q4P3H6; -.
DR   SMR; Q4P3H6; -.
DR   STRING; 5270.UM05337P0; -.
DR   EnsemblFungi; KIS66336; KIS66336; UMAG_05337.
DR   GeneID; 23565255; -.
DR   KEGG; uma:UMAG_05337; -.
DR   VEuPathDB; FungiDB:UMAG_05337; -.
DR   eggNOG; ENOG502QQC3; Eukaryota.
DR   HOGENOM; CLU_006319_0_0_1; -.
DR   InParanoid; Q4P3H6; -.
DR   OMA; PDWILVG; -.
DR   OrthoDB; 1483210at2759; -.
DR   Proteomes; UP000000561; Chromosome 19.
DR   GO; GO:0030479; C:actin cortical patch; IBA:GO_Central.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR   GO; GO:0042802; F:identical protein binding; IEA:InterPro.
DR   GO; GO:0030674; F:protein-macromolecule adaptor activity; IEA:InterPro.
DR   GO; GO:0043130; F:ubiquitin binding; IEA:InterPro.
DR   GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR   GO; GO:0006897; P:endocytosis; IBA:GO_Central.
DR   GO; GO:0016197; P:endosomal transport; IBA:GO_Central.
DR   CDD; cd11773; SH3_Sla1p_1; 1.
DR   CDD; cd11775; SH3_Sla1p_3; 1.
DR   Gene3D; 1.10.150.50; -; 1.
DR   InterPro; IPR013182; DUF1720.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   InterPro; IPR007131; SHD1.
DR   InterPro; IPR035800; Sla1_SH3_1.
DR   InterPro; IPR035821; Sla1_SH3_3.
DR   Pfam; PF08226; DUF1720; 1.
DR   Pfam; PF00018; SH3_1; 2.
DR   Pfam; PF14604; SH3_9; 1.
DR   Pfam; PF03983; SHD1; 1.
DR   PRINTS; PR00452; SH3DOMAIN.
DR   SMART; SM00326; SH3; 3.
DR   SUPFAM; SSF50044; SSF50044; 3.
DR   PROSITE; PS50002; SH3; 3.
PE   3: Inferred from homology;
KW   Actin-binding; Cell membrane; Cytoplasm; Cytoskeleton; Endocytosis;
KW   Endosome; Membrane; Reference proteome; Repeat; SH3 domain.
FT   CHAIN           1..1207
FT                   /note="Actin cytoskeleton-regulatory complex protein SLA1"
FT                   /id="PRO_0000349490"
FT   DOMAIN          2..76
FT                   /note="SH3 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          77..142
FT                   /note="SH3 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   DOMAIN          367..427
FT                   /note="SH3 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT   REGION          143..185
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          325..367
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          448..553
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          609..667
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          736..757
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          773..919
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          936..979
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1175..1207
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..170
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        337..361
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        448..496
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        614..630
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        640..667
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        799..827
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        874..912
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        941..963
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1176..1197
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1207 AA;  129327 MW;  F3F07812568EE3A6 CRC64;
     MAYVALCKAL YDYVAQAEDE LNLTEDDHLY ILESDDPEWW KAKLRRLDEH GTPIQDDSDD
     STVGLVPANY VEEAEPIRLS RALYDYEAQT EEELSMAEDE LLRVYESDGV WLLVKKQGND
     PLSGGEGRLG YVPANYVDEA EAVDTGAAPA VEDEYTAADE DDEDDDDTDV TGSGAPIPQI
     HLPQTAQLGK GDNIKMWPVS ALDSKKKKKK GTLGIGNASL FFASESDKTP VKKISILHIA
     SHSLEKGKTL HLQLSPEAGL SESTLDFHAG SKDAANDIIR KIEVSKANAL TAAAAPVPVP
     VPAPAPPAAA AAAASAAVPL PPPPPPAPPV ASAAALPPPT RTTSATLPPP VRKNVSFQSQ
     PAAEPEEAVE HGVAMYDFEA QGDDELTVTE NEHLIILEKE NDDWWKVRND AGQEGVVPAS
     YVEATDASAA AGASSGATAA AALAAQQEEE ERLRREEEEA ATVAEAERQR EAVDRQREAR
     ERGEREEKER ARREALKAQP VPAPPKLTQR PSTTDVSRAA KNVAIPQGRS APERPKDGGS
     RSKPSPTNTR MWTDRTGAFK VEAEFLGFNQ GKIRLHKMNG VVIEVAIEKM SNGDIAFLED
     ITGKKLNPTD EEIAASAARR RERERERQSS RPQSSAVAGM PREDRERERE RRKEKEREQR
     RRESARSGPK RNVDWFEFFL AAGVDVDDCT RYASSFERDK IDETVLADLD PSTLRSIGLR
     EGDIIRVTKF IDKKYRRDKS HSSLSSSRAS GRANANTAAD LERQIKADEE LARKLQEQES
     SARRGDSVSP APPQLFSGPD GTLKNNTRRG RPTPKSTSSS NVDAASLAAA SESLARTATP
     PARTATASPA VAPKRTGSSL ANGFDDDAWT PRPPSTKPTT PARPTVASPA PSTPAAPAAP
     PAPTPPPAAV AVASSAPPAD PNSALFEKLA AMKAPSASVS PRPGVSPSPG SSFLGQSQMY
     NPNAPRGPFA PVPANQGLLQ PLVPTQGTGQ FVPTKTGMMG MQMTGMQPQL TGWGMQGMQG
     MQPQMTGFNN SMGSMSVMGG MGMQPQATGF GNGNGYGMNG SSPFTGGQIS TQQTGLVGMG
     MQPQATGFNN FGQNAQQMMT QQTGFGMGSQ QQGQQLQAEQ DEKEKFKASN IFQQMKTGAF
     AKDPNAAPQS SEKYDALRPQ PTGFQPGGVM PQFTGMGFGQ SAQQQQQQQQ QQYPYNNAYG
     GGFGGGF