SLA1_SCHPO
ID SLA1_SCHPO Reviewed; 1420 AA.
AC O13736;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Actin cytoskeleton-regulatory complex protein sla1;
GN Name=sla1; ORFNames=SPAC16E8.01;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309; SER-311; SER-312;
RP SER-454; SER-573; SER-577; SER-927 AND THR-929, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
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:0000269|PubMed:16823372}. Note=Cytoplasmic and cortical actin
CC patches. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SLA1 family. {ECO:0000305}.
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DR EMBL; CU329670; CAB11030.1; -; Genomic_DNA.
DR PIR; T37781; T37781.
DR RefSeq; NP_594213.1; NM_001019636.2.
DR AlphaFoldDB; O13736; -.
DR SMR; O13736; -.
DR BioGRID; 278804; 6.
DR STRING; 4896.SPAC16E8.01.1; -.
DR iPTMnet; O13736; -.
DR SwissPalm; O13736; -.
DR MaxQB; O13736; -.
DR PaxDb; O13736; -.
DR PRIDE; O13736; -.
DR EnsemblFungi; SPAC16E8.01.1; SPAC16E8.01.1:pep; SPAC16E8.01.
DR GeneID; 2542338; -.
DR KEGG; spo:SPAC16E8.01; -.
DR PomBase; SPAC16E8.01; -.
DR VEuPathDB; FungiDB:SPAC16E8.01; -.
DR eggNOG; ENOG502QQC3; Eukaryota.
DR HOGENOM; CLU_003674_0_0_1; -.
DR InParanoid; O13736; -.
DR OMA; TIQNAYF; -.
DR PhylomeDB; O13736; -.
DR Reactome; R-SPO-983231; Factors involved in megakaryocyte development and platelet production.
DR PRO; PR:O13736; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0051286; C:cell tip; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005643; C:nuclear pore; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
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:0000147; P:actin cortical patch assembly; ISO:PomBase.
DR GO; GO:0044396; P:actin cortical patch organization; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; ISO:PomBase.
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 Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR013182; DUF1720.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR007131; SHD1.
DR InterPro; IPR029922; Sla1.
DR InterPro; IPR035800; Sla1_SH3_1.
DR InterPro; IPR035821; Sla1_SH3_3.
DR PANTHER; PTHR11216:SF134; PTHR11216:SF134; 1.
DR Pfam; PF08226; DUF1720; 3.
DR Pfam; PF00018; SH3_1; 2.
DR Pfam; PF03983; SHD1; 1.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50002; SH3; 3.
PE 1: Evidence at protein level;
KW Actin-binding; Cell membrane; Cytoplasm; Cytoskeleton; Endocytosis;
KW Endosome; Membrane; Phosphoprotein; Reference proteome; Repeat; SH3 domain.
FT CHAIN 1..1420
FT /note="Actin cytoskeleton-regulatory complex protein sla1"
FT /id="PRO_0000303944"
FT DOMAIN 5..81
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 82..139
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 508..568
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 138..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 708..786
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 902..1016
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 142..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 184..200
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..250
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..271
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 272..286
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 322..336
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 571..588
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..651
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 708..761
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1006
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 311
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 312
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 454
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 573
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 577
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 927
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 929
FT /note="Phosphothreonine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1420 AA; 154633 MW; 9B0D544FC6003B9F CRC64;
MANLPIIGIY KVLYSYEPQE INPGEEIPEN EREISIVEDE IVCLLEKGED DWYLVKRNVN
SNDDDEEIGI VPSNYITEAE PSTKMKALYD YTQQSVDEIS FQADQTLDCY GDTDSDWILV
GFNNNFGLAP RNYVEGMDAS SAPASQEPSA SGVNAPTVSA PNSMVSPPPS FQPPSAAAPA
TSLPSDYNPP PPPPPPPAVE DQAADANEPD DYYSSGRAVS PEIPPTYTPK QADPLPAPPP
PPPPTLPPQS TNTSQLPMPS RNVNNLGSQV NIPPPPATPS QPPRPPTNAS TRSTGTSSSM
AHSYDSPPSP SSPSDAYGDP NQHLKLRTDS HDDSRAYDSS SSMGNPAYEK WEVREVVGKK
KKRTGILAIN NKSIVLTFTK TMDAAQVWPV TDLVNYSSER KHVFIEFNSD SGITSLHLHA
SSNTNADNII RALGDVAGSA RAAGLREIAA ASGSPMPKLP SDSALHRLNA ASDAAGVNGG
RTGDYEMSTV YGDRSARAED HKPKDSSAGQ KMGTVLYDFI AEAADELTVK ANMRVVIVND
TASSDWWKCS VDGKEGVVPS NFIKPDTEGD AKSPPSSSKS GQGSSLSRRA SKHESKHKRD
SKHEARPESK HESHRESKSA EKDKKDKKDK KEDSKRSRSH SVSKPDSSKL RTWTDRTGAF
KVEAEFLGYS DDKIHLHKTN GVKISVPSAK MSYKDLDYVE LMTGKKVYSR TERKKDTQKQ
SHDHGHSHSK SHDREKEKEK KKDREHRKHR ETEEEDEGPP PQPARPESTR PALAPPSSSH
SNDKYDVIQE RPKISYDWFD FFLRCGVDFT VCNRYTHNFN NEHLDEACIP SLNPDTLRTL
GLKEGDIIRV MNHVNELNGV STKPASAITP ETKSTVNQIM SGGEALAAPV AVPAPIPAPV
AEPAPPAAPA KEVVEKAPSP PATRPKSTTP QKFDDDAWAN KPVTEPPVRA SSVTVEPARV
TESMNKMNIS EEAKKPEAPS RPRTAPIPEP EEQKKAPVEK KDAEKSVQAP IPAQPTGNIT
IQNAYFTAPQ PMAADPFQSP LYVQPTGFQP PPSALPIQPT GYMQPIPVQA TGYQPLMVQP
TGLQPHMTGV MPQVTGVMPQ MTGVVPQMTG VMPQMTGVQV QKTGAMPQQP VNYGYQVAGM
QPQATGIISQ PTGIRAQATG IMTQPTGLHT QATGMMQPTG MQPQATGIMP QATGMMQPTG
MQPQVTGIMP QSMPMQPQMT GVQVQKTGMV AQPMLSQYTG YQQNYTPTAM PAADGYGMQP
SMNDTQAYYN MNAQTPVNYG FAGGQDTSFG YEQQQMYSPM QQQQQQYYGT EMQPDMGYQQ
PMMSNYYDPM QMQQQTPYGY NQTGMEGYSE YGYAQPAGNM ANPMSYDPVS NASLYMPSDY
NQQTQPANYY DSSFGGAQGA NEAGKKASIY QATPDNPFGF
