FAT1_SCHPO
ID FAT1_SCHPO Reviewed; 1385 AA.
AC O13735; Q9UTJ0;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2001, sequence version 2.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Actin-interacting protein 3 homolog;
GN Name=fat1; ORFNames=SPAC15A10.16, SPAC15E1.01;
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 IDENTIFICATION, AND GENE NAME.
RX PubMed=10679021; DOI=10.1091/mbc.11.2.647;
RA Jin H., Amberg D.C.;
RT "The secretory pathway mediates localization of the cell polarity regulator
RT Aip3p/Bud6p.";
RL Mol. Biol. Cell 11:647-661(2000).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-602, AND IDENTIFICATION BY
RP MASS 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: Involved in the organization and/or function of the actin
CC cytoskeleton.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000305}.
CC -!- SIMILARITY: To yeast BUD6. {ECO:0000305}.
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DR EMBL; CU329670; CAB10112.1; -; Genomic_DNA.
DR PIR; T37715; T37715.
DR PIR; T37716; T37716.
DR RefSeq; NP_594302.2; NM_001019725.2.
DR AlphaFoldDB; O13735; -.
DR SMR; O13735; -.
DR BioGRID; 279206; 8.
DR STRING; 4896.SPAC15A10.16.1; -.
DR iPTMnet; O13735; -.
DR MaxQB; O13735; -.
DR PaxDb; O13735; -.
DR PRIDE; O13735; -.
DR EnsemblFungi; SPAC15A10.16.1; SPAC15A10.16.1:pep; SPAC15A10.16.
DR GeneID; 2542756; -.
DR KEGG; spo:SPAC15A10.16; -.
DR PomBase; SPAC15A10.16; -.
DR VEuPathDB; FungiDB:SPAC15A10.16; -.
DR eggNOG; ENOG502QS95; Eukaryota.
DR HOGENOM; CLU_005287_0_0_1; -.
DR InParanoid; O13735; -.
DR OMA; ADFTEHD; -.
DR PhylomeDB; O13735; -.
DR PRO; PR:O13735; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0030478; C:actin cap; ISO:PomBase.
DR GO; GO:0051286; C:cell tip; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; HDA:PomBase.
DR GO; GO:0003779; F:actin binding; ISO:PomBase.
DR GO; GO:0005519; F:cytoskeletal regulatory protein binding; IEA:InterPro.
DR GO; GO:0030010; P:establishment of cell polarity; IBA:GO_Central.
DR GO; GO:0051125; P:regulation of actin nucleation; IEA:InterPro.
DR InterPro; IPR022782; AIP3-like_C.
DR InterPro; IPR005613; AIP3_C.
DR Pfam; PF03915; AIP3; 1.
DR SMART; SM00806; AIP3; 1.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Phosphoprotein; Reference proteome.
FT CHAIN 1..1385
FT /note="Actin-interacting protein 3 homolog"
FT /id="PRO_0000087198"
FT REGION 1..55
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 177..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..369
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 505..708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 752..776
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 882..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1312..1340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1009..1096
FT /evidence="ECO:0000255"
FT COMPBIAS 177..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..231
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 316..369
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 418..475
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..547
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 560..575
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 577..596
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 619..650
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 668..690
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1313..1327
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 602
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 1385 AA; 154326 MW; ABB3D40CC4FF7537 CRC64;
MFNNGDNMSR ERFSSNHSMQ RQKTESRANF SRRLVPSDSN RKPVPNGASN SPLSRDAASH
LISTIETSIM KLLVVTKELL ESLTNWSKGT VNDSAVSSVY VTLIGEFLQT TKSFHEAGIE
TADLNDFPLE LRSVLEQTLE KTPSSDALET NLPNVRELVM HLLQSLKYKQ SLVKSRLNQS
RSNLPQMTRE ANDNDVNRRN SRGSSQGSIS SFRNPDSRKQ YEETTSASLS APGAFDALKQ
TNALERRASK RLSHMVKDQQ NNEGSSQNLR NITVESVRGF LRDSSKPDNI MDSPSPKVSK
RPSIVRQDSH DSNKLSRRPT INTSFDRKFS PKLTRTPSLT KSLDPGTPTS LKSPSLRKSP
SSFVQKDVYS RSNSLRISQA NRSNVFPGAT DVTRSVSDHR ILSSSTINDG EVAPPLPQRS
RTISSPNSPL SATVLPSSTP ILLPRGRSST LSVNKKQFNA DDGSTLNSPN SIRETEEYAA
SPKLEDIADE VETDATSQRE LLERQIQKAE SSEDTSEIES LQGKLSLPQV SSTQQEIQPS
SSVPEAASNE IAEKEPAVTA IESITERKEE APVISSSEKI ESGTSISTSD TKGGLANFEN
DSLEELERLI QQNNAEQDEP SYKFHKYEYS SEESGSEDEF KSEKDTKGYV ISNDDSTQVE
EDSEDKSTPN TGASAKLIND PSSTITVSDV YPKKPASPVE ITEPPSSALV SATSPTTNVP
IVPEAVHLST AFSTAPVSTI VSNISPLPTV APPNVSGSPS ETPISKPEKV PVVSQTEKAL
PKPLGVDTEK YYFLRYNNQT RKVKVESPLS NANELGELFS NVYKISFSGD SYELNIEDPD
TKISYLLEDL SDLKYKSLVS FMFKEQDANK KREDFHSGEV SAIQHSSAQN TLDDHVNTTT
HESPSSAFTE ILERLKAIEQ NISTNHTNDS AALKSSEDHS KLANNFSVPD SIDHKFYQQV
KNMQLELASL KQISAAFFTR IPLKIKDFKK EINAFNEKGS LDFQFGRGFV LSSKDRIERE
VKNVVEKFDE VNDQIELMRS DVLLRKVRPG LDQTSQLNEE SAYLEKRIQT LERSLEEVTP
IWKKQWEREL NAIVQEQEFL DSHTVLISDL KRDLSALSTV LSNVSAIAEL QAKSSIKSKP
LTLKTATESE IKGYRDQIQL EVLNLKPDSE ARLQAIERSE LLQKKRLLQR VDEFSKEVKT
FVENEKLNKI GGAEEADRIR TIQDEKVRKI LWDDFVSSKR NGKNGGSFIE ESSDTVLDEH
VVPDNSAKAT VAEIDYGSQV DTENFMLERS PLATPKPLKQ PDFNIYETPI VRSTAHETDD
EQTPSKYSDN RVESSSDTVF ENTDLKYDNN VQMSKVTHHV RHDTISTDDY DAYEDAEDVE
ETSLT
