FIMB_SCHPO
ID FIMB_SCHPO Reviewed; 614 AA.
AC O59945;
DT 01-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Fimbrin;
GN Name=fim1; ORFNames=SPBC1778.06c;
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 [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=11294907; DOI=10.1091/mbc.12.4.1061;
RA Wu J.-Q., Baehler J., Pringle J.R.;
RT "Roles of a fimbrin and an alpha-actinin-like protein in fission yeast cell
RT polarization and cytokinesis.";
RL Mol. Biol. Cell 12:1061-1077(2001).
RN [2]
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 [3]
RP FUNCTION.
RX PubMed=11694585; DOI=10.1091/mbc.12.11.3515;
RA Nakano K., Satoh K., Morimatsu A., Ohnuma M., Mabuchi I.;
RT "Interactions among a fimbrin, a capping protein, and an actin-
RT depolymerizing factor in organization of the fission yeast actin
RT cytoskeleton.";
RL Mol. Biol. Cell 12:3515-3526(2001).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 102-614.
RX PubMed=15274920; DOI=10.1016/j.str.2004.04.010;
RA Klein M.G., Shi W., Ramagopal U., Tseng Y., Wirtz D., Kovar D.R.,
RA Staiger C.J., Almo S.C.;
RT "Structure of the actin crosslinking core of fimbrin.";
RL Structure 12:999-1013(2004).
CC -!- FUNCTION: Binds to actin, and functionally associates with actin
CC structures involved in the development and maintenance of cell
CC polarity. Plays a role in cytokinesis. Plays important roles in mating
CC and in spore formation. {ECO:0000269|PubMed:11294907,
CC ECO:0000269|PubMed:11694585}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, actin patch
CC {ECO:0000269|PubMed:11294907}. Note=Localizes both to the cortical
CC actin patches and to the medial ring in an F-actin-dependent manner.
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DR EMBL; AF053722; AAC14025.1; -; Genomic_DNA.
DR EMBL; CU329671; CAB39801.1; -; Genomic_DNA.
DR PIR; T39688; T39688.
DR RefSeq; NP_596289.1; NM_001022211.2.
DR PDB; 1RT8; X-ray; 2.00 A; A=108-614.
DR PDBsum; 1RT8; -.
DR AlphaFoldDB; O59945; -.
DR SMR; O59945; -.
DR BioGRID; 276316; 13.
DR IntAct; O59945; 1.
DR MINT; O59945; -.
DR STRING; 4896.SPBC1778.06c.1; -.
DR iPTMnet; O59945; -.
DR MaxQB; O59945; -.
DR PaxDb; O59945; -.
DR PRIDE; O59945; -.
DR EnsemblFungi; SPBC1778.06c.1; SPBC1778.06c.1:pep; SPBC1778.06c.
DR GeneID; 2539765; -.
DR KEGG; spo:SPBC1778.06c; -.
DR PomBase; SPBC1778.06c; fim1.
DR VEuPathDB; FungiDB:SPBC1778.06c; -.
DR eggNOG; KOG0046; Eukaryota.
DR HOGENOM; CLU_015284_3_0_1; -.
DR InParanoid; O59945; -.
DR OMA; DAEMVRW; -.
DR PhylomeDB; O59945; -.
DR EvolutionaryTrace; O59945; -.
DR PRO; PR:O59945; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0099079; C:actin body; IDA:PomBase.
DR GO; GO:0030479; C:actin cortical patch; IDA:PomBase.
DR GO; GO:0005884; C:actin filament; IBA:GO_Central.
DR GO; GO:0032432; C:actin filament bundle; IBA:GO_Central.
DR GO; GO:0032153; C:cell division site; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0031097; C:medial cortex; IDA:PomBase.
DR GO; GO:0120106; C:mitotic actomyosin contractile ring, distal actin filament layer; IDA:PomBase.
DR GO; GO:0051015; F:actin filament binding; IDA:PomBase.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0051666; P:actin cortical patch localization; IMP:PomBase.
DR GO; GO:0044396; P:actin cortical patch organization; IDA:PomBase.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:PomBase.
DR GO; GO:0051639; P:actin filament network formation; IBA:GO_Central.
DR GO; GO:0044837; P:actomyosin contractile ring organization; IMP:PomBase.
DR GO; GO:0006897; P:endocytosis; IMP:PomBase.
DR GO; GO:0110009; P:formin-nucleated actin cable organization; IDA:PomBase.
DR GO; GO:1902404; P:mitotic actomyosin contractile ring contraction; EXP:PomBase.
DR GO; GO:1904530; P:negative regulation of actin filament binding; IDA:PomBase.
DR GO; GO:0034316; P:negative regulation of Arp2/3 complex-mediated actin nucleation; IDA:PomBase.
DR CDD; cd00014; CH; 3.
DR Gene3D; 1.10.418.10; -; 4.
DR InterPro; IPR001589; Actinin_actin-bd_CS.
DR InterPro; IPR001715; CH-domain.
DR InterPro; IPR036872; CH_dom_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR039959; Fimbrin/Plastin.
DR PANTHER; PTHR19961; PTHR19961; 1.
DR Pfam; PF00307; CH; 4.
DR SMART; SM00033; CH; 4.
DR SUPFAM; SSF47473; SSF47473; 1.
DR SUPFAM; SSF47576; SSF47576; 1.
DR PROSITE; PS00019; ACTININ_1; 1.
DR PROSITE; PS00020; ACTININ_2; 1.
DR PROSITE; PS50021; CH; 4.
DR PROSITE; PS50222; EF_HAND_2; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Calcium; Cytoplasm; Cytoskeleton;
KW Metal-binding; Reference proteome; Repeat.
FT CHAIN 1..614
FT /note="Fimbrin"
FT /id="PRO_0000073756"
FT DOMAIN 16..50
FT /note="EF-hand 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 51..86
FT /note="EF-hand 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00448"
FT DOMAIN 112..233
FT /note="Calponin-homology (CH) 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 261..364
FT /note="Calponin-homology (CH) 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 385..495
FT /note="Calponin-homology (CH) 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT DOMAIN 508..614
FT /note="Calponin-homology (CH) 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00044"
FT REGION 98..368
FT /note="Actin-binding 1"
FT REGION 369..614
FT /note="Actin-binding 2"
FT BINDING 29
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 31
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 35
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 40
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000305"
FT BINDING 66
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 68
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 70
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT BINDING 75
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000305"
FT HELIX 112..126
FT /evidence="ECO:0007829|PDB:1RT8"
FT TURN 130..132
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 144..148
FT /evidence="ECO:0007829|PDB:1RT8"
FT TURN 149..151
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 153..162
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 169..171
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 183..200
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 210..214
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 218..232
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 255..258
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 263..277
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 289..291
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 295..304
FT /evidence="ECO:0007829|PDB:1RT8"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 312..315
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 319..331
FT /evidence="ECO:0007829|PDB:1RT8"
FT TURN 332..334
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 341..345
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 349..362
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 383..397
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 407..410
FT /evidence="ECO:0007829|PDB:1RT8"
FT TURN 411..413
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 415..424
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 431..433
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 446..462
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 472..476
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 480..498
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 511..522
FT /evidence="ECO:0007829|PDB:1RT8"
FT TURN 523..525
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 537..541
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 543..552
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 554..556
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 559..561
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 568..584
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 593..597
FT /evidence="ECO:0007829|PDB:1RT8"
FT HELIX 601..612
FT /evidence="ECO:0007829|PDB:1RT8"
SQ SEQUENCE 614 AA; 68617 MW; DAE738D5C7F0F097 CRC64;
MLALKLQKKY PELTNEEILT LTDQFNKLDV DGKGYLDQPT TIKAFEDSKK GSYDEVREAI
REVNVDSSGR VEPEDFVGIF NVLKKGVEGT EVKKGRITIK GSSSSVSHTI NEEERREFIK
HINSVLAGDP DVGSRVPINT ETFEFFDQCK DGLILSKLIN DSVPDTIDER VLNKQRNNKP
LDNFKCIENN NVVINSAKAM GGISITNIGA GDILEGREHL ILGLVWQIIR RGLLGKIDIT
LHPELYRLLE EDETLDQFLR LPPEKILLRW FNYHLKAANW PRTVSNFSKD VSDGENYTVL
LNQLAPELCS RAPLQTTDVL QRAEQVLQNA EKLDCRKYLT PTAMVAGNPK LNLAFVAHLF
NTHPGLEPLN EEEKPEIEPF DAEGEREARV FTLWLNSLDV TPSIHDFFNN LRDGLILLQA
YDKITPNTVN WKKVNKAPAS GDEMMRFKAV ENCNYAVDLG KNQGFSLVGI QGADITDGSR
TLTLALVWQM MRMNITKTLH SLSRGGKTLS DSDMVAWANS MAAKGGKGSQ IRSFRDPSIS
TGVFVLDVLH GIKSEYVDYN LVTDGSTEEL AIQNARLAIS IARKLGAVIF ILPEDIVAVR
PRLVLHFIGS LMAV
