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Protein

Fimbrin

Gene

fim1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to actin, and functionally associates with actin structures involved in the development and maintenance of cell polarity. Plays a role in cytokinesis. Plays important roles in mating and in spore formation.2 Publications

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Calcium bindingi29 – 40121PROSITE-ProRule annotationAdd
BLAST
Calcium bindingi64 – 75122PROSITE-ProRule annotationAdd
BLAST

GO - Molecular functioni

  • actin binding Source: PomBase
  • actin filament binding Source: PomBase
  • calcium ion binding Source: InterPro
  • protein binding, bridging Source: PomBase

GO - Biological processi

  • actin cortical patch localization Source: PomBase
  • actin crosslink formation Source: PomBase
  • actin cytoskeleton organization Source: PomBase
  • actin filament bundle assembly Source: PomBase
  • ascospore formation Source: PomBase
  • endocytosis Source: PomBase
  • establishment or maintenance of cell polarity regulating cell shape Source: PomBase
  • mitotic actomyosin contractile ring assembly Source: PomBase
  • mitotic cytokinesis Source: PomBase
  • negative regulation of actin filament depolymerization Source: PomBase
  • regulation of cell shape Source: PomBase
Complete GO annotation...

Keywords - Ligandi

Actin-binding, Calcium, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Fimbrin
Gene namesi
Name:fim1
ORF Names:SPBC1778.06c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome II

Organism-specific databases

EuPathDBiFungiDB:SPBC1778.06c.
PomBaseiSPBC1778.06c. fim1.

Subcellular locationi

  • Cytoplasmcytoskeletonactin patch 1 Publication

  • Note: Localizes both to the cortical actin patches and to the medial ring in an F-actin-dependent manner.

GO - Cellular componenti

  • actin cortical patch Source: PomBase
  • actomyosin contractile ring Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 614614FimbrinPRO_0000073756Add
BLAST

Proteomic databases

MaxQBiO59945.
PRIDEiO59945.

Interactioni

GO - Molecular functioni

  • actin binding Source: PomBase
  • actin filament binding Source: PomBase
  • protein binding, bridging Source: PomBase

Protein-protein interaction databases

BioGridi276316. 10 interactions.
IntActiO59945. 1 interaction.
MINTiMINT-4676731.

Structurei

Secondary structure

1
614
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi112 – 12615Combined sources
Turni130 – 1323Combined sources
Helixi133 – 1353Combined sources
Helixi144 – 1485Combined sources
Turni149 – 1513Combined sources
Helixi153 – 16210Combined sources
Helixi169 – 1713Combined sources
Helixi183 – 20018Combined sources
Helixi210 – 2145Combined sources
Helixi218 – 23215Combined sources
Helixi255 – 2584Combined sources
Helixi263 – 27715Combined sources
Helixi289 – 2913Combined sources
Helixi295 – 30410Combined sources
Turni306 – 3083Combined sources
Helixi312 – 3154Combined sources
Helixi319 – 33113Combined sources
Turni332 – 3343Combined sources
Helixi341 – 3455Combined sources
Helixi349 – 36214Combined sources
Helixi383 – 39715Combined sources
Helixi407 – 4104Combined sources
Turni411 – 4133Combined sources
Helixi415 – 42410Combined sources
Helixi431 – 4333Combined sources
Helixi446 – 46217Combined sources
Helixi472 – 4765Combined sources
Helixi480 – 49819Combined sources
Helixi511 – 52212Combined sources
Turni523 – 5253Combined sources
Helixi537 – 5415Combined sources
Helixi543 – 55210Combined sources
Helixi554 – 5563Combined sources
Helixi559 – 5613Combined sources
Helixi568 – 58417Combined sources
Helixi593 – 5975Combined sources
Helixi601 – 61212Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RT8X-ray2.00A108-614[»]
ProteinModelPortaliO59945.
SMRiO59945. Positions 110-614.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59945.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini16 – 5035EF-hand 1PROSITE-ProRule annotationAdd
BLAST
Domaini51 – 8636EF-hand 2PROSITE-ProRule annotationAdd
BLAST
Domaini98 – 368271Actin-binding 1Add
BLAST
Domaini112 – 233122CH 1PROSITE-ProRule annotationAdd
BLAST
Domaini261 – 364104CH 2PROSITE-ProRule annotationAdd
BLAST
Domaini369 – 614246Actin-binding 2Add
BLAST
Domaini385 – 495111CH 3PROSITE-ProRule annotationAdd
BLAST
Domaini508 – 614107CH 4PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 2 actin-binding domains.Curated
Contains 4 CH (calponin-homology) domains.PROSITE-ProRule annotation
Contains 2 EF-hand domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

HOGENOMiHOG000213447.
InParanoidiO59945.
KOiK17275.
OMAiCREERAF.
OrthoDBiEOG71P2KM.
PhylomeDBiO59945.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 4 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF00307. CH. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 4 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O59945-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLALKLQKKY PELTNEEILT LTDQFNKLDV DGKGYLDQPT TIKAFEDSKK
60 70 80 90 100
GSYDEVREAI REVNVDSSGR VEPEDFVGIF NVLKKGVEGT EVKKGRITIK
110 120 130 140 150
GSSSSVSHTI NEEERREFIK HINSVLAGDP DVGSRVPINT ETFEFFDQCK
160 170 180 190 200
DGLILSKLIN DSVPDTIDER VLNKQRNNKP LDNFKCIENN NVVINSAKAM
210 220 230 240 250
GGISITNIGA GDILEGREHL ILGLVWQIIR RGLLGKIDIT LHPELYRLLE
260 270 280 290 300
EDETLDQFLR LPPEKILLRW FNYHLKAANW PRTVSNFSKD VSDGENYTVL
310 320 330 340 350
LNQLAPELCS RAPLQTTDVL QRAEQVLQNA EKLDCRKYLT PTAMVAGNPK
360 370 380 390 400
LNLAFVAHLF NTHPGLEPLN EEEKPEIEPF DAEGEREARV FTLWLNSLDV
410 420 430 440 450
TPSIHDFFNN LRDGLILLQA YDKITPNTVN WKKVNKAPAS GDEMMRFKAV
460 470 480 490 500
ENCNYAVDLG KNQGFSLVGI QGADITDGSR TLTLALVWQM MRMNITKTLH
510 520 530 540 550
SLSRGGKTLS DSDMVAWANS MAAKGGKGSQ IRSFRDPSIS TGVFVLDVLH
560 570 580 590 600
GIKSEYVDYN LVTDGSTEEL AIQNARLAIS IARKLGAVIF ILPEDIVAVR
610
PRLVLHFIGS LMAV
Length:614
Mass (Da):68,617
Last modified:August 1, 1998 - v1
Checksum:iDAE738D5C7F0F097
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053722 Genomic DNA. Translation: AAC14025.1.
CU329671 Genomic DNA. Translation: CAB39801.1.
PIRiT39688.
RefSeqiNP_596289.1. NM_001022211.2.

Genome annotation databases

EnsemblFungiiSPBC1778.06c.1; SPBC1778.06c.1:pep; SPBC1778.06c.
GeneIDi2539765.
KEGGispo:SPBC1778.06c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF053722 Genomic DNA. Translation: AAC14025.1.
CU329671 Genomic DNA. Translation: CAB39801.1.
PIRiT39688.
RefSeqiNP_596289.1. NM_001022211.2.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RT8X-ray2.00A108-614[»]
ProteinModelPortaliO59945.
SMRiO59945. Positions 110-614.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276316. 10 interactions.
IntActiO59945. 1 interaction.
MINTiMINT-4676731.

Proteomic databases

MaxQBiO59945.
PRIDEiO59945.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC1778.06c.1; SPBC1778.06c.1:pep; SPBC1778.06c.
GeneIDi2539765.
KEGGispo:SPBC1778.06c.

Organism-specific databases

EuPathDBiFungiDB:SPBC1778.06c.
PomBaseiSPBC1778.06c. fim1.

Phylogenomic databases

HOGENOMiHOG000213447.
InParanoidiO59945.
KOiK17275.
OMAiCREERAF.
OrthoDBiEOG71P2KM.
PhylomeDBiO59945.

Miscellaneous databases

EvolutionaryTraceiO59945.
NextBioi20800915.
PROiO59945.

Family and domain databases

Gene3Di1.10.238.10. 1 hit.
1.10.418.10. 4 hits.
InterProiIPR001589. Actinin_actin-bd_CS.
IPR001715. CH-domain.
IPR011992. EF-hand-dom_pair.
IPR002048. EF_hand_dom.
[Graphical view]
PfamiPF00307. CH. 4 hits.
[Graphical view]
SMARTiSM00033. CH. 4 hits.
[Graphical view]
SUPFAMiSSF47473. SSF47473. 2 hits.
SSF47576. SSF47576. 1 hit.
PROSITEiPS00019. ACTININ_1. 1 hit.
PS00020. ACTININ_2. 1 hit.
PS50021. CH. 4 hits.
PS50222. EF_HAND_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Roles of a fimbrin and an alpha-actinin-like protein in fission yeast cell polarization and cytokinesis."
    Wu J.-Q., Baehler J., Pringle J.R.
    Mol. Biol. Cell 12:1061-1077(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, SUBCELLULAR LOCATION.
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Interactions among a fimbrin, a capping protein, and an actin-depolymerizing factor in organization of the fission yeast actin cytoskeleton."
    Nakano K., Satoh K., Morimatsu A., Ohnuma M., Mabuchi I.
    Mol. Biol. Cell 12:3515-3526(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  4. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 102-614.

Entry informationi

Entry nameiFIMB_SCHPO
AccessioniPrimary (citable) accession number: O59945
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: August 1, 1998
Last modified: May 11, 2016
This is version 130 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.