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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)DescriptionActionsGraphical viewLength
Calcium bindingi29 – 401PROSITE-ProRule annotationAdd BLAST12
Calcium bindingi64 – 752PROSITE-ProRule annotationAdd BLAST12

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
  • actin filament network formation Source: GO_Central
  • 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
  • actin filament Source: GO_Central
  • actomyosin contractile ring Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000737561 – 614FimbrinAdd BLAST614

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 interactors.
IntActiO59945. 1 interactor.
MINTiMINT-4676731.

Structurei

Secondary structure

1614
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi112 – 126Combined sources15
Turni130 – 132Combined sources3
Helixi133 – 135Combined sources3
Helixi144 – 148Combined sources5
Turni149 – 151Combined sources3
Helixi153 – 162Combined sources10
Helixi169 – 171Combined sources3
Helixi183 – 200Combined sources18
Helixi210 – 214Combined sources5
Helixi218 – 232Combined sources15
Helixi255 – 258Combined sources4
Helixi263 – 277Combined sources15
Helixi289 – 291Combined sources3
Helixi295 – 304Combined sources10
Turni306 – 308Combined sources3
Helixi312 – 315Combined sources4
Helixi319 – 331Combined sources13
Turni332 – 334Combined sources3
Helixi341 – 345Combined sources5
Helixi349 – 362Combined sources14
Helixi383 – 397Combined sources15
Helixi407 – 410Combined sources4
Turni411 – 413Combined sources3
Helixi415 – 424Combined sources10
Helixi431 – 433Combined sources3
Helixi446 – 462Combined sources17
Helixi472 – 476Combined sources5
Helixi480 – 498Combined sources19
Helixi511 – 522Combined sources12
Turni523 – 525Combined sources3
Helixi537 – 541Combined sources5
Helixi543 – 552Combined sources10
Helixi554 – 556Combined sources3
Helixi559 – 561Combined sources3
Helixi568 – 584Combined sources17
Helixi593 – 597Combined sources5
Helixi601 – 612Combined sources12

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO59945.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini16 – 50EF-hand 1PROSITE-ProRule annotationAdd BLAST35
Domaini51 – 86EF-hand 2PROSITE-ProRule annotationAdd BLAST36
Domaini98 – 368Actin-binding 1Add BLAST271
Domaini112 – 233CH 1PROSITE-ProRule annotationAdd BLAST122
Domaini261 – 364CH 2PROSITE-ProRule annotationAdd BLAST104
Domaini369 – 614Actin-binding 2Add BLAST246
Domaini385 – 495CH 3PROSITE-ProRule annotationAdd BLAST111
Domaini508 – 614CH 4PROSITE-ProRule annotationAdd BLAST107

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.
OMAiAKANGMH.
OrthoDBiEOG092C14NT.
PhylomeDBiO59945.

Family and domain databases

CDDicd00014. CH. 3 hits.
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
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1RT8X-ray2.00A108-614[»]
ProteinModelPortaliO59945.
SMRiO59945.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276316. 10 interactors.
IntActiO59945. 1 interactor.
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.
OMAiAKANGMH.
OrthoDBiEOG092C14NT.
PhylomeDBiO59945.

Miscellaneous databases

EvolutionaryTraceiO59945.
PROiO59945.

Family and domain databases

CDDicd00014. CH. 3 hits.
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...

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: November 30, 2016
This is version 135 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.