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Protein

Fermitin family homolog 1

Gene

Fermt1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in cell adhesion. Contributes to integrin activation. When coexpressed with talin, potentiates activation of ITGA2B. Required for normal keratinocyte proliferation. Required for normal polarization of basal keratinocytes in skin, and for normal cell shape. Required for normal adhesion of keratinocytes to fibronectin and laminin, and for normal keratinocyte migration to wound sites (By similarity).By similarity

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Names & Taxonomyi

Protein namesi
Recommended name:
Fermitin family homolog 1
Alternative name(s):
Kindlin-1
Unc-112-related protein 1
Gene namesi
Name:Fermt1
Synonyms:Kind1, Urp1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:2443583. Fermt1.

Subcellular locationi

GO - Cellular componenti

  • cell junction Source: UniProtKB
  • cytoskeleton Source: UniProtKB-SubCell
  • cytosol Source: UniProtKB
  • focal adhesion Source: MGI
  • ruffle membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Cell projection, Cytoplasm, Cytoskeleton, Membrane

Pathology & Biotechi

Disruption phenotypei

Mice are born with the expected Mendelian distribution and appear normal at birth, but fail to thrive, become dehydrated and die after three to five days. They develop skin atrophy and die due to a lethal intestinal epithelial dysfunction. The colon is shortened and swollen and presents signs of acute inflammation. At the time of death, about 80% of the colonic epithelium is detached.1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002194531 – 677Fermitin family homolog 1Add BLAST677

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei170PhosphoserineBy similarity1
Modified residuei179PhosphoserineBy similarity1

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiP59113.
PaxDbiP59113.
PeptideAtlasiP59113.
PRIDEiP59113.

PTM databases

iPTMnetiP59113.
PhosphoSitePlusiP59113.

Expressioni

Gene expression databases

BgeeiENSMUSG00000027356.

Interactioni

Subunit structurei

Interacts with the cytoplasmic domain of integrins ITGB1 and ITGB3.By similarity

Protein-protein interaction databases

IntActiP59113. 1 interactor.
MINTiMINT-4139673.
STRINGi10090.ENSMUSP00000047616.

Structurei

Secondary structure

1677
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi1 – 5Combined sources5
Beta strandi12 – 19Combined sources8
Beta strandi26 – 33Combined sources8
Helixi39 – 50Combined sources12
Beta strandi57 – 63Combined sources7
Turni64 – 67Combined sources4
Beta strandi68 – 70Combined sources3
Helixi77 – 80Combined sources4
Beta strandi88 – 92Combined sources5
Beta strandi372 – 379Combined sources8
Beta strandi390 – 397Combined sources8
Beta strandi400 – 406Combined sources7
Helixi407 – 409Combined sources3
Beta strandi415 – 419Combined sources5
Beta strandi424 – 430Combined sources7
Turni431 – 434Combined sources4
Beta strandi435 – 444Combined sources10
Beta strandi447 – 457Combined sources11
Helixi458 – 472Combined sources15
Helixi482 – 496Combined sources15

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KMCNMR-A1-96[»]
4BBKX-ray2.10A364-509[»]
DisProtiDP00655.
ProteinModelPortaliP59113.
SMRiP59113.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP59113.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini96 – 653FERMAdd BLAST558
Domaini377 – 473PHPROSITE-ProRule annotationAdd BLAST97

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi147 – 154Poly-Lys8

Domaini

The FERM domain is not correctly detected by PROSITE or Pfam techniques because it contains the insertion of a PH domain. The FERM domain contains the subdomains F1, F2 and F3. It is preceded by a F0 domain with a ubiquitin-like fold. The F0 domain is required for integrin activation and for localization at focal adhesions (By similarity).By similarity

Sequence similaritiesi

Belongs to the kindlin family.Curated
Contains 1 FERM domain.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG3727. Eukaryota.
ENOG410XS1B. LUCA.
GeneTreeiENSGT00390000013444.
HOGENOMiHOG000231715.
HOVERGENiHBG020688.
InParanoidiP59113.
KOiK17082.
OMAiFKQYWFI.
OrthoDBiEOG091G03SD.
TreeFamiTF314677.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 2 hits.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00295. B41. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50729. SSF50729. 2 hits.
PROSITEiPS00661. FERM_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P59113-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLSSGDLTSA SWELVVRVDH ANGEQQTEIT LRVSGDLHIG GVMLKLVEQM
60 70 80 90 100
NIAQDWSDYA LWWEQKRCWL LKTHWTLDKC GVQADANLLF TPQHKMLRLR
110 120 130 140 150
LPNAKTVRLR VSFSAVVFKA VADICKVLNI RRPEELSLLK PSSDYCKKKK
160 170 180 190 200
KKEKNSKEPV IEDILNLESS STSSGSPVSP GLYSKTMTPT YDPINGTPAL
210 220 230 240 250
STMTWFGDSP LTEQNCSVLA FSQPPPSPDV LADMFQPRSL VDKAKMNAGW
260 270 280 290 300
LDSSRSLMEQ SIQEDEQLQL RFKYYTFFDL NPKYDAVRIN QLYEQARWAV
310 320 330 340 350
LLEEIDCTEE EMLIFAALQY HISKLSQCAE IQDFATKSEV DEVEAALSSL
360 370 380 390 400
EVTLEGGKAD NTLEDITDIP KLADYLKLFR PKKLMLKACK QYWFVFKDTS
410 420 430 440 450
IAYFKNKELE QGEPIEKLNL RGCEIVPDVN VSGRKFGIKL LIPVADGMNE
460 470 480 490 500
VYLRCDHEDQ YARWMAACIL ASKGKTMADS SYQPEVISIL SFLKMKNRNS
510 520 530 540 550
SPLVASSLEN MDMNPECLVS PCCAKKHKSK QLAARILEAH HNVAQMPLVE
560 570 580 590 600
AKLQFIQAWQ SLPEFGLTYY LVRFKGSKKD DILGVAYNRL IRIDAVTGIP
610 620 630 640 650
VTTWRFANMK QWNVNWEIRQ VAIEFDQNVS IAFTCLSADC KIVHEYIGGY
660 670
IFLSTRSKDQ NETLDEDLFH KLTGGQD
Length:677
Mass (Da):76,941
Last modified:July 27, 2011 - v4
Checksum:i9B8B1876FA7621EE
GO

Sequence cautioni

The sequence AAH29093 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti522C → R in AAH29093 (PubMed:15489334).Curated1
Sequence conflicti586A → S in AAH29093 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL831763 Genomic DNA. Translation: CAM20382.1.
BC029093 mRNA. Translation: AAH29093.1. Different initiation.
BC042792 mRNA. No translation available.
AK050804 mRNA. Translation: BAC34417.1.
CCDSiCCDS38248.1.
RefSeqiNP_932146.2. NM_198029.2.
XP_017173695.1. XM_017318206.1.
XP_017173696.1. XM_017318207.1.
XP_017173699.1. XM_017318210.1.
UniGeneiMm.209784.

Genome annotation databases

EnsembliENSMUST00000038280; ENSMUSP00000047616; ENSMUSG00000027356.
GeneIDi241639.
KEGGimmu:241639.
UCSCiuc008mno.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL831763 Genomic DNA. Translation: CAM20382.1.
BC029093 mRNA. Translation: AAH29093.1. Different initiation.
BC042792 mRNA. No translation available.
AK050804 mRNA. Translation: BAC34417.1.
CCDSiCCDS38248.1.
RefSeqiNP_932146.2. NM_198029.2.
XP_017173695.1. XM_017318206.1.
XP_017173696.1. XM_017318207.1.
XP_017173699.1. XM_017318210.1.
UniGeneiMm.209784.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2KMCNMR-A1-96[»]
4BBKX-ray2.10A364-509[»]
DisProtiDP00655.
ProteinModelPortaliP59113.
SMRiP59113.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiP59113. 1 interactor.
MINTiMINT-4139673.
STRINGi10090.ENSMUSP00000047616.

PTM databases

iPTMnetiP59113.
PhosphoSitePlusiP59113.

Proteomic databases

MaxQBiP59113.
PaxDbiP59113.
PeptideAtlasiP59113.
PRIDEiP59113.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000038280; ENSMUSP00000047616; ENSMUSG00000027356.
GeneIDi241639.
KEGGimmu:241639.
UCSCiuc008mno.1. mouse.

Organism-specific databases

CTDi55612.
MGIiMGI:2443583. Fermt1.

Phylogenomic databases

eggNOGiKOG3727. Eukaryota.
ENOG410XS1B. LUCA.
GeneTreeiENSGT00390000013444.
HOGENOMiHOG000231715.
HOVERGENiHBG020688.
InParanoidiP59113.
KOiK17082.
OMAiFKQYWFI.
OrthoDBiEOG091G03SD.
TreeFamiTF314677.

Miscellaneous databases

EvolutionaryTraceiP59113.
PROiP59113.
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000027356.

Family and domain databases

Gene3Di1.20.80.10. 2 hits.
2.30.29.30. 2 hits.
InterProiIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PfamiPF00373. FERM_M. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTiSM00295. B41. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF47031. SSF47031. 1 hit.
SSF50729. SSF50729. 2 hits.
PROSITEiPS00661. FERM_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiFERM1_MOUSE
AccessioniPrimary (citable) accession number: P59113
Secondary accession number(s): A2ANX1, Q8BQG6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: July 27, 2011
Last modified: November 2, 2016
This is version 121 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.