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P59113 (FERM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 103. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Fermitin family homolog 1
Alternative name(s):
Kindlin-1
Unc-112-related protein 1
Gene names
Name:Fermt1
Synonyms:Kind1, Urp1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length677 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Subunit structure

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

Subcellular location

Cytoplasmcytoskeleton By similarity. Cell junctionfocal adhesion By similarity. Cell projectionruffle membrane; Peripheral membrane protein; Cytoplasmic side By similarity. Note: Colocalizes with filamentous actin. Constituent of focal adhesions By similarity. Localized at the basal aspect of skin keratinocytes, close to the cell membrane By similarity. Upon TGFB1 treatment, it localizes to membrane ruffles By similarity.

Domain

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. Ref.5

Disruption phenotype

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. Ref.4

Sequence similarities

Belongs to the kindlin family.

Contains 1 FERM domain.

Contains 1 PH domain.

Sequence caution

The sequence AAH29093.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 677677Fermitin family homolog 1
PRO_0000219453

Regions

Domain96 – 653558FERM
Domain377 – 47397PH
Compositional bias147 – 1548Poly-Lys

Amino acid modifications

Modified residue1701Phosphoserine By similarity
Modified residue1791Phosphoserine By similarity

Experimental info

Sequence conflict5221C → R in AAH29093. Ref.2
Sequence conflict5861A → S in AAH29093. Ref.2

Secondary structure

.................................. 677
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P59113 [UniParc].

Last modified July 27, 2011. Version 4.
Checksum: 9B8B1876FA7621EE

FASTA67776,941
        10         20         30         40         50         60 
MLSSGDLTSA SWELVVRVDH ANGEQQTEIT LRVSGDLHIG GVMLKLVEQM NIAQDWSDYA 

        70         80         90        100        110        120 
LWWEQKRCWL LKTHWTLDKC GVQADANLLF TPQHKMLRLR LPNAKTVRLR VSFSAVVFKA 

       130        140        150        160        170        180 
VADICKVLNI RRPEELSLLK PSSDYCKKKK KKEKNSKEPV IEDILNLESS STSSGSPVSP 

       190        200        210        220        230        240 
GLYSKTMTPT YDPINGTPAL STMTWFGDSP LTEQNCSVLA FSQPPPSPDV LADMFQPRSL 

       250        260        270        280        290        300 
VDKAKMNAGW LDSSRSLMEQ SIQEDEQLQL RFKYYTFFDL NPKYDAVRIN QLYEQARWAV 

       310        320        330        340        350        360 
LLEEIDCTEE EMLIFAALQY HISKLSQCAE IQDFATKSEV DEVEAALSSL EVTLEGGKAD 

       370        380        390        400        410        420 
NTLEDITDIP KLADYLKLFR PKKLMLKACK QYWFVFKDTS IAYFKNKELE QGEPIEKLNL 

       430        440        450        460        470        480 
RGCEIVPDVN VSGRKFGIKL LIPVADGMNE VYLRCDHEDQ YARWMAACIL ASKGKTMADS 

       490        500        510        520        530        540 
SYQPEVISIL SFLKMKNRNS SPLVASSLEN MDMNPECLVS PCCAKKHKSK QLAARILEAH 

       550        560        570        580        590        600 
HNVAQMPLVE AKLQFIQAWQ SLPEFGLTYY LVRFKGSKKD DILGVAYNRL IRIDAVTGIP 

       610        620        630        640        650        660 
VTTWRFANMK QWNVNWEIRQ VAIEFDQNVS IAFTCLSADC KIVHEYIGGY IFLSTRSKDQ 

       670 
NETLDEDLFH KLTGGQD 

« Hide

References

« Hide 'large scale' references
[1]"Lineage-specific biology revealed by a finished genome assembly of the mouse."
Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S. expand/collapse author list , Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K., Eichler E.E., Ponting C.P.
PLoS Biol. 7:E1000112-E1000112(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C57BL/6J.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-152 AND 448-677.
Tissue: Mammary fibroblast.
[3]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-677.
Strain: C57BL/6J.
[4]"Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal epithelial dysfunction."
Ussar S., Moser M., Widmaier M., Rognoni E., Harrer C., Genzel-Boroviczeny O., Fassler R.
PLoS Genet. 4:E1000289-E1000289(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: DISRUPTION PHENOTYPE.
[5]"The structure of the N-terminus of kindlin-1: a domain important for alphaIIbbeta3 integrin activation."
Goult B.T., Bouaouina M., Harburger D.S., Bate N., Patel B., Anthis N.J., Campbell I.D., Calderwood D.A., Barsukov I.L., Roberts G.C., Critchley D.R.
J. Mol. Biol. 394:944-956(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 1-96, DOMAIN FERM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL831763 Genomic DNA. Translation: CAM20382.1.
BC029093 mRNA. Translation: AAH29093.1. Different initiation.
BC042792 mRNA. No translation available.
AK050804 mRNA. Translation: BAC34417.1.
RefSeqNP_932146.2. NM_198029.2.
UniGeneMm.209784.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2KMCNMR-A1-96[»]
4BBKX-ray2.10A364-509[»]
DisProtDP00655.
ProteinModelPortalP59113.
SMRP59113. Positions 1-138, 266-324, 370-497, 525-651.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP59113. 1 interaction.
MINTMINT-4139673.

PTM databases

PhosphoSiteP59113.

Proteomic databases

PaxDbP59113.
PRIDEP59113.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000038280; ENSMUSP00000047616; ENSMUSG00000027356.
GeneID241639.
KEGGmmu:241639.
UCSCuc008mno.1. mouse.

Organism-specific databases

CTD55612.
MGIMGI:2443583. Fermt1.

Phylogenomic databases

eggNOGNOG238024.
GeneTreeENSGT00390000013444.
HOGENOMHOG000231715.
HOVERGENHBG020688.
InParanoidA2ANX1.
KOK17082.
OMAVSPRCAK.
OrthoDBEOG7T7GSC.
TreeFamTF314677.

Gene expression databases

BgeeP59113.
GenevestigatorP59113.

Family and domain databases

Gene3D1.20.80.10. 2 hits.
2.30.29.30. 2 hits.
InterProIPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF00373. FERM_M. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]
SMARTSM00295. B41. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]
SUPFAMSSF47031. SSF47031. 1 hit.
PROSITEPS00661. FERM_2. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP59113.
NextBio385110.
PROP59113.
SOURCESearch...

Entry information

Entry nameFERM1_MOUSE
AccessionPrimary (citable) accession number: P59113
Secondary accession number(s): A2ANX1, Q8BQG6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 6, 2002
Last sequence update: July 27, 2011
Last modified: April 16, 2014
This is version 103 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot