P59113 (FERM1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Fermitin family homolog 1

Alternative name(s):
Kindlin-1
Unc-112-related protein 1

Gene names

Name:	Fermt1
Synonyms:	Kind1, Urp1

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	677 AA.
Sequence status	Complete.
Protein existence	Evidence 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	Cytoplasm › cytoskeleton By similarity. Cell junction › focal adhesion By similarity. Cell projection › ruffle 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.

Ontologies

Keywords
Biological process	Cell adhesion
Cellular component	Cell junction Cell membrane Cell projection Cytoplasm Cytoskeleton Membrane
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell adhesion Inferred from sequence or structural similarity. Source: UniProtKB establishment of epithelial cell polarity Inferred from sequence or structural similarity. Source: UniProtKB keratinocyte migration Inferred from sequence or structural similarity. Source: UniProtKB keratinocyte proliferation Inferred from sequence or structural similarity. Source: UniProtKB
Cellular_component	cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell cytosol Inferred from sequence or structural similarity. Source: UniProtKB focal adhesion Inferred from direct assay PubMed 16876785. Source: MGI ruffle membrane Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 677

677

Fermitin family homolog 1

PRO_0000219453

Regions

Domain

96 – 653

558

FERM

Domain

377 – 473

97

PH

Compositional bias

147 – 154

8

Poly-Lys

Amino acid modifications

Modified residue

170

1

Phosphoserine By similarity

Modified residue

179

1

Phosphoserine By similarity

Experimental info

Sequence conflict

522

1

C → R in AAH29093. Ref.2

Sequence conflict

586

1

A → S in AAH29093. Ref.2

Secondary structure

1

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677

Helix Strand Turn

Details...

Beta strand

1 – 5

5

Beta strand

12 – 19

8

Beta strand

26 – 33

8

Helix

39 – 50

12

Beta strand

57 – 63

7

Turn

64 – 67

4

Beta strand

68 – 70

3

Helix

77 – 80

4

Beta strand

88 – 92

5

Beta strand

372 – 379

8

Beta strand

390 – 397

8

Beta strand

400 – 406

7

Helix

407 – 409

3

Beta strand

415 – 419

5

Beta strand

424 – 430

7

Turn

431 – 434

4

Beta strand

435 – 444

10

Beta strand

447 – 457

11

Helix

458 – 472

15

Helix

482 – 496

15

Sequences

	Sequence		Length	Mass (Da)
	P59113 [UniParc]. Last modified July 27, 2011. Version 4. Checksum: 9B8B1876FA7621EE	FASTA	677	76,941
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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.

IPI

IPI00670967.

RefSeq

NP_932146.2. NM_198029.2.

UniGene

Mm.209784.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2KMC	NMR	-	A	1-96	[»]
4BBK	X-ray	2.10	A	364-509	[»]

ProteinModelPortal

P59113.

SMR

P59113. Positions 1-96, 370-497, 525-651.

ModBase

Search...

Protein-protein interaction databases

MINT

MINT-4139673.

PTM databases

PhosphoSite

P59113.

Proteomic databases

PaxDb

P59113.

PRIDE

P59113.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENSMUST00000038280; ENSMUSP00000047616; ENSMUSG00000027356.

GeneID

241639.

KEGG

mmu:241639.

UCSC

uc008mno.1. mouse.

Organism-specific databases

CTD

55612.

MGI

MGI:2443583. Fermt1.

Phylogenomic databases

eggNOG

NOG238024.

GeneTree

ENSGT00390000013444.

HOGENOM

HOG000231715.

HOVERGEN

HBG020688.

InParanoid

A2ANX1.

OMA

ADSSYQP.

OrthoDB

EOG4RBQJ4.

Gene expression databases

Bgee

P59113.

Genevestigator

P59113.

Family and domain databases

Gene3D

1.20.80.10. 2 hits.
2.30.29.30. 2 hits.

InterPro

IPR019749. Band_41_domain.
IPR014352. FERM/acyl-CoA-bd_prot_3-hlx.
IPR019748. FERM_central.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]

Pfam

PF00373. FERM_M. 1 hit.
PF00169. PH. 1 hit.
[Graphical view]

SMART

SM00295. B41. 1 hit.
SM00233. PH. 1 hit.
[Graphical view]

SUPFAM

SSF47031. FERM_3-hlx. 1 hit.

PROSITE

PS00660. FERM_1. False negative.
PS00661. FERM_2. 1 hit.
PS50057. FERM_3. False negative.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

EvolutionaryTrace

P59113.

NextBio

385110.

SOURCE

Search...

Entry information

Entry name

FERM1_MOUSE

Accession

Primary (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:	May 29, 2013
This is version 94 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program