ID FERM1_MOUSE Reviewed; 677 AA. AC P59113; A2ANX1; Q8BQG6; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 27-JUL-2011, sequence version 4. DT 15-FEB-2017, entry version 122. DE RecName: Full=Fermitin family homolog 1; DE AltName: Full=Kindlin-1; DE AltName: Full=Unc-112-related protein 1; GN Name=Fermt1; Synonyms=Kind1, Urp1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=C57BL/6J; RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112; RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., RA She X., Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., RA Kapustin Y., Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., RA Zhou S., Teague B., Potamousis K., Churas C., Place M., Herschleb J., RA Runnheim R., Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., RA Lindblad-Toh K., Eichler E.E., Ponting C.P.; RT "Lineage-specific biology revealed by a finished genome assembly of RT the mouse."; RL PLoS Biol. 7:E1000112-E1000112(2009). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-152 AND 448-677. RC TISSUE=Mammary fibroblast; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 41-677. RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP DISRUPTION PHENOTYPE. RX PubMed=19057668; DOI=10.1371/journal.pgen.1000289; RA Ussar S., Moser M., Widmaier M., Rognoni E., Harrer C., RA Genzel-Boroviczeny O., Fassler R.; RT "Loss of Kindlin-1 causes skin atrophy and lethal neonatal intestinal RT epithelial dysfunction."; RL PLoS Genet. 4:E1000289-E1000289(2008). RN [5] RP STRUCTURE BY NMR OF 1-96, AND DOMAIN FERM. RX PubMed=19804783; DOI=10.1016/j.jmb.2009.09.061; RA Goult B.T., Bouaouina M., Harburger D.S., Bate N., Patel B., RA Anthis N.J., Campbell I.D., Calderwood D.A., Barsukov I.L., RA Roberts G.C., Critchley D.R.; RT "The structure of the N-terminus of kindlin-1: a domain important for RT alphaIIbbeta3 integrin activation."; RL J. Mol. Biol. 394:944-956(2009). CC -!- FUNCTION: Involved in cell adhesion. Contributes to integrin CC activation. When coexpressed with talin, potentiates activation of CC ITGA2B. Required for normal keratinocyte proliferation. Required CC for normal polarization of basal keratinocytes in skin, and for CC normal cell shape. Required for normal adhesion of keratinocytes CC to fibronectin and laminin, and for normal keratinocyte migration CC to wound sites (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Interacts with the cytoplasmic domain of integrins ITGB1 CC and ITGB3. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton {ECO:0000250}. Cell CC junction, focal adhesion {ECO:0000250}. Cell projection, ruffle CC membrane {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; CC Cytoplasmic side {ECO:0000250}. Note=Colocalizes with filamentous CC actin. Constituent of focal adhesions (By similarity). Localized CC at the basal aspect of skin keratinocytes, close to the cell CC membrane (By similarity). Upon TGFB1 treatment, it localizes to CC membrane ruffles (By similarity). {ECO:0000250}. CC -!- DOMAIN: The FERM domain is not correctly detected by PROSITE or CC Pfam techniques because it contains the insertion of a PH domain. CC The FERM domain contains the subdomains F1, F2 and F3. It is CC preceded by a F0 domain with a ubiquitin-like fold. The F0 domain CC is required for integrin activation and for localization at focal CC adhesions (By similarity). {ECO:0000250}. CC -!- DISRUPTION PHENOTYPE: Mice are born with the expected Mendelian CC distribution and appear normal at birth, but fail to thrive, CC become dehydrated and die after three to five days. They develop CC skin atrophy and die due to a lethal intestinal epithelial CC dysfunction. The colon is shortened and swollen and presents signs CC of acute inflammation. At the time of death, about 80% of the CC colonic epithelium is detached. {ECO:0000269|PubMed:19057668}. CC -!- SIMILARITY: Belongs to the kindlin family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH29093.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AL831763; CAM20382.1; -; Genomic_DNA. DR EMBL; BC029093; AAH29093.1; ALT_INIT; mRNA. DR EMBL; BC042792; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK050804; BAC34417.1; -; mRNA. DR CCDS; CCDS38248.1; -. DR RefSeq; NP_932146.2; NM_198029.2. DR RefSeq; XP_017173695.1; XM_017318206.1. DR RefSeq; XP_017173696.1; XM_017318207.1. DR RefSeq; XP_017173699.1; XM_017318210.1. DR UniGene; Mm.209784; -. DR PDB; 2KMC; NMR; -; A=1-96. DR PDB; 4BBK; X-ray; 2.10 A; A=364-509. DR PDBsum; 2KMC; -. DR PDBsum; 4BBK; -. DR DisProt; DP00655; -. DR ProteinModelPortal; P59113; -. DR SMR; P59113; -. DR IntAct; P59113; 1. DR MINT; MINT-4139673; -. DR STRING; 10090.ENSMUSP00000047616; -. DR iPTMnet; P59113; -. DR PhosphoSitePlus; P59113; -. DR MaxQB; P59113; -. DR PaxDb; P59113; -. DR PeptideAtlas; P59113; -. DR PRIDE; P59113; -. DR Ensembl; ENSMUST00000038280; ENSMUSP00000047616; ENSMUSG00000027356. DR GeneID; 241639; -. DR KEGG; mmu:241639; -. DR UCSC; uc008mno.1; mouse. DR CTD; 55612; -. DR MGI; MGI:2443583; Fermt1. DR eggNOG; KOG3727; Eukaryota. DR eggNOG; ENOG410XS1B; LUCA. DR GeneTree; ENSGT00390000013444; -. DR HOGENOM; HOG000231715; -. DR HOVERGEN; HBG020688; -. DR InParanoid; P59113; -. DR KO; K17082; -. DR OMA; FKQYWFI; -. DR OrthoDB; EOG090B037N; -. DR TreeFam; TF314677; -. DR EvolutionaryTrace; P59113; -. DR PRO; PR:P59113; -. DR Proteomes; UP000000589; Chromosome 2. DR Bgee; ENSMUSG00000027356; -. DR GO; GO:0030054; C:cell junction; ISS:UniProtKB. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005829; C:cytosol; ISS:UniProtKB. DR GO; GO:0005925; C:focal adhesion; IDA:MGI. DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell. DR GO; GO:0007155; P:cell adhesion; ISS:UniProtKB. DR GO; GO:0090162; P:establishment of epithelial cell polarity; ISS:UniProtKB. DR GO; GO:0051546; P:keratinocyte migration; ISS:UniProtKB. DR GO; GO:0043616; P:keratinocyte proliferation; ISS:UniProtKB. DR Gene3D; 1.20.80.10; -; 2. DR Gene3D; 2.30.29.30; -; 2. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_3-hlx. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR011993; PH_dom-like. DR InterPro; IPR001849; PH_domain. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00295; B41; 1. DR SMART; SM00233; PH; 1. DR SUPFAM; SSF47031; SSF47031; 1. DR SUPFAM; SSF50729; SSF50729; 2. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50003; PH_DOMAIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell adhesion; Cell junction; Cell membrane; KW Cell projection; Complete proteome; Cytoplasm; Cytoskeleton; Membrane; KW Phosphoprotein; Reference proteome. FT CHAIN 1 677 Fermitin family homolog 1. FT /FTId=PRO_0000219453. FT DOMAIN 96 653 FERM. FT DOMAIN 377 473 PH. {ECO:0000255|PROSITE- FT ProRule:PRU00145}. FT COMPBIAS 147 154 Poly-Lys. FT MOD_RES 170 170 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BQL6}. FT MOD_RES 179 179 Phosphoserine. FT {ECO:0000250|UniProtKB:Q9BQL6}. FT CONFLICT 522 522 C -> R (in Ref. 2; AAH29093). FT {ECO:0000305}. FT CONFLICT 586 586 A -> S (in Ref. 2; AAH29093). FT {ECO:0000305}. FT STRAND 1 5 {ECO:0000244|PDB:2KMC}. FT STRAND 12 19 {ECO:0000244|PDB:2KMC}. FT STRAND 26 33 {ECO:0000244|PDB:2KMC}. FT HELIX 39 50 {ECO:0000244|PDB:2KMC}. FT STRAND 57 63 {ECO:0000244|PDB:2KMC}. FT TURN 64 67 {ECO:0000244|PDB:2KMC}. FT STRAND 68 70 {ECO:0000244|PDB:2KMC}. FT HELIX 77 80 {ECO:0000244|PDB:2KMC}. FT STRAND 88 92 {ECO:0000244|PDB:2KMC}. FT STRAND 372 379 {ECO:0000244|PDB:4BBK}. FT STRAND 390 397 {ECO:0000244|PDB:4BBK}. FT STRAND 400 406 {ECO:0000244|PDB:4BBK}. FT HELIX 407 409 {ECO:0000244|PDB:4BBK}. FT STRAND 415 419 {ECO:0000244|PDB:4BBK}. FT STRAND 424 430 {ECO:0000244|PDB:4BBK}. FT TURN 431 434 {ECO:0000244|PDB:4BBK}. FT STRAND 435 444 {ECO:0000244|PDB:4BBK}. FT STRAND 447 457 {ECO:0000244|PDB:4BBK}. FT HELIX 458 472 {ECO:0000244|PDB:4BBK}. FT HELIX 482 496 {ECO:0000244|PDB:4BBK}. SQ SEQUENCE 677 AA; 76941 MW; 9B8B1876FA7621EE CRC64; MLSSGDLTSA SWELVVRVDH ANGEQQTEIT LRVSGDLHIG GVMLKLVEQM NIAQDWSDYA LWWEQKRCWL LKTHWTLDKC GVQADANLLF TPQHKMLRLR LPNAKTVRLR VSFSAVVFKA VADICKVLNI RRPEELSLLK PSSDYCKKKK KKEKNSKEPV IEDILNLESS STSSGSPVSP GLYSKTMTPT YDPINGTPAL STMTWFGDSP LTEQNCSVLA FSQPPPSPDV LADMFQPRSL VDKAKMNAGW LDSSRSLMEQ SIQEDEQLQL RFKYYTFFDL NPKYDAVRIN QLYEQARWAV LLEEIDCTEE EMLIFAALQY HISKLSQCAE IQDFATKSEV DEVEAALSSL EVTLEGGKAD NTLEDITDIP KLADYLKLFR PKKLMLKACK QYWFVFKDTS IAYFKNKELE QGEPIEKLNL RGCEIVPDVN VSGRKFGIKL LIPVADGMNE VYLRCDHEDQ YARWMAACIL ASKGKTMADS SYQPEVISIL SFLKMKNRNS SPLVASSLEN MDMNPECLVS PCCAKKHKSK QLAARILEAH HNVAQMPLVE AKLQFIQAWQ SLPEFGLTYY LVRFKGSKKD DILGVAYNRL IRIDAVTGIP VTTWRFANMK QWNVNWEIRQ VAIEFDQNVS IAFTCLSADC KIVHEYIGGY IFLSTRSKDQ NETLDEDLFH KLTGGQD //