FERM1_HUMAN
ID FERM1_HUMAN Reviewed; 677 AA.
AC Q9BQL6; D3DW10; Q8IX34; Q8IYH2; Q9NWM2; Q9NXQ3;
DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Fermitin family homolog 1;
DE AltName: Full=Kindlerin;
DE AltName: Full=Kindlin syndrome protein;
DE AltName: Full=Kindlin-1;
DE AltName: Full=Unc-112-related protein 1;
GN Name=FERMT1; Synonyms=C20orf42, KIND1, URP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANT
RP LYS-526.
RC TISSUE=Colon cancer;
RX PubMed=12697302; DOI=10.1016/s0925-4439(03)00035-8;
RA Weinstein E.J., Bourner M., Head R., Zakeri H., Bauer C., Mazzarella R.;
RT "URP1: a member of a novel family of PH and FERM domain-containing
RT membrane-associated proteins is significantly over-expressed in lung and
RT colon carcinomas.";
RL Biochim. Biophys. Acta 1637:207-216(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INVOLVEMENT IN KNDLRS, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=12789646; DOI=10.1086/376609;
RA Siegel D.H., Ashton G.H.S., Penagos H.G., Lee J.V., Feiler H.S.,
RA Wilhelmsen K.C., South A.P., Smith F.J.D., Prescott A.R., Wessagowit V.,
RA Oyama N., Akiyama M., Al-Aboud D., Al-Aboud K., Al-Githami A.,
RA Al-Hawsawi K., Al-Ismaily A., Al-Suwaid R., Atherton D.J., Caputo R.,
RA Fine J.-D., Frieden I.J., Fuchs E., Haber R.M., Harada T., Kitajima Y.,
RA Mallory S.B., Ogawa H., Sahin S., Shimizu H., Suga Y., Tadini G.,
RA Tsuchiya K., Wiebe C.B., Wojnarowska F., Zaghloul A.B., Hamada T.,
RA Mallipeddi R., Eady R.A.J., McLean W.H.I., McGrath J.A., Epstein E.H. Jr.;
RT "Loss of kindlin-1, a human homolog of the Caenorhabditis elegans actin-
RT extracellular-matrix linker protein UNC-112, causes Kindler syndrome.";
RL Am. J. Hum. Genet. 73:174-187(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3), PARTIAL NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT LYS-526.
RC TISSUE=Colon, Hepatoma, and Teratocarcinoma;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
RC TISSUE=Brain;
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 project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP INVOLVEMENT IN KNDLRS, AND TISSUE SPECIFICITY.
RX PubMed=12668616; DOI=10.1093/hmg/ddg097;
RA Jobard F., Bouadjar B., Caux F., Hadj-Rabia S., Has C., Matsuda F.,
RA Weissenbach J., Lathrop M., Prud'homme J.-F., Fischer J.;
RT "Identification of mutations in a new gene encoding a FERM family protein
RT with a pleckstrin homology domain in Kindler syndrome.";
RL Hum. Mol. Genet. 12:925-935(2003).
RN [8]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INDUCTION, AND
RP INTERACTION WITH ITGB1 AND ITGB3.
RX PubMed=14634021; DOI=10.1074/jbc.m307978200;
RA Kloeker S., Major M.B., Calderwood D.A., Ginsberg M.H., Jones D.A.,
RA Beckerle M.C.;
RT "The Kindler syndrome protein is regulated by transforming growth factor-
RT beta and involved in integrin-mediated adhesion.";
RL J. Biol. Chem. 279:6824-6833(2004).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND PHOSPHORYLATION.
RX PubMed=17012746; DOI=10.1074/jbc.m606259200;
RA Herz C., Aumailley M., Schulte C., Schlotzer-Schrehardt U.,
RA Bruckner-Tuderman L., Has C.;
RT "Kindlin-1 is a phosphoprotein involved in regulation of polarity,
RT proliferation, and motility of epidermal keratinocytes.";
RL J. Biol. Chem. 281:36082-36090(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND SER-179, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP FUNCTION, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=19804783; DOI=10.1016/j.jmb.2009.09.061;
RA Goult B.T., Bouaouina M., Harburger D.S., Bate N., Patel B., Anthis N.J.,
RA Campbell I.D., Calderwood D.A., Barsukov I.L., Roberts G.C.,
RA 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).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-361, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [15]
RP VARIANTS KNDLRS ARG-100 DEL; PRO-400; ARG-559 AND ILE-623 DEL.
RX PubMed=21936020; DOI=10.1002/humu.21576;
RA Has C., Castiglia D., del Rio M., Diez M.G., Piccinni E., Kiritsi D.,
RA Kohlhase J., Itin P., Martin L., Fischer J., Zambruno G.,
RA Bruckner-Tuderman L.;
RT "Kindler syndrome: extension of FERMT1 mutational spectrum and natural
RT history.";
RL Hum. Mutat. 32:1204-1212(2011).
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 for
CC normal polarization of basal keratinocytes in skin, and for normal cell
CC shape. Required for normal adhesion of keratinocytes to fibronectin and
CC laminin, and for normal keratinocyte migration to wound sites. May
CC mediate TGF-beta 1 signaling in tumor progression.
CC {ECO:0000269|PubMed:14634021, ECO:0000269|PubMed:17012746,
CC ECO:0000269|PubMed:19804783}.
CC -!- SUBUNIT: Interacts with the cytoplasmic domain of integrins ITGB1 and
CC ITGB3. {ECO:0000269|PubMed:14634021}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton. Cell junction, focal
CC adhesion. Cell projection, ruffle membrane; Peripheral membrane
CC protein; Cytoplasmic side. Note=Constituent of focal adhesions.
CC Localized at the basal aspect of skin keratinocytes, close to the cell
CC membrane. Colocalizes with filamentous actin. Upon TGFB1 treatment, it
CC localizes to membrane ruffles.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9BQL6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BQL6-2; Sequence=VSP_003810, VSP_003811;
CC Name=3;
CC IsoId=Q9BQL6-3; Sequence=VSP_003809;
CC Name=4;
CC IsoId=Q9BQL6-4; Sequence=VSP_009224, VSP_009225;
CC -!- TISSUE SPECIFICITY: Expressed in brain, skeletal muscle, kidney, colon,
CC adrenal gland, prostate, and placenta. Weakly or not expressed in
CC heart, thymus, spleen, liver, small intestine, bone marrow, lung and
CC peripheral blood leukocytes. Overexpressed in some colon and lung
CC tumors. In skin, it is localized within the epidermis and particularly
CC in basal keratocytes. Not detected in epidermal melanocytes and dermal
CC fibroblasts. {ECO:0000269|PubMed:12668616, ECO:0000269|PubMed:12697302,
CC ECO:0000269|PubMed:12789646, ECO:0000269|PubMed:14634021,
CC ECO:0000269|PubMed:17012746}.
CC -!- INDUCTION: By TGFB1. {ECO:0000269|PubMed:14634021}.
CC -!- DOMAIN: The FERM domain is not correctly detected by PROSITE or Pfam
CC techniques because it contains the insertion of a PH domain. The FERM
CC domain contains the subdomains F1, F2 and F3. It is preceded by a F0
CC domain with a ubiquitin-like fold. The F0 domain is required for
CC integrin activation and for localization at focal adhesions.
CC {ECO:0000269|PubMed:19804783}.
CC -!- DISEASE: Kindler syndrome (KNDLRS) [MIM:173650]: An autosomal recessive
CC skin disorder characterized by skin blistering, photosensitivity,
CC progressive poikiloderma, and extensive skin atrophy. Additional
CC clinical features include gingival erosions, ocular, esophageal,
CC gastrointestinal and urogenital involvement, and an increased risk of
CC mucocutaneous malignancy. {ECO:0000269|PubMed:12668616,
CC ECO:0000269|PubMed:12789646, ECO:0000269|PubMed:21936020}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry. Although most FERMT1 mutations are predicted to lead to
CC premature termination of translation, and to loss of FERMT1 function,
CC significant clinical variability is observed among patients. There is
CC an association of FERMT1 missense and in-frame deletion mutations with
CC milder disease phenotypes, and later onset of complications
CC (PubMed:21936020). {ECO:0000269|PubMed:21936020}.
CC -!- SIMILARITY: Belongs to the kindlin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91358.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC03826.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF443278; AAN75822.1; -; mRNA.
DR EMBL; AY137240; AAM94174.1; -; mRNA.
DR EMBL; AK000123; BAA90957.1; -; mRNA.
DR EMBL; AK000747; BAA91358.1; ALT_INIT; mRNA.
DR EMBL; AK092195; BAC03826.1; ALT_INIT; mRNA.
DR EMBL; AL118505; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471133; EAX10392.1; -; Genomic_DNA.
DR EMBL; CH471133; EAX10393.1; -; Genomic_DNA.
DR EMBL; BC035882; AAH35882.1; -; mRNA.
DR CCDS; CCDS13098.1; -. [Q9BQL6-1]
DR RefSeq; NP_060141.3; NM_017671.4. [Q9BQL6-1]
DR AlphaFoldDB; Q9BQL6; -.
DR SMR; Q9BQL6; -.
DR BioGRID; 120752; 34.
DR IntAct; Q9BQL6; 12.
DR MINT; Q9BQL6; -.
DR STRING; 9606.ENSP00000217289; -.
DR GlyGen; Q9BQL6; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9BQL6; -.
DR PhosphoSitePlus; Q9BQL6; -.
DR BioMuta; FERMT1; -.
DR DMDM; 26392456; -.
DR EPD; Q9BQL6; -.
DR jPOST; Q9BQL6; -.
DR MassIVE; Q9BQL6; -.
DR MaxQB; Q9BQL6; -.
DR PaxDb; Q9BQL6; -.
DR PeptideAtlas; Q9BQL6; -.
DR PRIDE; Q9BQL6; -.
DR ProteomicsDB; 78697; -. [Q9BQL6-1]
DR ProteomicsDB; 78698; -. [Q9BQL6-2]
DR ProteomicsDB; 78699; -. [Q9BQL6-3]
DR ProteomicsDB; 78700; -. [Q9BQL6-4]
DR Antibodypedia; 8379; 238 antibodies from 27 providers.
DR DNASU; 55612; -.
DR Ensembl; ENST00000217289.9; ENSP00000217289.4; ENSG00000101311.16. [Q9BQL6-1]
DR GeneID; 55612; -.
DR KEGG; hsa:55612; -.
DR MANE-Select; ENST00000217289.9; ENSP00000217289.4; NM_017671.5; NP_060141.3.
DR UCSC; uc002wmr.3; human. [Q9BQL6-1]
DR CTD; 55612; -.
DR DisGeNET; 55612; -.
DR GeneCards; FERMT1; -.
DR GeneReviews; FERMT1; -.
DR HGNC; HGNC:15889; FERMT1.
DR HPA; ENSG00000101311; Tissue enhanced (intestine).
DR MalaCards; FERMT1; -.
DR MIM; 173650; phenotype.
DR MIM; 607900; gene.
DR neXtProt; NX_Q9BQL6; -.
DR OpenTargets; ENSG00000101311; -.
DR Orphanet; 2908; Kindler epidermolysis bullosa.
DR PharmGKB; PA162388314; -.
DR VEuPathDB; HostDB:ENSG00000101311; -.
DR eggNOG; KOG3727; Eukaryota.
DR GeneTree; ENSGT00390000013444; -.
DR HOGENOM; CLU_011611_0_0_1; -.
DR InParanoid; Q9BQL6; -.
DR OMA; EDQYARW; -.
DR PhylomeDB; Q9BQL6; -.
DR TreeFam; TF314677; -.
DR PathwayCommons; Q9BQL6; -.
DR SignaLink; Q9BQL6; -.
DR SIGNOR; Q9BQL6; -.
DR BioGRID-ORCS; 55612; 42 hits in 1078 CRISPR screens.
DR ChiTaRS; FERMT1; human.
DR GeneWiki; C20orf42; -.
DR GenomeRNAi; 55612; -.
DR Pharos; Q9BQL6; Tbio.
DR PRO; PR:Q9BQL6; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9BQL6; protein.
DR Bgee; ENSG00000101311; Expressed in mucosa of sigmoid colon and 164 other tissues.
DR ExpressionAtlas; Q9BQL6; baseline and differential.
DR Genevisible; Q9BQL6; HS.
DR GO; GO:0030054; C:cell junction; IDA:UniProtKB.
DR GO; GO:0071944; C:cell periphery; IDA:ARUK-UCL.
DR GO; GO:0030055; C:cell-substrate junction; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IDA:ARUK-UCL.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; IDA:ARUK-UCL.
DR GO; GO:0032587; C:ruffle membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0051015; F:actin filament binding; IEA:Ensembl.
DR GO; GO:0005178; F:integrin binding; IBA:GO_Central.
DR GO; GO:0071711; P:basement membrane organization; IEA:Ensembl.
DR GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR GO; GO:0007160; P:cell-matrix adhesion; IBA:GO_Central.
DR GO; GO:0090162; P:establishment of epithelial cell polarity; IDA:UniProtKB.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:InterPro.
DR GO; GO:0051546; P:keratinocyte migration; IDA:UniProtKB.
DR GO; GO:0043616; P:keratinocyte proliferation; IDA:UniProtKB.
DR GO; GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IEA:Ensembl.
DR GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR GO; GO:0042308; P:negative regulation of protein import into nucleus; IEA:Ensembl.
DR GO; GO:2000647; P:negative regulation of stem cell proliferation; IEA:Ensembl.
DR GO; GO:0051886; P:negative regulation of timing of anagen; IEA:Ensembl.
DR GO; GO:0033630; P:positive regulation of cell adhesion mediated by integrin; IEA:Ensembl.
DR GO; GO:0001954; P:positive regulation of cell-matrix adhesion; IEA:Ensembl.
DR GO; GO:0033625; P:positive regulation of integrin activation; IGI:ARUK-UCL.
DR GO; GO:0071636; P:positive regulation of transforming growth factor beta production; IEA:Ensembl.
DR GO; GO:0030511; P:positive regulation of transforming growth factor beta receptor signaling pathway; IEA:Ensembl.
DR GO; GO:1903691; P:positive regulation of wound healing, spreading of epidermal cells; IGI:ARUK-UCL.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd01237; PH_fermitin; 1.
DR Gene3D; 2.30.29.30; -; 2.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR037843; Kindlin/fermitin.
DR InterPro; IPR040790; Kindlin_2_N.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR037837; PH_Kindlin/fermitin.
DR PANTHER; PTHR16160; PTHR16160; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF18124; Kindlin_2_N; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00295; B41; 1.
DR SMART; SM00233; PH; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell junction; Cell membrane;
KW Cell projection; Cytoplasm; Cytoskeleton; Disease variant; Membrane;
KW Phosphoprotein; Reference proteome.
FT CHAIN 1..677
FT /note="Fermitin family homolog 1"
FT /id="PRO_0000219452"
FT DOMAIN 96..653
FT /note="FERM"
FT DOMAIN 377..473
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 179
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..447
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_003809"
FT VAR_SEQ 458..495
FT /note="ENQYAQWMAACMLASKGKTMADSSYQPEVLNILSFLRM -> VSKTPKILSH
FT FTSTKPKSKTQKCFHKFRALLCHSAIAL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009224"
FT VAR_SEQ 496..677
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_009225"
FT VAR_SEQ 541..554
FT /note="QNVAQMPLVEAKLR -> LQAPFHSYRSLSHL (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003810"
FT VAR_SEQ 555..677
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000305"
FT /id="VSP_003811"
FT VARIANT 100
FT /note="Missing (in KNDLRS)"
FT /evidence="ECO:0000269|PubMed:21936020"
FT /id="VAR_066942"
FT VARIANT 160
FT /note="I -> T (in dbSNP:rs16991866)"
FT /id="VAR_048368"
FT VARIANT 241
FT /note="V -> A (in dbSNP:rs55666319)"
FT /id="VAR_061035"
FT VARIANT 400
FT /note="S -> P (in KNDLRS; dbSNP:rs869312718)"
FT /evidence="ECO:0000269|PubMed:21936020"
FT /id="VAR_066943"
FT VARIANT 526
FT /note="R -> K (in dbSNP:rs2232074)"
FT /evidence="ECO:0000269|PubMed:12697302,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_014398"
FT VARIANT 534
FT /note="A -> T (in dbSNP:rs2232078)"
FT /id="VAR_014399"
FT VARIANT 559
FT /note="W -> R (in KNDLRS; dbSNP:rs869312719)"
FT /evidence="ECO:0000269|PubMed:21936020"
FT /id="VAR_066944"
FT VARIANT 623
FT /note="Missing (in KNDLRS; dbSNP:rs869312721)"
FT /evidence="ECO:0000269|PubMed:21936020"
FT /id="VAR_066945"
FT CONFLICT 117
FT /note="V -> A (in Ref. 4; BAC03826)"
FT /evidence="ECO:0000305"
FT CONFLICT 262
FT /note="I -> T (in Ref. 4; BAC03826)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 677 AA; 77437 MW; 7354DCD84C516F90 CRC64;
MLSSTDFTFA SWELVVRVDH PNEEQQKDVT LRVSGDLHVG GVMLKLVEQI NISQDWSDFA
LWWEQKHCWL LKTHWTLDKY GVQADAKLLF TPQHKMLRLR LPNLKMVRLR VSFSAVVFKA
VSDICKILNI RRSEELSLLK PSGDYFKKKK KKDKNNKEPI IEDILNLESS PTASGSSVSP
GLYSKTMTPI YDPINGTPAS STMTWFSDSP LTEQNCSILA FSQPPQSPEA LADMYQPRSL
VDKAKLNAGW LDSSRSLMEQ GIQEDEQLLL RFKYYSFFDL NPKYDAVRIN QLYEQARWAI
LLEEIDCTEE EMLIFAALQY HISKLSLSAE TQDFAGESEV DEIEAALSNL EVTLEGGKAD
SLLEDITDIP KLADNLKLFR PKKLLPKAFK QYWFIFKDTS IAYFKNKELE QGEPLEKLNL
RGCEVVPDVN VAGRKFGIKL LIPVADGMNE MYLRCDHENQ YAQWMAACML ASKGKTMADS
SYQPEVLNIL SFLRMKNRNS ASQVASSLEN MDMNPECFVS PRCAKRHKSK QLAARILEAH
QNVAQMPLVE AKLRFIQAWQ SLPEFGLTYY LVRFKGSKKD DILGVSYNRL IKIDAATGIP
VTTWRFTNIK QWNVNWETRQ VVIEFDQNVF TAFTCLSADC KIVHEYIGGY IFLSTRSKDQ
NETLDEDLFH KLTGGQD
