ID FERM1_MOUSE Reviewed; 677 AA. AC P59113; Q8BQG6; DT 06-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 3. DT 13-OCT-2009, entry version 66. DE RecName: Full=Fermitin family homolog 1; DE AltName: Full=Unc-112-related protein 1; DE AltName: Full=Kindlin-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. OX NCBI_TaxID=10090; RN [1] 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 [2] 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). CC -!- FUNCTION: Involved in cell adhesion, possibly via its interaction CC with integrins (By similarity). CC -!- SUBUNIT: Interacts with the cytoplasmic domain of integrins ITGB1 CC and ITGB3 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton (By similarity). CC Cell junction, focal adhesion (By similarity). Cell projection, CC ruffle membrane; Peripheral membrane protein; Cytoplasmic side (By CC similarity). Note=Colocalizes with filamentous actin. Constituent CC of focal adhesions (By similarity). Upon TGFB1 treatment, it CC localizes to membrane ruffles (By similarity). 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 -!- SIMILARITY: Belongs to the kindlin family. CC -!- SIMILARITY: Contains 1 FERM domain. CC -!- SIMILARITY: Contains 1 PH domain. 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; BC029093; AAH29093.1; ALT_INIT; mRNA. DR EMBL; BC042792; -; NOT_ANNOTATED_CDS; mRNA. DR EMBL; AK050804; BAC34417.1; -; mRNA. DR IPI; IPI00670967; -. DR RefSeq; NP_932146.2; -. DR UniGene; Mm.209784; -. DR STRING; P59113; -. DR PhosphoSite; P59113; -. DR PRIDE; P59113; -. DR Ensembl; ENSMUST00000038280; ENSMUSP00000047616; ENSMUSG00000027356; Mus musculus. DR GeneID; 241639; -. DR KEGG; mmu:241639; -. DR UCSC; uc008mno.1; mouse. DR CTD; 241639; -. DR MGI; MGI:2443583; Fermt1. DR HOGENOM; P59113; -. DR HOVERGEN; P59113; -. DR NextBio; 385110; -. DR ArrayExpress; P59113; -. DR Bgee; P59113; -. DR Genevestigator; P59113; -. DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW. DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell. DR GO; GO:0005925; C:focal adhesion; IDA:MGI. DR GO; GO:0009898; C:internal side of plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005515; F:protein binding; IEA:UniProtKB-KW. DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW. DR InterPro; IPR019749; Band_41_domain. DR InterPro; IPR019748; FERM_central. DR InterPro; IPR019747; FERM_CS. DR InterPro; IPR011993; PH_type. DR InterPro; IPR001849; Pleckstrin_homology. DR Gene3D; G3DSA:2.30.29.30; PH_type; 1. DR Pfam; PF00373; FERM_M; 1. DR Pfam; PF00169; PH; 1. DR SMART; SM00295; B41; 1. DR SMART; SM00233; PH; 1. DR PROSITE; PS00660; FERM_1; FALSE_NEG. DR PROSITE; PS00661; FERM_2; 1. DR PROSITE; PS50057; FERM_3; FALSE_NEG. DR PROSITE; PS50003; PH_DOMAIN; 1. PE 2: Evidence at transcript level; KW Cell adhesion; Cell junction; Cell membrane; Cell projection; KW Cytoplasm; Cytoskeleton; Membrane; Phosphoprotein. FT CHAIN 1 677 Fermitin family homolog 1. FT /FTId=PRO_0000219453. FT DOMAIN 250 570 FERM. FT DOMAIN 377 473 PH. FT COMPBIAS 147 154 Poly-Lys. FT MOD_RES 170 170 Phosphoserine (By similarity). FT MOD_RES 179 179 Phosphoserine (By similarity). FT CONFLICT 522 522 R -> C (in Ref. 2; BAC34417). FT CONFLICT 586 586 S -> A (in Ref. 2; BAC34417). SQ SEQUENCE 677 AA; 77010 MW; 826E62DF73C5A1DD 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 PRCAKKHKSK QLAARILEAH HNVAQMPLVE AKLQFIQAWQ SLPEFGLTYY LVRFKGSKKD DILGVSYNRL IRIDAVTGIP VTTWRFANMK QWNVNWEIRQ VAIEFDQNVS IAFTCLSADC KIVHEYIGGY IFLSTRSKDQ NETLDEDLFH KLTGGQD //