ID Q497H5_MOUSE Unreviewed; 1309 AA. AC Q497H5; DT 13-SEP-2005, integrated into UniProtKB/TrEMBL. DT 13-SEP-2005, sequence version 1. DT 03-AUG-2022, entry version 114. DE SubName: Full=Fat1 protein {ECO:0000313|EMBL:AAI00555.1}; DE Flags: Fragment; GN Name=Fat1 {ECO:0000313|EMBL:AAI00555.1, ECO:0000313|MGI:MGI:109168}; GN Synonyms=Fath {ECO:0000313|MGI:MGI:109168}; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae; OC Murinae; Mus; Mus. OX NCBI_TaxID=10090 {ECO:0000313|EMBL:AAI00555.1}; RN [1] {ECO:0000313|EMBL:AAI00555.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6 {ECO:0000313|EMBL:AAI00555.1}; RC TISSUE=Brain {ECO:0000313|EMBL:AAI00555.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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). CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00076}. 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; BC100554; AAI00555.1; -; mRNA. DR PeptideAtlas; Q497H5; -. DR MGI; MGI:109168; Fat1. DR ChiTaRS; Fat1; mouse. DR GO; GO:0016324; C:apical plasma membrane; IDA:MGI. DR GO; GO:0030054; C:cell junction; IDA:MGI. DR GO; GO:0005911; C:cell-cell junction; ISO:MGI. DR GO; GO:0030175; C:filopodium; IDA:MGI. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0030027; C:lamellipodium; IDA:MGI. DR GO; GO:0005634; C:nucleus; ISO:MGI. DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:MGI. DR GO; GO:0005886; C:plasma membrane; IDA:MGI. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-UniRule. DR GO; GO:0007015; P:actin filament organization; IMP:MGI. DR GO; GO:0043010; P:camera-type eye development; IMP:MGI. DR GO; GO:0048593; P:camera-type eye morphogenesis; IMP:MGI. DR GO; GO:0098609; P:cell-cell adhesion; IMP:MGI. DR GO; GO:0003382; P:epithelial cell morphogenesis; IMP:MGI. DR GO; GO:0003412; P:establishment of epithelial cell apical/basal polarity involved in camera-type eye morphogenesis; IMP:MGI. DR GO; GO:0007163; P:establishment or maintenance of cell polarity; IMP:MGI. DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IMP:MGI. DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro. DR GO; GO:0002088; P:lens development in camera-type eye; IMP:MGI. DR CDD; cd00110; LamG; 1. DR InterPro; IPR002126; Cadherin-like_dom. DR InterPro; IPR015919; Cadherin-like_sf. DR InterPro; IPR020894; Cadherin_CS. DR InterPro; IPR013320; ConA-like_dom_sf. DR InterPro; IPR001881; EGF-like_Ca-bd_dom. DR InterPro; IPR000742; EGF-like_dom. DR InterPro; IPR000152; EGF-type_Asp/Asn_hydroxyl_site. DR InterPro; IPR018097; EGF_Ca-bd_CS. DR InterPro; IPR009030; Growth_fac_rcpt_cys_sf. DR InterPro; IPR001791; Laminin_G. DR Pfam; PF00028; Cadherin; 2. DR Pfam; PF00008; EGF; 2. DR Pfam; PF07645; EGF_CA; 1. DR Pfam; PF02210; Laminin_G_2; 1. DR PRINTS; PR00205; CADHERIN. DR SMART; SM00112; CA; 4. DR SMART; SM00181; EGF; 5. DR SMART; SM00179; EGF_CA; 4. DR SMART; SM00282; LamG; 1. DR SUPFAM; SSF49313; SSF49313; 4. DR SUPFAM; SSF49899; SSF49899; 1. DR SUPFAM; SSF57184; SSF57184; 1. DR PROSITE; PS00010; ASX_HYDROXYL; 1. DR PROSITE; PS00232; CADHERIN_1; 2. DR PROSITE; PS50268; CADHERIN_2; 4. DR PROSITE; PS00022; EGF_1; 4. DR PROSITE; PS01186; EGF_2; 1. DR PROSITE; PS50026; EGF_3; 5. DR PROSITE; PS01187; EGF_CA; 1. DR PROSITE; PS50025; LAM_G_DOMAIN; 1. PE 2: Evidence at transcript level; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|PROSITE- KW ProRule:PRU00043}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE- KW ProRule:PRU00076}; KW EGF-like domain {ECO:0000256|ARBA:ARBA00022536, ECO:0000256|PROSITE- KW ProRule:PRU00076}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW Repeat {ECO:0000256|ARBA:ARBA00022737}; KW Signal {ECO:0000256|ARBA:ARBA00022729}; KW Transmembrane {ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|SAM:Phobius}. FT TRANSMEM 892..912 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 3..45 FT /note="Cadherin" FT /evidence="ECO:0000259|PROSITE:PS50268" FT DOMAIN 46..150 FT /note="Cadherin" FT /evidence="ECO:0000259|PROSITE:PS50268" FT DOMAIN 151..255 FT /note="Cadherin" FT /evidence="ECO:0000259|PROSITE:PS50268" FT DOMAIN 271..357 FT /note="Cadherin" FT /evidence="ECO:0000259|PROSITE:PS50268" FT DOMAIN 500..537 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 539..719 FT /note="LAM_G_DOMAIN" FT /evidence="ECO:0000259|PROSITE:PS50025" FT DOMAIN 723..760 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 762..798 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 799..835 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT DOMAIN 837..873 FT /note="EGF-like" FT /evidence="ECO:0000259|PROSITE:PS50026" FT REGION 964..1000 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1013..1037 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1054..1107 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1131..1201 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1220..1245 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1285..1309 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 965..983 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1066..1089 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1154..1174 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT DISULFID 509..526 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 750..759 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 788..797 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 825..834 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT DISULFID 863..872 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00076" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:AAI00555.1" SQ SEQUENCE 1309 AA; 143805 MW; 9A208181C4136D09 CRC64; ESLDYKSSHE YYLTVEATDG GTPSLSDVAT VNINVTDIND NSPVFSQDTY TTVVSEDAAL EQPVITIMAD DADGPSNSHI HYSIIEGNQG SPFTIDPVRG EVKVTKPLDR ETISGYTLTV QAADNGNPPR VNTTTVNIDV SDVNDNAPLF SRDNYSVIIQ ENKPVGFSVL KLVVTDKDSS HNGPPFFFTI VSGNDENAFE VNQHGVLLTA ATIKRKVKDH YLLHVKVADS GKPQLSSMTH IDIRVIEESI HPPAILPLEI FITAFGEEYS GGVIGKIHAT DQDVYDTLMY SLDPHMDGLF SVSSTGGKLI AHRKLDIGQY LLNVSVTDGK FTTVADITVH IQQVTQEMLN HTVAIRFANL TPEEFVGDYW RNFQRALRNI LGVRKNDIQI VSLQPSEPHS HLDVLLFVER SGGTHVSTKQ LLHKINSSVT DVEEIIGVRI LEVFQKLCAG LDCPWKFCDE KVSVDENVMS THSTARLSFV TPRHHRTAVC LCKDGTCPPV HHGCEDNPCP AGSECVADPR EEKYSCVCPG GGFGKCPGSS SITFTGNSFV KYRLLENENR LEMKLSMRLR TYSSHAVVMY ARGTDYSILE IHTGRLQYKF DCGSGPGIVS VQSIQVNDGQ WHAVSLEVEG NYAKLVLDEV HTASGTAPGA LKTLNLDNYV FFGGHLRQQG TKHGRGAQVA SGFRGCMDSI YLNGQELPLN NKPRAYAHIE EWVDLSHGCL LTATEDCSSS PCQNGGVCNP SPTGGYYCKC SALYVGTFCE VSVNPCSSNP CLYGGTCMVD NGGFVCQCRG LYTGQRCQLS PYCKDDPCKN GGTCFDSLDG AVCQCDSGFR GERCQSDIDE CAGNPCRNGA LCENTHGSYH CNCSQEYRGK HCEDASPNHY VSTPWNIGLA EGIGIIVFIA GIVLLVMVFV LCRKMISRKK KRQAEPEDKR LGPTTAFLQR PYFDSKLNKN IYSDIPPQVP VRPISYTPSI PSDSRNNLDR NSFEGSAIPE HPEFSTFNPE SMHGHRKAVA VCSVAPNLPP PPPSNSPSDS DSIQKPSWDF DYDAKVVDLD PCLSKKPLEE KPSQPYSARE SLSEVQSLSS FQSESCDDNE SLAAPDLSKP RGYHWDTSDW MPSVPLPDIQ EFPNYEAIDE HTPLYSADPN AIDTDYYPGG YDIESDFPPP PEDFPAPDEL PPLPPEFSDQ FESIHPPRDM PAAGSLGSSS RSRQRFNLNQ YLPNFYPADM SEPQKQGAGE NSPCREPYTP YPPGYQNFEA PTIENMPMSV YASTASCSDV SACCEVESEV MMSDYESGDD GHFEEVTIPP LDSQQHTEV //