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Protein

Cadherin-related tumor suppressor

Gene

ft

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Involved in regulation of planar cell polarity in the compound eye where it is required for correct specification of the R3 and R4 photoreceptor cells by regulating Fz activity in the R3/R4 precursor cells (PubMed:11893338). This is likely to occur through creation of an ft gradient so that the equatorial R3/R4 precursor cell has a higher level of ft function than its polar neighbor (PubMed:15548581). Also required for planar cell polarity of wing hairs (PubMed:12540853, PubMed:15240556). Mediates heterophilic cell adhesion in vitro and is required to stabilize ds on the cell surface (PubMed:15240556). Involved in regulation of eye imaginal disk size (PubMed:23667559). Upstream component of the Hippo pathway where it is likely to act as a cell surface receptor involved in regulation of tissue size and is required for the localization and stability of ex (PubMed:16996265). Probably acts as a cell surface receptor for ds (PubMed:20434335).7 Publications
Ft-mito: Regulates mitochondrial electron transport chain integrity and promotes oxidative phosphorylation.1 Publication

GO - Molecular functioni

  • cadherin binding Source: FlyBase
  • calcium ion binding Source: FlyBase
  • cell adhesion molecule binding Source: FlyBase
  • receptor activity Source: FlyBase

GO - Biological processi

  • calcium-dependent cell-cell adhesion via plasma membrane cell adhesion molecules Source: UniProtKB
  • cell-cell adhesion mediated by cadherin Source: FlyBase
  • cell morphogenesis involved in differentiation Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • equator specification Source: UniProtKB
  • establishment of body hair planar orientation Source: FlyBase
  • establishment of epithelial cell apical/basal polarity Source: FlyBase
  • establishment of imaginal disc-derived wing hair orientation Source: FlyBase
  • establishment of ommatidial planar polarity Source: UniProtKB
  • establishment of planar polarity Source: FlyBase
  • establishment of tissue polarity Source: FlyBase
  • establishment or maintenance of polarity of larval imaginal disc epithelium Source: UniProtKB
  • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules Source: FlyBase
  • hippo signaling Source: FlyBase
  • homophilic cell adhesion via plasma membrane adhesion molecules Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • imaginal disc growth Source: FlyBase
  • imaginal disc pattern formation Source: UniProtKB
  • microtubule cytoskeleton organization involved in establishment of planar polarity Source: FlyBase
  • negative regulation of cell proliferation Source: FlyBase
  • negative regulation of gene expression Source: UniProtKB
  • negative regulation of growth Source: FlyBase
  • negative regulation of imaginal disc growth Source: FlyBase
  • negative regulation of Wnt signaling pathway Source: FlyBase
  • ommatidial rotation Source: FlyBase
  • peptide cross-linking Source: UniProtKB
  • pupal development Source: UniProtKB
  • regulation of growth Source: FlyBase
  • regulation of imaginal disc growth Source: UniProtKB
  • regulation of organ growth Source: FlyBase
  • regulation of protein localization Source: FlyBase
  • regulation of tube length, open tracheal system Source: FlyBase
  • single organismal cell-cell adhesion Source: FlyBase
  • tissue development Source: UniProtKB
  • wing disc development Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Receptor

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Cadherin-related tumor suppressor
Alternative name(s):
Protein fat
Cleaved into the following chain:
Ft-mito1 Publication
Gene namesi
Name:ftImported
ORF Names:CG3352Imported
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 2L

Organism-specific databases

FlyBaseiFBgn0001075. ft.

Subcellular locationi

Ft-mito :

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini36 – 45834548ExtracellularSequence analysisAdd
BLAST
Transmembranei4584 – 460926HelicalSequence analysisAdd
BLAST
Topological domaini4610 – 5147538CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • apical plasma membrane Source: UniProtKB-SubCell
  • integral component of membrane Source: FlyBase
  • integral component of plasma membrane Source: UniProtKB
  • mitochondrion Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Mitochondrion

Pathology & Biotechi

Disruption phenotypei

Severe overgrown imaginal disk derivatives and pupal death (PubMed:16996265). Overall larval growth is reduced (PubMed:25215488). Cells are round, swollen and have abnormal mitochondrial cristae due to defects in assembly of the mitochondrial electron chain complexes I and V (CI and CV) (PubMed:25215488). Loss of CI activity results in a switch to aerobic glycosis which increases lactate levels (PubMed:25215488). RNAi-mediated knockdown results in dorsal-ventral inversions in ommatidia planar cell polarity (PubMed:25215488).2 Publications

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi273 – 2731S → A or D: Blocks ability of fj to enhance binding to ds. 1 Publication
Mutagenesisi4854 – 48541T → I in ft61; strong overgrowth of eye imaginal disks. Binding to Fbxl7 is not affected. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini? – 5147Ft-mito1 PublicationPRO_0000434022
Signal peptidei1 – 3535Sequence analysisAdd
BLAST
Chaini36 – 51475112Cadherin-related tumor suppressorPRO_0000004015Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi239 – 2391N-linked (GlcNAc...)Sequence analysis
Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence analysis
Glycosylationi276 – 2761N-linked (GlcNAc...)Sequence analysis
Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence analysis
Glycosylationi402 – 4021N-linked (GlcNAc...)Sequence analysis
Glycosylationi461 – 4611N-linked (GlcNAc...)Sequence analysis
Glycosylationi605 – 6051N-linked (GlcNAc...)Sequence analysis
Glycosylationi631 – 6311N-linked (GlcNAc...)Sequence analysis
Glycosylationi1155 – 11551N-linked (GlcNAc...)Sequence analysis
Glycosylationi1367 – 13671N-linked (GlcNAc...)Sequence analysis
Glycosylationi1458 – 14581N-linked (GlcNAc...)Sequence analysis
Glycosylationi1751 – 17511N-linked (GlcNAc...)Sequence analysis
Glycosylationi1831 – 18311N-linked (GlcNAc...)Sequence analysis
Glycosylationi1880 – 18801N-linked (GlcNAc...)Sequence analysis
Glycosylationi2080 – 20801N-linked (GlcNAc...)Sequence analysis
Glycosylationi2171 – 21711N-linked (GlcNAc...)Sequence analysis
Glycosylationi2247 – 22471N-linked (GlcNAc...)Sequence analysis
Glycosylationi2290 – 22901N-linked (GlcNAc...)Sequence analysis
Glycosylationi2437 – 24371N-linked (GlcNAc...)Sequence analysis
Glycosylationi2581 – 25811N-linked (GlcNAc...)Sequence analysis
Glycosylationi2799 – 27991N-linked (GlcNAc...)Sequence analysis
Glycosylationi2920 – 29201N-linked (GlcNAc...)Sequence analysis
Glycosylationi2946 – 29461N-linked (GlcNAc...)Sequence analysis
Glycosylationi2967 – 29671N-linked (GlcNAc...)Sequence analysis
Glycosylationi3167 – 31671N-linked (GlcNAc...)Sequence analysis
Glycosylationi3303 – 33031N-linked (GlcNAc...)Sequence analysis
Glycosylationi3386 – 33861N-linked (GlcNAc...)Sequence analysis
Glycosylationi3389 – 33891N-linked (GlcNAc...)Sequence analysis
Glycosylationi3525 – 35251N-linked (GlcNAc...)Sequence analysis
Glycosylationi3852 – 38521N-linked (GlcNAc...)Sequence analysis
Glycosylationi3865 – 38651N-linked (GlcNAc...)Sequence analysis
Glycosylationi3905 – 39051N-linked (GlcNAc...)Sequence analysis
Disulfide bondi3954 ↔ 3966By similarity
Disulfide bondi3960 ↔ 3999By similarity
Disulfide bondi4001 ↔ 4010By similarity
Disulfide bondi4017 ↔ 4028By similarity
Disulfide bondi4022 ↔ 4037By similarity
Disulfide bondi4039 ↔ 4048By similarity
Disulfide bondi4056 ↔ 4067By similarity
Disulfide bondi4061 ↔ 4078By similarity
Disulfide bondi4080 ↔ 4089By similarity
Disulfide bondi4096 ↔ 4107By similarity
Disulfide bondi4101 ↔ 4116By similarity
Disulfide bondi4118 ↔ 4127By similarity
Disulfide bondi4294 ↔ 4320By similarity
Glycosylationi4306 – 43061N-linked (GlcNAc...)Sequence analysis
Disulfide bondi4325 ↔ 4341By similarity
Disulfide bondi4334 ↔ 4350By similarity
Disulfide bondi4352 ↔ 4361By similarity
Glycosylationi4414 – 44141N-linked (GlcNAc...)Sequence analysis
Glycosylationi4471 – 44711N-linked (GlcNAc...)Sequence analysis
Glycosylationi4487 – 44871N-linked (GlcNAc...)Sequence analysis
Disulfide bondi4536 ↔ 4569By similarity
Glycosylationi4539 – 45391N-linked (GlcNAc...)Sequence analysis
Glycosylationi4550 – 45501N-linked (GlcNAc...)Sequence analysis
Modified residuei4843 – 48431Phosphoserine1 Publication
Modified residuei5054 – 50541Phosphoserine1 Publication
Modified residuei5061 – 50611Phosphoserine1 Publication

Post-translational modificationi

Phosphorylated by fj on Ser/Thr of cadherin domains (PubMed:18635802). Phosphorylation by fj enhances binding to ds (PubMed:20434335). Phosphorylated in the cytoplasmic domain in a dco-dependent manner which is promoted by ds (PubMed:19574458).3 Publications
Proteolytically cleaved to yield stably associated N- and C-terminal fragments (PubMed:19574458). The C-terminal fragment is processed further to release a 68 kDa mitochondrial fragment, Ft-mito (PubMed:25215488).2 Publications

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein

Proteomic databases

PaxDbiP33450.
PRIDEiP33450.

PTM databases

iPTMnetiP33450.

Expressioni

Gene expression databases

BgeeiP33450.
ExpressionAtlasiP33450. differential.
GenevisibleiP33450. DM.

Interactioni

Subunit structurei

Interacts with Fbxl7 (PubMed:25107277). Ft-mito interacts with NADH dehydrogenase subunit ND-24 and with ATP synthase subunit ATPsynC (PubMed:25215488).2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ATPsynCQ6NN092EBI-135374,EBI-153383
GugQ8IQA63EBI-135374,EBI-153156
ND-24Q9VX364EBI-135374,EBI-189196

GO - Molecular functioni

  • cadherin binding Source: FlyBase
  • cell adhesion molecule binding Source: FlyBase

Protein-protein interaction databases

BioGridi59824. 11 interactions.
DIPiDIP-21094N.
IntActiP33450. 51 interactions.
MINTiMINT-1746562.
STRINGi7227.FBpp0077167.

Structurei

3D structure databases

ProteinModelPortaliP33450.
SMRiP33450. Positions 97-3787, 3956-4505.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini36 – 156121Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini157 – 270114Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini271 – 382112Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini383 – 494112Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini495 – 599105Cadherin 5PROSITE-ProRule annotationAdd
BLAST
Domaini600 – 708109Cadherin 6PROSITE-ProRule annotationAdd
BLAST
Domaini709 – 820112Cadherin 7PROSITE-ProRule annotationAdd
BLAST
Domaini821 – 942122Cadherin 8PROSITE-ProRule annotationAdd
BLAST
Domaini943 – 1049107Cadherin 9PROSITE-ProRule annotationAdd
BLAST
Domaini1050 – 1153104Cadherin 10PROSITE-ProRule annotationAdd
BLAST
Domaini1154 – 1278125Cadherin 11PROSITE-ProRule annotationAdd
BLAST
Domaini1279 – 1384106Cadherin 12PROSITE-ProRule annotationAdd
BLAST
Domaini1385 – 1489105Cadherin 13PROSITE-ProRule annotationAdd
BLAST
Domaini1490 – 1601112Cadherin 14PROSITE-ProRule annotationAdd
BLAST
Domaini1602 – 1713112Cadherin 15PROSITE-ProRule annotationAdd
BLAST
Domaini1714 – 1823110Cadherin 16PROSITE-ProRule annotationAdd
BLAST
Domaini1824 – 192299Cadherin 17PROSITE-ProRule annotationAdd
BLAST
Domaini1923 – 2027105Cadherin 18PROSITE-ProRule annotationAdd
BLAST
Domaini2028 – 2167140Cadherin 19PROSITE-ProRule annotationAdd
BLAST
Domaini2168 – 2278111Cadherin 20PROSITE-ProRule annotationAdd
BLAST
Domaini2279 – 2385107Cadherin 21PROSITE-ProRule annotationAdd
BLAST
Domaini2386 – 2491106Cadherin 22PROSITE-ProRule annotationAdd
BLAST
Domaini2492 – 2596105Cadherin 23PROSITE-ProRule annotationAdd
BLAST
Domaini2597 – 2703107Cadherin 24PROSITE-ProRule annotationAdd
BLAST
Domaini2704 – 2810107Cadherin 25PROSITE-ProRule annotationAdd
BLAST
Domaini2811 – 2913103Cadherin 26PROSITE-ProRule annotationAdd
BLAST
Domaini2914 – 3013100Cadherin 27PROSITE-ProRule annotationAdd
BLAST
Domaini3014 – 3124111Cadherin 28PROSITE-ProRule annotationAdd
BLAST
Domaini3125 – 3229105Cadherin 29PROSITE-ProRule annotationAdd
BLAST
Domaini3230 – 3334105Cadherin 30PROSITE-ProRule annotationAdd
BLAST
Domaini3335 – 3439105Cadherin 31PROSITE-ProRule annotationAdd
BLAST
Domaini3440 – 3545106Cadherin 32PROSITE-ProRule annotationAdd
BLAST
Domaini3546 – 3651106Cadherin 33PROSITE-ProRule annotationAdd
BLAST
Domaini3652 – 3756105Cadherin 34PROSITE-ProRule annotationAdd
BLAST
Domaini3950 – 401162EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini4013 – 404937EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini4052 – 409039EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Domaini4092 – 412837EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini4129 – 4320192Laminin G-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini4321 – 436242EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini4402 – 4569168Laminin G-like 2PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni4744 – 477128Essential for stability of mitochondrial electron chain complexes I and V, and promotes interaction with ND-241 PublicationAdd
BLAST

Domaini

The extracellular domain is required for correct subcellular localization and for cell adhesion.1 Publication
The intracellular domain is sufficient for viability, growth control and planar cell polarity.1 Publication

Sequence similaritiesi

Contains 34 cadherin domains.PROSITE-ProRule annotation
Contains 5 EGF-like domains.PROSITE-ProRule annotation
Contains 2 laminin G-like domains.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG1219. Eukaryota.
ENOG410XPEI. LUCA.
GeneTreeiENSGT00760000118805.
HOGENOMiHOG000107041.
InParanoidiP33450.
KOiK16669.
OMAiVYAIEKS.
OrthoDBiEOG75TM9Z.
PhylomeDBiP33450.

Family and domain databases

Gene3Di2.60.120.200. 3 hits.
2.60.40.60. 35 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00028. Cadherin. 33 hits.
PF00008. EGF. 2 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 34 hits.
SM00181. EGF. 5 hits.
SM00179. EGF_CA. 3 hits.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 34 hits.
SSF49899. SSF49899. 3 hits.
PROSITEiPS00232. CADHERIN_1. 22 hits.
PS50268. CADHERIN_2. 34 hits.
PS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 4 hits.
PS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33450-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MERLLLLFFL LLAGRESLCQ TGDTKLELLA PRGRSYATTY EQYAAFPRRR
60 70 80 90 100
SSSSSPSGEM QSRAVDTSAD FEVLEGQPRG TTVGFIPTKP KFSYRFNEPP
110 120 130 140 150
REFTLDPVTG EVKTNVVLDR EGMRDHYDLV VLSSQPTYPI EVRIKVLDVN
160 170 180 190 200
DNSPEFPEPS IAISFSESAT SGTRLLLDAA TDADVGENGV TDQYEIVAGN
210 220 230 240 250
VDNKFRLVTT ANPSGDTSYL HLETTGNLDR ESRGSYQLNI SARDGGSPPR
260 270 280 290 300
FGYLQVNVTI LDVNDNPPIF DHSDYNVSLN ETALPGTPVV TVMASDNDLG
310 320 330 340 350
DNSKITYYLA ETEHQFTVNP ETGVISTTER VNCPQQTNVK SSASQKSCVF
360 370 380 390 400
TVFARDHGSP RQDGRTYVTV NLLDTNDHDP IISFRFFPDG GKVATVDENA
410 420 430 440 450
VNGTVVAAVA VKDSDSGLNG RTSVRIVSGN ELGHFRLEEA ADLHIVRVNG
460 470 480 490 500
VLDREEIGKY NLTVVAMDQG TPARTTTAHL IIDVNDVNDH EPVFEKSEYS
510 520 530 540 550
AVLSELAPTG SFVASITATD EDTGVNAQVH YDILSGNELK WFSMDPLTGL
560 570 580 590 600
IVTTGPLDRE IRDTVELSIS ARDGGPNPKF AYTQLKVIIL DENDEAPQFS
610 620 630 640 650
QREQNVTLGE DAPPQTIVAL MTATDHDQGT NGSVTFALAP SVERLYPLQF
660 670 680 690 700
ALDALTGQLT TRRPLDREKM SQYEISVIAR DQGAPTPQSA TATVWLNVAD
710 720 730 740 750
VNDNDPQFYP RHYIYSLADD DDDIKLKKEV EKERILLHVT ASDKDDGDNA
760 770 780 790 800
LIEYRLESGG EGLFQLDARS GAISLRGDAP ASMHWKPHYK LLVSARDAGQ
810 820 830 840 850
RRSQQDAIVE IVLKSKLEML ECGQAQAGGY EFQMVEDHEQ QRNSQPNREV
860 870 880 890 900
GIVQVKSTNG KANSHIEYDI IQGDRAQNFR IDTRSGRITT ARPLDREEQA
910 920 930 940 950
NYRLTILASS SSSSSAAASS VSYGQCIVNI AIIDLNDNAP VFALDRESEP
960 970 980 990 1000
TISLPENAAV GQEIYLSRVR DRDAGVNSRI SYSLTNNPNQ QFRIGPVTGV
1010 1020 1030 1040 1050
LYLQRPIRAE PGSLIHVELM ATDAGSPPLS SKLSLSVLIA DVNDHTPVFD
1060 1070 1080 1090 1100
HTSYETSLPE TTKVNTRFFA LAATDIDLGD NGRISYEIIE GNTERMFGVF
1110 1120 1130 1140 1150
PDGYLFVRAP LDREERDYYA LTVSCRDAGQ PSRSSVVPVV IHVIDENDNA
1160 1170 1180 1190 1200
PQFTNSTFTF SIPENAPADT FVGKLTAVDR DIGRNAELSF TLSSQTQDFT
1210 1220 1230 1240 1250
IDTRNGFIKT LRPFDREALV KVSRNAEASG EDGSLRGSMA GNYMLLEATV
1260 1270 1280 1290 1300
SDNGIPRLQD KVKVKVIVTD VNDNAPEFLR APYHVTISEG ASEGTHITHV
1310 1320 1330 1340 1350
FTQDADEGLN GDVYYSLAKG NEAGQFNLDS ATGQLSLGRR LDRESQEIHH
1360 1370 1380 1390 1400
LIVVAKDAAL KHPLSSNASI TIVVLDENDN APEFTQSSSE VSVLETSPTG
1410 1420 1430 1440 1450
TELMRFRASD ADQGVNSQVV FSISAGNRRD TFHIDSITGS LYLHKPLDYE
1460 1470 1480 1490 1500
DITSYTLNIT ASDCGTPSLS TTVLYNVLVV DDNDNPPIFP STAIVRQIKE
1510 1520 1530 1540 1550
GIPLKTPIVT VTADDPDSGL NGKVSYAISK QEPQLPQGRH FGINTETGVI
1560 1570 1580 1590 1600
HTLREIDRES IDTFRLTVVA TDRAQPSERQ LSTEKLVTVI VEDINDNAPV
1610 1620 1630 1640 1650
FVSMNAAILP PKFSTSKGSS TAVMQVHAKD ADSSSNGLVT YEIVSGPQEL
1660 1670 1680 1690 1700
FKLQRNTGII TFTPGPQFKQ EVRYQLTLKS TDEAVQSERR SSEVYITIIT
1710 1720 1730 1740 1750
PGSGGSESSV PQFEQRSKLS GSVYENEPIG TSILTVTAHL ASAEIEYFVT
1760 1770 1780 1790 1800
NVTATGSRGQ VDRLFDIDAK LGILSTAAEL DREAGPEEYE VEVYAIALGG
1810 1820 1830 1840 1850
QPRTSRTKVR VTVLDKNDSP PQFLDTPFVY NVSEDLQIGH TISTLRAHDP
1860 1870 1880 1890 1900
DTLGSVTFLL MDGHDGKFLL EPSTGKLILN DTLDRETKSK YELRIRVSDG
1910 1920 1930 1940 1950
VQYTEAYATI QVSDTNDNPP LFEDTVYSFD IPENAQRGYQ VGQIVARDAD
1960 1970 1980 1990 2000
LGQNAQLSYG VVSDWANDVF SLNPQTGMLT LTARLDYEEV QHYILIVQAQ
2010 2020 2030 2040 2050
DNGQPSLSTT ITVYCNVLDL NDNAPIFDPM SYSSEVFENV PIATEVVTVS
2060 2070 2080 2090 2100
AKDIDSGNNG LIEYSITAGD VDSEFGIDSN GTIRTRRNLD REHRSTYTLT
2110 2120 2130 2140 2150
VTARDCADEF ASFSELEETQ LKLKYRSPRK YQQTRQEFLA HQKQQRLSST
2160 2170 2180 2190 2200
VKVTILIKDV NDEVPVFISA NETAIMENVA INTVVIAVKA VDNDEGRNGY
2210 2220 2230 2240 2250
IDYLMKEARD EDMGQSDPLP FSLNPTDGQL RVVDALDREL RSSYLLNITA
2260 2270 2280 2290 2300
RDRGEPPQST ESQLLIRILD ENDNSPVFDP KQYSASVAEN ASIGAMVLQV
2310 2320 2330 2340 2350
SATDVDEGAN GRIRYSIVLG DQNHDFSISE DTGVVRVAKN LNYERLSRYS
2360 2370 2380 2390 2400
LTVRAEDCAL ENPAGDTAEL TINILDINDN RPTFLDSPYL ARVMENTVPP
2410 2420 2430 2440 2450
NGGYVLTVNA YDADTPPLNS QVRYFLKEGD SDLFRINASS GDIALLKPLD
2460 2470 2480 2490 2500
REQQSEYTLT LVAMDTGSPP LTGTGIVRVE VQDINDNDPV FELQSYHATV
2510 2520 2530 2540 2550
RENLPSGTHV LTPRATDKDE GLNAKLRFNL LGEHMHRFHI DSETGEISTA
2560 2570 2580 2590 2600
TTLDREETSV YHLTLMAQDS SITEPRASSV NLTISVSDVN DNIPKFDSTT
2610 2620 2630 2640 2650
YNVAVPERIS KGEFVFGARA LDLDDGENAV VHYTISGRDQ HYFDINTKTG
2660 2670 2680 2690 2700
VVSTKLELKT KTKSHDDLTY TIVISAMDQG EQSLSSKAEL TVILRPPELF
2710 2720 2730 2740 2750
PTFAYMANSH FAMSEDVRPG KMITKVSATS PKKGLVGKIR YAIAGGIMGD
2760 2770 2780 2790 2800
SLRVDPNSGL LSVGQDGLDY ELTHLYEIWI EAADGDTPSL RSVTLITLNV
2810 2820 2830 2840 2850
TDANDNAPVM EQLIYNAEVL EEESPPQLIA VVKASDRDSG DNGNVIYRLQ
2860 2870 2880 2890 2900
NDFDGTFEIT ESGEIYTRMR LDREEIGDYA FVVEAVDQGV PHMTGTASVL
2910 2920 2930 2940 2950
LHLLDKNDNP PKFTRLFSLN VTENAEIGSF VIRVTSSDLD LGANANASYS
2960 2970 2980 2990 3000
FSENPGEKFR IEPQSGNITV AGHLDREQQD EYILKVVASD GAWRAETPIT
3010 3020 3030 3040 3050
ITIQDQNDNA PEFEHSFYSF SFPELQQSIA LVGQIIATDR DKQGPNSVIS
3060 3070 3080 3090 3100
YSLQQPSPMF SIDPATGEVF SKKAVRFKHS QYVRSPENMY ALTVLATDNG
3110 3120 3130 3140 3150
KPPLYSECLV NINIVDAHNN PPKFEQAEYL APLPQDAVRG QRIVRVHAND
3160 3170 3180 3190 3200
KQDLGTNEMD YSLMTFNLSS IFSVGRHDGW ITLVKPIQVP PNTRYELVVR
3210 3220 3230 3240 3250
ATDRGVPPQS DETRVVIVVT GENMDTPRFS VNSYQVIVPE NEPVGSTILT
3260 3270 3280 3290 3300
VGATDDDTGP NGMLRYSISG GNERQDFSVD ERTGGIVIQQ QLDYDLIQEY
3310 3320 3330 3340 3350
HLNITVQDLG YHPLSSVAML TIILTDVNDN PPVFNHKEYH CYIPENKPVG
3360 3370 3380 3390 3400
TFVFQAHAAD KDSPKNAIIH YAFLPSGPDR HFFIMNQSNG TISSAVSFDY
3410 3420 3430 3440 3450
EERRIYTLQI KAKNPDSSME SYANLYVHVL GVNEFYPQFL QPVFHFDVSE
3460 3470 3480 3490 3500
TSAVGTRVGA VQATDKDSGE DGRVYYLLVG SSNDKGFRID TNTGLIYVAR
3510 3520 3530 3540 3550
HLDRETQNRV VLTVMAKNYG SIRGNDTDEA QVIISIQDGN DPPEFIKHYY
3560 3570 3580 3590 3600
TSTISEAAPV GTKVTTVKAI DKDVRTQNNQ FSYSIINGNL KQSFKIDVQT
3610 3620 3630 3640 3650
GEISTASRLD REETSTYNLV IGAIDTGLPP QTGSATVHIE LEDVNDNGPT
3660 3670 3680 3690 3700
FTPEGLNGYI SENEPAGTSI MTLIASDPDL PRNGGPFTYQ LIGGKHKSWL
3710 3720 3730 3740 3750
SVDRNSGVVR STTSFDREMT PILEAIIEVE DSGKPKQKSQ HLLTITVLDQ
3760 3770 3780 3790 3800
NDNPSTTRSL HIAVSLFNGD LPSNVKLADV RPNDIDIVGD YRCRLQKNPA
3810 3820 3830 3840 3850
QSQLQLAIPR ACDLITTSHT TPIASVFSYT GNDGKHGDVS SKVSVAFQSF
3860 3870 3880 3890 3900
NNETLANSVS IMVRNMTAYH FLANHYRPIL EMIKSRMSNE DEVILYSLLE
3910 3920 3930 3940 3950
GGSGNSTNLQ LLMAVRLAKT SYQQPKYLIE RLREKRSAFS ELLQKEVIVG
3960 3970 3980 3990 4000
YEPCSEPDVC ENGGVCSATM RLLDAHSFVI QDSPALVLSG PRVVHDYSCQ
4010 4020 4030 4040 4050
CTSGFSGEQC SRRQDPCLPN PCHSQVQCRR LGSDFQCMCP ANRDGKHCEK
4060 4070 4080 4090 4100
ERSDVCYSKP CRNGGSCQRS PDGSSYFCLC RPGFRGNQCE SVSDSCRPNP
4110 4120 4130 4140 4150
CLHGGLCVSL KPGYKCNCTP GRYGRHCERF SYGFQPLSYM TFPALDVTTN
4160 4170 4180 4190 4200
DISIVFATTK PNSLLLYNYG MQSGGRSDFL AIELVHGRAY FSSGGARTAI
4210 4220 4230 4240 4250
STVIAGRNLA DGGWHKVTAT RNGRVMSLSV AKCADSGDVC TECLPGDSSC
4260 4270 4280 4290 4300
YADEVGPVGT LNFNKQPLMI GGLSSADPIL ERPGQVHSDD LVGCLHSVHI
4310 4320 4330 4340 4350
GGRALNLSLP LQQKGILAGC NRQACQPALA AERCGGFAGQ CIDRWSSSLC
4360 4370 4380 4390 4400
QCGGHLQSPD CSDSLEPITL GEGAFVEFRI SEIYRRMQLL DNLYNSKSAW
4410 4420 4430 4440 4450
LDNQQMRERR AVSNFSTASQ IYEAPKMLSM LFRTYKDQGQ ILYAATNQMF
4460 4470 4480 4490 4500
TSLSLREGRL VYYSKQHLTI NMTVQETSTL NDGKWHNVSL FSESRSLRLI
4510 4520 4530 4540 4550
VDGRQVGDEL DIAGVHDFLD PYLTILNVGG EAFVGCLANV TVNNELQPLN
4560 4570 4580 4590 4600
GSGSIFPEVR YHGKIESGCR GDIGQDAAQV ADPLSIGFTL VIVFFVILVV
4610 4620 4630 4640 4650
AILGSYVIYR FRGKQEKIGS LSCGVPGFKI KHPGGPVTQS QVDHVLVRNL
4660 4670 4680 4690 4700
HPSEAPSPPV GAGDHMRPPV GSHHLVGPEL LTKKFKEPTA EMPQPQQQQQ
4710 4720 4730 4740 4750
RPQRPDIIER ESPLIREDHH LPIPPLHPLP LEHASSVDMG SEYPEHYDLE
4760 4770 4780 4790 4800
NASSIAPSDI DIVYHYKGYR EAAGLRKYKA SVPPVSAYTH HKHQNSGSQQ
4810 4820 4830 4840 4850
QQQQHRHTAP FVTRNQGGQP PPPPTSASRT HQSTPLARLS PSSELSSQQP
4860 4870 4880 4890 4900
RILTLHDISG KPLQSALLAT TSSSGGVGKD VHSNSERSLN SPVMSQLSGQ
4910 4920 4930 4940 4950
SSSASRQKPG VPQQQAQQTS MGLTAEEIER LNGRPRTCSL ISTLDAVSSS
4960 4970 4980 4990 5000
SEAPRVSSSA LHMSLGGDVD AHSSTSTDES GNDSFTCSEI EYDNNSLSGD
5010 5020 5030 5040 5050
GKYSTSKSLL DGRSPVSRAL SGGETSRNPP TTVVKTPPIP PHAYDGFESS
5060 5070 5080 5090 5100
FRGSLSTLVA SDDDIANHLS GIYRKANGAA SPSATTLGWE YLLNWGPSYE
5110 5120 5130 5140
NLMGVFKDIA ELPDTNGPSQ QQQQQTQVVS TLRMPSSNGP AAPEEYV
Length:5,147
Mass (Da):564,791
Last modified:February 21, 2001 - v3
Checksum:i6A5A4743FC7E07D0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti676 – 6761S → P in AAA28530 (PubMed:1959133).Curated
Sequence conflicti718 – 7181A → T in AAA28530 (PubMed:1959133).Curated
Sequence conflicti889 – 8891T → S in AAA28530 (PubMed:1959133).Curated
Sequence conflicti1298 – 12981T → M in AAA28530 (PubMed:1959133).Curated
Sequence conflicti1338 – 13381G → A in AAA28530 (PubMed:1959133).Curated
Sequence conflicti1366 – 13661S → T in AAA28530 (PubMed:1959133).Curated
Sequence conflicti1408 – 14081A → G in AAA28530 (PubMed:1959133).Curated
Sequence conflicti1755 – 17551T → V in AAA28530 (PubMed:1959133).Curated
Sequence conflicti2168 – 21681I → V in AAA28530 (PubMed:1959133).Curated
Sequence conflicti2266 – 22661I → V in AAA28530 (PubMed:1959133).Curated
Sequence conflicti2665 – 26651H → T in AAA28530 (PubMed:1959133).Curated
Sequence conflicti2712 – 27121A → T in AAA28530 (PubMed:1959133).Curated
Sequence conflicti2816 – 28161N → T in AAA28530 (PubMed:1959133).Curated
Sequence conflicti2893 – 28931M → L in AAA28530 (PubMed:1959133).Curated
Sequence conflicti3359 – 33591A → T in AAA28530 (PubMed:1959133).Curated
Sequence conflicti3674 – 36741I → M in AAA28530 (PubMed:1959133).Curated
Sequence conflicti3722 – 37221I → V in AAA28530 (PubMed:1959133).Curated
Sequence conflicti3869 – 38691Y → N in AAA28530 (PubMed:1959133).Curated
Sequence conflicti4187 – 41871G → D in AAA28530 (PubMed:1959133).Curated
Sequence conflicti4309 – 43091L → S in AAA28530 (PubMed:1959133).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti1229 – 12291S → G.
Natural varianti1233 – 12331G → S.

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80537 Genomic DNA. Translation: AAA28530.1.
AE014134 Genomic DNA. Translation: AAF51036.1.
PIRiA41087. IJFFTM.
RefSeqiNP_477497.1. NM_058149.4.
UniGeneiDm.293.

Genome annotation databases

EnsemblMetazoaiFBtr0077478; FBpp0077167; FBgn0001075.
GeneIDi33627.
KEGGidme:Dmel_CG3352.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M80537 Genomic DNA. Translation: AAA28530.1.
AE014134 Genomic DNA. Translation: AAF51036.1.
PIRiA41087. IJFFTM.
RefSeqiNP_477497.1. NM_058149.4.
UniGeneiDm.293.

3D structure databases

ProteinModelPortaliP33450.
SMRiP33450. Positions 97-3787, 3956-4505.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi59824. 11 interactions.
DIPiDIP-21094N.
IntActiP33450. 51 interactions.
MINTiMINT-1746562.
STRINGi7227.FBpp0077167.

PTM databases

iPTMnetiP33450.

Proteomic databases

PaxDbiP33450.
PRIDEiP33450.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiFBtr0077478; FBpp0077167; FBgn0001075.
GeneIDi33627.
KEGGidme:Dmel_CG3352.

Organism-specific databases

CTDi33627.
FlyBaseiFBgn0001075. ft.

Phylogenomic databases

eggNOGiKOG1219. Eukaryota.
ENOG410XPEI. LUCA.
GeneTreeiENSGT00760000118805.
HOGENOMiHOG000107041.
InParanoidiP33450.
KOiK16669.
OMAiVYAIEKS.
OrthoDBiEOG75TM9Z.
PhylomeDBiP33450.

Miscellaneous databases

GenomeRNAii33627.
NextBioi784506.
PROiP33450.

Gene expression databases

BgeeiP33450.
ExpressionAtlasiP33450. differential.
GenevisibleiP33450. DM.

Family and domain databases

Gene3Di2.60.120.200. 3 hits.
2.60.40.60. 35 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00028. Cadherin. 33 hits.
PF00008. EGF. 2 hits.
PF00054. Laminin_G_1. 1 hit.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 34 hits.
SM00181. EGF. 5 hits.
SM00179. EGF_CA. 3 hits.
SM00282. LamG. 2 hits.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 34 hits.
SSF49899. SSF49899. 3 hits.
PROSITEiPS00232. CADHERIN_1. 22 hits.
PS50268. CADHERIN_2. 34 hits.
PS00022. EGF_1. 4 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 4 hits.
PS50025. LAM_G_DOMAIN. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The fat tumor suppressor gene in Drosophila encodes a novel member of the cadherin gene superfamily."
    Mahoney P.A., Weber U., Onofrechuk P., Biessmann H., Bryant P.J., Goodman C.S.
    Cell 67:853-868(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "The genome sequence of Drosophila melanogaster."
    Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
    , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
    Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Berkeley.
  3. Cited for: GENOME REANNOTATION.
    Strain: Berkeley.
  4. "Regulation of Frizzled by fat-like cadherins during planar polarity signaling in the Drosophila compound eye."
    Yang C.H., Axelrod J.D., Simon M.A.
    Cell 108:675-688(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  5. "Fidelity in planar cell polarity signalling."
    Ma D., Yang C.H., McNeill H., Simon M.A., Axelrod J.D.
    Nature 421:543-547(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Interactions between Fat and Dachsous and the regulation of planar cell polarity in the Drosophila wing."
    Matakatsu H., Blair S.S.
    Development 131:3785-3794(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  7. "Planar cell polarity in the Drosophila eye is directed by graded Four-jointed and Dachsous expression."
    Simon M.A.
    Development 131:6175-6184(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "Separating the adhesive and signaling functions of the Fat and Dachsous protocadherins."
    Matakatsu H., Blair S.S.
    Development 133:2315-2324(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: DOMAIN.
  9. "The fat cadherin acts through the hippo tumor-suppressor pathway to regulate tissue size."
    Willecke M., Hamaratoglu F., Kango-Singh M., Udan R., Chen C.L., Tao C., Zhang X., Halder G.
    Curr. Biol. 16:2090-2100(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, DISRUPTION PHENOTYPE.
  10. "Phosphoproteome analysis of Drosophila melanogaster embryos."
    Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.
    J. Proteome Res. 7:1675-1682(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-4843; SER-5054 AND SER-5061, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Embryo.
  11. "Four-jointed is a Golgi kinase that phosphorylates a subset of cadherin domains."
    Ishikawa H.O., Takeuchi H., Haltiwanger R.S., Irvine K.D.
    Science 321:401-404(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION.
  12. "Processing and phosphorylation of the Fat receptor."
    Feng Y., Irvine K.D.
    Proc. Natl. Acad. Sci. U.S.A. 106:11989-11994(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, CLEAVAGE.
  13. "Modulation of fat:dachsous binding by the cadherin domain kinase four-jointed."
    Simon M.A., Xu A., Ishikawa H.O., Irvine K.D.
    Curr. Biol. 20:811-817(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, PHOSPHORYLATION, MUTAGENESIS OF SER-273.
  14. "The Drosophila Cadherin Fat regulates tissue size and planar cell polarity through different domains."
    Zhao X., Yang C.H., Simon M.A.
    PLoS ONE 8:E62998-E62998(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. Cited for: FUNCTION, SUBCELLULAR LOCATION, CLEAVAGE, DISRUPTION PHENOTYPE, INTERACTION WITH ATPSYNC AND ND-24.
  16. "The Drosophila F-box protein Fbxl7 binds to the protocadherin fat and regulates Dachs localization and Hippo signaling."
    Bosch J.A., Sumabat T.M., Hafezi Y., Pellock B.J., Gandhi K.D., Hariharan I.K.
    Elife 3:E03383-E03383(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH FBXL7, MUTAGENESIS OF THR-4854.

Entry informationi

Entry nameiFAT_DROME
AccessioniPrimary (citable) accession number: P33450
Secondary accession number(s): Q9VQX5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 21, 2001
Last modified: May 11, 2016
This is version 150 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

The name 'fat' originates from weak mutant alleles that exhibit a broadening of the abdomen.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.