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O88277

- FAT2_RAT

UniProt

O88277 - FAT2_RAT

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Protein

Protocadherin Fat 2

Gene

Fat2

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

May modulate the extracellular space surronding parallel fibers of cerebellar during development. Plays a role in the migration of epidermal cells (By similarity).By similarity

GO - Molecular functioni

  1. calcium ion binding Source: InterPro

GO - Biological processi

  1. epithelial cell migration Source: UniProtKB
  2. homophilic cell adhesion Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium

Names & Taxonomyi

Protein namesi
Recommended name:
Protocadherin Fat 2
Alternative name(s):
Multiple epidermal growth factor-like domains protein 1
Short name:
Multiple EGF-like domains protein 1
Gene namesi
Name:Fat2
Synonyms:Fath2, Megf1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494: Unplaced

Organism-specific databases

RGDi620656. Fat2.

Subcellular locationi

Cell membrane Curated; Single-pass membrane protein Curated. Cell junction By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cell-cell adherens junction Source: UniProtKB
  2. integral component of membrane Source: UniProtKB-KW
  3. nucleus Source: UniProtKB-KW
  4. plasma membrane Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Cell junction, Cell membrane, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence AnalysisAdd
BLAST
Chaini19 – 43514333Protocadherin Fat 2PRO_0000004019Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi39 – 391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi210 – 2101N-linked (GlcNAc...)Sequence Analysis
Glycosylationi280 – 2801N-linked (GlcNAc...)Sequence Analysis
Glycosylationi330 – 3301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi459 – 4591N-linked (GlcNAc...)Sequence Analysis
Glycosylationi568 – 5681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi627 – 6271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi789 – 7891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi996 – 9961N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1175 – 11751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1276 – 12761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1417 – 14171N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1899 – 18991N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1998 – 19981N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2007 – 20071N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2102 – 21021N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2165 – 21651N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2183 – 21831N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2325 – 23251N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2368 – 23681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2387 – 23871N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2430 – 24301N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2470 – 24701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2547 – 25471N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2597 – 25971N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3127 – 31271N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3278 – 32781N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3312 – 33121N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3432 – 34321N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3603 – 36031N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3770 – 37701N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3774 – 37741N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3815 – 38151N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3842 – 38421N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3875 – 38751N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3906 – 39061N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3914 ↔ 3946By similarity
Disulfide bondi3953 ↔ 3964By similarity
Disulfide bondi3958 ↔ 3974By similarity
Disulfide bondi3976 ↔ 3985By similarity
Glycosylationi3991 – 39911N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3992 ↔ 4003By similarity
Disulfide bondi3997 ↔ 4012By similarity
Disulfide bondi4014 ↔ 4023By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiO88277.
PRIDEiO88277.

PTM databases

PhosphoSiteiO88277.

Expressioni

Tissue specificityi

Cerebellum-specific expression. Expressed in thin parallel fibers of cerebellar granule cells.2 Publications

Developmental stagei

In the developing cerebellum, expressed in granule cells in the inner external germinal layer and in migrating granule cells whereas proliferating cells in the outer extessornal germinal layer did not shown expression. Expression levels in the internal granule cell layer peak during the third postnatal week and remain considerably high in the adult cerebellum.1 Publication

Gene expression databases

GenevestigatoriO88277.

Interactioni

Subunit structurei

Homodimer.1 Publication

Protein-protein interaction databases

BioGridi249241. 1 interaction.
STRINGi10116.ENSRNOP00000017106.

Structurei

3D structure databases

ProteinModelPortaliO88277.
ModBaseiSearch...
MobiDBiSearch...

Topological domain

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini19 – 40504032ExtracellularSequence AnalysisAdd
BLAST
Topological domaini4072 – 4351280CytoplasmicSequence AnalysisAdd
BLAST

Transmembrane

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transmembranei4051 – 407121HelicalSequence AnalysisAdd
BLAST

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini34 – 148115Cadherin 1PROSITE-ProRule annotationAdd
BLAST
Domaini149 – 256108Cadherin 2PROSITE-ProRule annotationAdd
BLAST
Domaini363 – 45896Cadherin 3PROSITE-ProRule annotationAdd
BLAST
Domaini459 – 564106Cadherin 4PROSITE-ProRule annotationAdd
BLAST
Domaini565 – 669105Cadherin 5PROSITE-ProRule annotationAdd
BLAST
Domaini716 – 820105Cadherin 6PROSITE-ProRule annotationAdd
BLAST
Domaini821 – 925105Cadherin 7PROSITE-ProRule annotationAdd
BLAST
Domaini926 – 1032107Cadherin 8PROSITE-ProRule annotationAdd
BLAST
Domaini1033 – 1142110Cadherin 9PROSITE-ProRule annotationAdd
BLAST
Domaini1138 – 1242105Cadherin 10PROSITE-ProRule annotationAdd
BLAST
Domaini1243 – 1346104Cadherin 11PROSITE-ProRule annotationAdd
BLAST
Domaini1350 – 144899Cadherin 12PROSITE-ProRule annotationAdd
BLAST
Domaini1449 – 1555107Cadherin 13PROSITE-ProRule annotationAdd
BLAST
Domaini1556 – 1660105Cadherin 14PROSITE-ProRule annotationAdd
BLAST
Domaini1661 – 175898Cadherin 15PROSITE-ProRule annotationAdd
BLAST
Domaini1759 – 1872114Cadherin 16PROSITE-ProRule annotationAdd
BLAST
Domaini1873 – 196896Cadherin 17PROSITE-ProRule annotationAdd
BLAST
Domaini1969 – 2070102Cadherin 18PROSITE-ProRule annotationAdd
BLAST
Domaini2071 – 2171101Cadherin 19PROSITE-ProRule annotationAdd
BLAST
Domaini2172 – 2272101Cadherin 20PROSITE-ProRule annotationAdd
BLAST
Domaini2273 – 2379107Cadherin 21PROSITE-ProRule annotationAdd
BLAST
Domaini2380 – 2481102Cadherin 22PROSITE-ProRule annotationAdd
BLAST
Domaini2482 – 2585104Cadherin 23PROSITE-ProRule annotationAdd
BLAST
Domaini2586 – 2692107Cadherin 24PROSITE-ProRule annotationAdd
BLAST
Domaini2693 – 2799107Cadherin 25PROSITE-ProRule annotationAdd
BLAST
Domaini2800 – 2908109Cadherin 26PROSITE-ProRule annotationAdd
BLAST
Domaini2909 – 3013105Cadherin 27PROSITE-ProRule annotationAdd
BLAST
Domaini3014 – 3115102Cadherin 28PROSITE-ProRule annotationAdd
BLAST
Domaini3116 – 3220105Cadherin 29PROSITE-ProRule annotationAdd
BLAST
Domaini3221 – 3323103Cadherin 30PROSITE-ProRule annotationAdd
BLAST
Domaini3324 – 3428105Cadherin 31PROSITE-ProRule annotationAdd
BLAST
Domaini3429 – 3533105Cadherin 32PROSITE-ProRule annotationAdd
BLAST
Domaini3534 – 363198Cadherin 33PROSITE-ProRule annotationAdd
BLAST
Domaini3775 – 3946172Laminin G-likePROSITE-ProRule annotationAdd
BLAST
Domaini3949 – 398638EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini3988 – 402437EGF-like 2PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 33 cadherin domains.PROSITE-ProRule annotation
Contains 2 EGF-like domains.PROSITE-ProRule annotation
Contains 1 laminin G-like domain.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiNOG12793.
HOGENOMiHOG000046499.
HOVERGENiHBG005641.
InParanoidiO88277.
KOiK16506.
PhylomeDBiO88277.

Family and domain databases

Gene3Di2.60.120.200. 1 hit.
2.60.40.60. 33 hits.
InterProiIPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR001791. Laminin_G.
[Graphical view]
PfamiPF00028. Cadherin. 27 hits.
PF00008. EGF. 2 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view]
PRINTSiPR00205. CADHERIN.
SMARTiSM00112. CA. 33 hits.
SM00181. EGF. 2 hits.
SM00282. LamG. 1 hit.
[Graphical view]
SUPFAMiSSF49313. SSF49313. 33 hits.
SSF49899. SSF49899. 1 hit.
PROSITEiPS00232. CADHERIN_1. 14 hits.
PS50268. CADHERIN_2. 33 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS50025. LAM_G_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

O88277-1 [UniParc]FASTAAdd to Basket

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        10         20         30         40         50
MTLVLLGLAI LLLHRAACEK SLEETIPPLS WRFTHSLYNA TIYENSAPKT
60 70 80 90 100
YVESPVKMGM YLAEPHWVVK YRIISGDAAG VFKTEEHVVG NFCFLRIRTK
110 120 130 140 150
SSNTALLNRE VRDSYTLIVQ ASDKSLEFEA LTQVVVHILD QNDLKPLFSP
160 170 180 190 200
PSYRVTISED RPLKSPICKV TATDADLGQN AEFYYAFNAR SEVFAIHPTS
210 220 230 240 250
GVVTVAGKLN VTRRGKYELQ VLAVDRMRKI SEGNGFGNLA SLVIRVEPVH
260 270 280 290 300
RKPPAINLVV LNPPEGDEGD IYAIVTVDTN GSGAEVDSLE VVGGDPGKYF
310 320 330 340 350
KVLRSYAQGN EFNLVAVRDI NWAEHPHGFN ISLQTHSWSR FPPHSIIRAF
360 370 380 390 400
HLPSWKLANL RFEKAVYRVK LSEFSPPGSR VALVKVTTAL PNLRYSLKPS
410 420 430 440 450
SRNTAFKLNA RTGLITTTKL VDFHEQNQYQ LHVKTSLGQA TTTVIIDIVD
460 470 480 490 500
CNNHAPVFNR SSYEGTLDEN IPPGTSVLTV TATDQDHGDN GHITYSIAGP
510 520 530 540 550
KAVPFSIDPL LGVISTTKPM DYELMKRIYT FRVRASDWGS PFRQEKEVSV
560 570 580 590 600
SLRLKNLNDN QPMFEEVNCT VSLRQDVPVG KSIMAVSAID MDELQNLKYE
610 620 630 640 650
IVSGNEQDYF HLNHFSGVIS LKRSFMNLTA VRPTIYSLKI TASDGKNYAS
660 670 680 690 700
PTTLKVTVVK DPHSEVPVQC DKTGVLTHIT KTILQSAGLQ SQELGEEEFT
710 720 730 740 750
SLSNYQINHH SPQFEDHFPQ SIDILEQVPI NTPLARLAAT DPDTGFHGKL
760 770 780 790 800
VYVISDGNEE GCFDIELETG LLMVAAALDY ETTSFYVLNV TVYDLGTPPK
810 820 830 840 850
SSWKLLTVTV KDWNDNPPRF PPGGYQLTIS EDTEVGTTIA ELKTEDADSE
860 870 880 890 900
DNRRVRYTLL TPTEKFSLHP FTGELVVTGH LDRESESQYI LKAEARDQPT
910 920 930 940 950
KGHQLFSVTD LIVTLEDIND NPPQCITEHR RLKVPEDMPL GTVLTFLDAS
960 970 980 990 1000
DPDLGPAGEV KYILVEDAHG TFQVHPMTGA LSLEKELDFE RRAGYNLSFW
1010 1020 1030 1040 1050
ASDSGKPLSR RTLCHVEVLV MDVNENLHSP HFSSFVYQGQ VQENSPAGTP
1060 1070 1080 1090 1100
VMVVTAQDDD SGLDGELQYF LRAGTGLETF SINQDTGMLE TLAPLDREFT
1110 1120 1130 1140 1150
PYYWLTVLAV DRGSVPLSAV TEVYIEVTDI NDNIPSMSRP VFYPSVLEDA
1160 1170 1180 1190 1200
PLGTSVLQLE AWDPDSSSQG KLTFNLTSGN HLGHFIVHPF TGLLTTAKQL
1210 1220 1230 1240 1250
DRENKDEYVL EVTVQDNGDP SLRSTSRVVV CILDVNDNPP MFSHKLFNVR
1260 1270 1280 1290 1300
LSERLSPLSP EPVYRLVASD PDEGLNGSVT YSIEESDEES FRIDPVTGVV
1310 1320 1330 1340 1350
SSSSTFAAGE YNILTIKATD SGQPALSTSV RLHIEWIPQP RPSSIPLSFD
1360 1370 1380 1390 1400
ESYYSFTVME TDPVNHMVGV ISVEGRPGLF WFHISDGDKD MDFDIEKTTG
1410 1420 1430 1440 1450
SIVIARPLDT RRKSSYNLTV EVTDGFHTIA TQVHIFMIAN INHHRPQFLQ
1460 1470 1480 1490 1500
DHYEIRVPQD TLPGVELLRV QATDQDHGKG LIYTILSSQD PGSANLFQLD
1510 1520 1530 1540 1550
PSSGVLVTVG TLELHSGPSQ HILTVMVRDQ EMPIKRNFVW VTIHVEDGNL
1560 1570 1580 1590 1600
HSPHFTQLRY EANVPDTTAP GTELLQVRAV DADRGANAEI HYSFLKGNSD
1610 1620 1630 1640 1650
GFFNIDSLLG IITVAQRLYH VHLTRHALTV KAEDQGSPRR HDLALVVIHV
1660 1670 1680 1690 1700
HPSDSSAPVF SKDEYFIEIP ESVPIGSPIL LLSAGSSSEV TYELREGNKD
1710 1720 1730 1740 1750
SVFSMNSYSG LISTQKRLDH EKVPSYRLRI RGSNMAGVFT EVVALVYIID
1760 1770 1780 1790 1800
ENDNPPAFGK PTFLGHISEA APLHSLILGE DNSPLVVRAS DSDREANSLL
1810 1820 1830 1840 1850
VYKILEPEAL KFFKIDPSMG TLTTTSELDF EDTPLFQFNI YVHDQGTPIL
1860 1870 1880 1890 1900
FAPRSAKVII HVRDVNDSPP RFSEQIYEVA VVEPIHPGMG LLTVQAEDND
1910 1920 1930 1940 1950
SRVTYSIKTS NADEAVTIHP TTGQISVVNP ATLRLFQKFS IRASDGLYHD
1960 1970 1980 1990 2000
TAVVKISLTQ VLDKSLQFDQ DVYRARVTEN TPHRKALVIL GVHGNHLNDT
2010 2020 2030 2040 2050
LSYFLLNGTD LFHMIESAGV LQTRGGTFDR EQQDTHEVAV EVRDNRVPQR
2060 2070 2080 2090 2100
VAQALVRVSV EDVNDNIPEF QHLPYYTVIQ DGTEPGDVLF QVSATDKDLG
2110 2120 2130 2140 2150
ANGSVTYGFA EDYAYFRIDP YVGDISLKKP FDYQALNKYH LRVIARDSGI
2160 2170 2180 2190 2200
PPLQTEVEVH VTVRNKSNPL FQSPYYKVKV PENITLYTPI LHTQARSPEG
2210 2220 2230 2240 2250
LRLIYNIVEE EPLMLFTTDF KTGVLTVTGP LDYESKNKHV FTVRATDTAL
2260 2270 2280 2290 2300
GSFSEATVEV LVEDINDNPP TFSQLVYTTS VSEGSPAQTP VIQLLASDQD
2310 2320 2330 2340 2350
SGQNQDVSYQ IVEDGSDVSK FFRINGSTGE IFTIQELDYE THQHFRVKVR
2360 2370 2380 2390 2400
AMDKGDPPLT GETLVVVNVS DINDNPPKFR EPQYEANVSE LATCGHLVLK
2410 2420 2430 2440 2450
VQALDPDIGD TSRLEYLILS GNQDRHFSIN STSGIISMFN LCKKQLDSSY
2460 2470 2480 2490 2500
NLRVGASDGV FRATVPVYIN TTNANKYSPE FQQNVYEAEL AENAKVGTKV
2510 2520 2530 2540 2550
IELLAIDKDS GPYGTVDYTI INKLAGERFF INPRGQITTL QKLDRENSTE
2560 2570 2580 2590 2600
RVIAIKVMAR DGGGKVAFCT VKIILTDEND NAPQFKASGY TVSIPSNVSR
2610 2620 2630 2640 2650
DSPIIQVLAY DADEGRNADV TYSVDSTEDL AEEIIEVNPT TGVVKVKESL
2660 2670 2680 2690 2700
VGLENRAVDF NIKAQDGGPP HWDSLVPVRL QVVPNEIPLP KFSEPLYTFS
2710 2720 2730 2740 2750
APEDLPEGSE IGSVKAVAAQ DPIIYSLVQG TTPESNSDDV FSLDQDTGVL
2760 2770 2780 2790 2800
KVRKAMDHES TKWYQIDLMA HCPHEDTDLV SLVSVSIQVE DVNDNRPVFE
2810 2820 2830 2840 2850
ADPYKAFLTE NMPGGTTVIQ VTANDQDTGS DGQVSYRLSV EPGSNIHELF
2860 2870 2880 2890 2900
AVDSESGWIT TLQELDCETQ QTYRFYVVAF DHGQTIQLSS QALVEVSITD
2910 2920 2930 2940 2950
ENDNPPRFAS EDYRGSVVEN NEPGELVATL KTLDADVSDQ NRQVTCYITE
2960 2970 2980 2990 3000
GDPLGQFSIS QVGDEWRISS RKTLDREHIA KYLLRVTASD GKFQASVPVE
3010 3020 3030 3040 3050
VFVVDINDNS PQCSQLLYTG KVREDVTPGH FILKVSAIDV DMDTNAQITY
3060 3070 3080 3090 3100
SLHGPGAQEF KLDPHTGELT TLTVLDRERK DVYNLVAKAT DGGGQSCQAE
3110 3120 3130 3140 3150
VTLHIEDVND NAPRFFPSHC DVAVFDNTTV KTPVAVVFAR DPDQGANAQV
3160 3170 3180 3190 3200
VYSLTDSADG QFSIDATSGV IRLEKPLQVR ASSAVELTVR ASDLGTPIPL
3210 3220 3230 3240 3250
STLGTVTVSV VGLEDYLPIF LNAEHSTQVP EDAPIDMEVL HLATLTRPGS
3260 3270 3280 3290 3300
EKTGYHITGG NEQGKFRLDA HTGILYVNGS LDFETNPKYF LSIECSRKSS
3310 3320 3330 3340 3350
SSLSDVTTIV INVTDVNEHH PRFTHDLYTV RVLENAVVGD VILTVSASDD
3360 3370 3380 3390 3400
DGPVNSAITY SLVGGNQLGH FTINPKKGKL QVAKALDWEQ TPSYSLRLRA
3410 3420 3430 3440 3450
TDSGQPPLHE DTEVAVEVVD VNDNPPRFFQ LNYSTSVQEN SPIGIKVLQL
3460 3470 3480 3490 3500
ILDDPDSPQN GPPYFFRITE GNTGSVFRVT PDGWLVTAAS LSKKAREWYQ
3510 3520 3530 3540 3550
LHIEVSDSGL PPLSSSTLVR VQVTEQSRYP PSTLPLEISI TKGEEEFQGG
3560 3570 3580 3590 3600
MIGKIHATDR DPQDTLTYSL EQEGGLDRYF TVGASDGKII ASQGLPHGRY
3610 3620 3630 3640 3650
SFNVTVSDGT FTTTTGVHVH VWHMEPEVPQ QAVWLGFHQL TPEELVSDHW
3660 3670 3680 3690 3700
RNLQRFLSNL LDVKRANIHL ASLQPAEVTA GVDVLLVFER HSGTSYDLQE
3710 3720 3730 3740 3750
LASAIAHSVR EIEHSVGIRM RSALPVVPCQ GQSCQDQTCQ ETVSLEPRVG
3760 3770 3780 3790 3800
PSYSTARLSI LTPRHHLGRN CSCNGTTLRF SGQSYVQYRP LEAQNWQIHF
3810 3820 3830 3840 3850
YLKTLQPWAL LMFTNETASI SLKLANGFSH LEYHCPGGFY GNLSSRYPVN
3860 3870 3880 3890 3900
DGQWHSMLLE ERDTSVHLLV DITDNASLVI PEECQGLRTE RQLLLGGLVP
3910 3920 3930 3940 3950
SNPSSNVSLG FEGCLDAVVV NGERLELLGR EKKMEGRLET WALSQCCWPG
3960 3970 3980 3990 4000
TACSQSPCLN GGSCSPALGS GYLCRCPPPF SGRNCELGRE NCTSAPCQEG
4010 4020 4030 4040 4050
GTCVSSPEGT SCNCPHPYTG DRCEMEARGC SGGHCLITPE IKRGDWGQQE
4060 4070 4080 4090 4100
FLVITVALPL VIIATVGLLL YCRRRKSHKP VTMEDPDLLA RSIGVDTQAS
4110 4120 4130 4140 4150
PAIELDPLNT SSCNNLNQPE PSKTSVPNEL VTFGPSSKQR PMVCSVPPRL
4160 4170 4180 4190 4200
PPAAVSSHPG HEPIIKRTWS GEELVYPSGA AVWPPTYSRK KHWEYPHPET
4210 4220 4230 4240 4250
MQGTLPPSPR RHVGPAVMPD PTGLYGGFPF PLELENKRAP LPPRYSNQNL
4260 4270 4280 4290 4300
EDLMPPRPPS PREHLLAPCL NEYTAISYYH SQFRQGGGGP CLAEGGYKGV
4310 4320 4330 4340 4350
SMRLSRAGPS YADCEVNGGP ATGRSQPRAP PNYEGSDMVE SDYGSCEEVM

F
Length:4,351
Mass (Da):480,654
Last modified:November 1, 1998 - v1
Checksum:iC564E7F98EBB3888
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB011527 mRNA. Translation: BAA32458.1.
PIRiT00252.
RefSeqiNP_075243.1. NM_022954.1.
UniGeneiRn.137161.

Genome annotation databases

GeneIDi65048.
KEGGirno:65048.
UCSCiRGD:620656. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB011527 mRNA. Translation: BAA32458.1 .
PIRi T00252.
RefSeqi NP_075243.1. NM_022954.1.
UniGenei Rn.137161.

3D structure databases

ProteinModelPortali O88277.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 249241. 1 interaction.
STRINGi 10116.ENSRNOP00000017106.

PTM databases

PhosphoSitei O88277.

Proteomic databases

PaxDbi O88277.
PRIDEi O88277.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 65048.
KEGGi rno:65048.
UCSCi RGD:620656. rat.

Organism-specific databases

CTDi 2196.
RGDi 620656. Fat2.

Phylogenomic databases

eggNOGi NOG12793.
HOGENOMi HOG000046499.
HOVERGENi HBG005641.
InParanoidi O88277.
KOi K16506.
PhylomeDBi O88277.

Miscellaneous databases

NextBioi 613888.
PROi O88277.

Gene expression databases

Genevestigatori O88277.

Family and domain databases

Gene3Di 2.60.120.200. 1 hit.
2.60.40.60. 33 hits.
InterProi IPR002126. Cadherin.
IPR015919. Cadherin-like.
IPR020894. Cadherin_CS.
IPR013320. ConA-like_dom.
IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR001791. Laminin_G.
[Graphical view ]
Pfami PF00028. Cadherin. 27 hits.
PF00008. EGF. 2 hits.
PF02210. Laminin_G_2. 1 hit.
[Graphical view ]
PRINTSi PR00205. CADHERIN.
SMARTi SM00112. CA. 33 hits.
SM00181. EGF. 2 hits.
SM00282. LamG. 1 hit.
[Graphical view ]
SUPFAMi SSF49313. SSF49313. 33 hits.
SSF49899. SSF49899. 1 hit.
PROSITEi PS00232. CADHERIN_1. 14 hits.
PS50268. CADHERIN_2. 33 hits.
PS00022. EGF_1. 2 hits.
PS01186. EGF_2. 2 hits.
PS50026. EGF_3. 2 hits.
PS50025. LAM_G_DOMAIN. 1 hit.
[Graphical view ]
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Publicationsi

  1. "Identification of high-molecular-weight proteins with multiple EGF-like motifs by motif-trap screening."
    Nakayama M., Nakajima D., Nagase T., Nomura N., Seki N., Ohara O.
    Genomics 51:27-34(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  2. Lubec G., Kang S.U., Lubec S.
    Submitted (SEP-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 673-681; 2566-2572; 2968-2976 AND 3081-3088, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Brain.
  3. "MEGF1/fat2 proteins containing extraordinarily large extracellular domains are localized to thin parallel fibers of cerebellar granule cells."
    Nakayama M., Nakajima D., Yoshimura R., Endo Y., Ohara O.
    Mol. Cell. Neurosci. 20:563-578(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBUNIT, DEVELOPMENTAL STAGE.

Entry informationi

Entry nameiFAT2_RAT
AccessioniPrimary (citable) accession number: O88277
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 2, 2002
Last sequence update: November 1, 1998
Last modified: October 29, 2014
This is version 113 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3