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Protein

Neurogenic locus notch homolog protein 3

Gene

Notch3

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

Functioni

Functions as a receptor for membrane-bound ligands Jagged1, Jagged2 and Delta1 to regulate cell-fate determination. Upon ligand activation through the released notch intracellular domain (NICD) it forms a transcriptional activator complex with RBPJ/RBPSUH and activates genes of the enhancer of split locus. Affects the implementation of differentiation, proliferation and apoptotic programs (By similarity). Acts instructively to control the cell fate determination of CNS multipotent progenitor cells, resulting in astroglial induction and neuron/oligodendrocyte suppression.By similarity1 Publication

GO - Molecular functioni

GO - Biological processi

  • cell differentiation Source: UniProtKB-KW
  • multicellular organism development Source: UniProtKB-KW
  • Notch signaling pathway Source: RGD
  • regulation of transcription, DNA-templated Source: RGD
  • tissue regeneration Source: RGD
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Receptor

Keywords - Biological processi

Differentiation, Notch signaling pathway, Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Neurogenic locus notch homolog protein 3
Short name:
Notch 3
Cleaved into the following 2 chains:
Gene namesi
Name:Notch3
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi620761. Notch3.

Subcellular locationi

Notch 3 intracellular domain :
  • Nucleus

  • Note: Following proteolytical processing NICD is translocated to the nucleus.

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini41 – 1645ExtracellularSequence analysisAdd BLAST1605
Transmembranei1646 – 1666HelicalSequence analysisAdd BLAST21
Topological domaini1667 – 2319CytoplasmicSequence analysisAdd BLAST653

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 40Sequence analysisAdd BLAST40
ChainiPRO_000000769841 – 2319Neurogenic locus notch homolog protein 3Add BLAST2279
ChainiPRO_00000076991631 – 2319Notch 3 extracellular truncationBy similarityAdd BLAST689
ChainiPRO_00000077001664 – 2319Notch 3 intracellular domainBy similarityAdd BLAST656

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi44 ↔ 56By similarity
Disulfide bondi50 ↔ 67By similarity
Disulfide bondi69 ↔ 78By similarity
Disulfide bondi84 ↔ 95By similarity
Disulfide bondi89 ↔ 108By similarity
Disulfide bondi110 ↔ 119By similarity
Disulfide bondi125 ↔ 136By similarity
Disulfide bondi130 ↔ 146By similarity
Disulfide bondi148 ↔ 157By similarity
Disulfide bondi164 ↔ 176By similarity
Disulfide bondi170 ↔ 185By similarity
Disulfide bondi187 ↔ 196By similarity
Disulfide bondi203 ↔ 214By similarity
Disulfide bondi208 ↔ 224By similarity
Disulfide bondi226 ↔ 235By similarity
Disulfide bondi242 ↔ 253By similarity
Disulfide bondi247 ↔ 262By similarity
Disulfide bondi264 ↔ 273By similarity
Disulfide bondi280 ↔ 293By similarity
Disulfide bondi287 ↔ 302By similarity
Disulfide bondi304 ↔ 313By similarity
Disulfide bondi320 ↔ 331By similarity
Disulfide bondi325 ↔ 340By similarity
Disulfide bondi342 ↔ 351By similarity
Disulfide bondi357 ↔ 368By similarity
Disulfide bondi362 ↔ 379By similarity
Disulfide bondi381 ↔ 390By similarity
Disulfide bondi397 ↔ 410By similarity
Disulfide bondi404 ↔ 419By similarity
Disulfide bondi421 ↔ 430By similarity
Disulfide bondi437 ↔ 448By similarity
Disulfide bondi442 ↔ 457By similarity
Disulfide bondi459 ↔ 468By similarity
Disulfide bondi475 ↔ 486By similarity
Disulfide bondi480 ↔ 495By similarity
Disulfide bondi497 ↔ 506By similarity
Disulfide bondi513 ↔ 524By similarity
Disulfide bondi518 ↔ 533By similarity
Disulfide bondi535 ↔ 544By similarity
Disulfide bondi551 ↔ 561By similarity
Disulfide bondi556 ↔ 570By similarity
Disulfide bondi572 ↔ 581By similarity
Disulfide bondi588 ↔ 599By similarity
Disulfide bondi593 ↔ 608By similarity
Disulfide bondi610 ↔ 619By similarity
Disulfide bondi626 ↔ 636By similarity
Disulfide bondi631 ↔ 645By similarity
Disulfide bondi647 ↔ 656By similarity
Disulfide bondi663 ↔ 674By similarity
Disulfide bondi668 ↔ 683By similarity
Disulfide bondi685 ↔ 694By similarity
Disulfide bondi701 ↔ 711By similarity
Disulfide bondi706 ↔ 720By similarity
Disulfide bondi722 ↔ 731By similarity
Disulfide bondi740 ↔ 751By similarity
Disulfide bondi745 ↔ 760By similarity
Disulfide bondi762 ↔ 771By similarity
Disulfide bondi777 ↔ 788By similarity
Disulfide bondi782 ↔ 798By similarity
Disulfide bondi800 ↔ 809By similarity
Disulfide bondi816 ↔ 828By similarity
Disulfide bondi822 ↔ 837By similarity
Disulfide bondi839 ↔ 848By similarity
Disulfide bondi855 ↔ 866By similarity
Disulfide bondi860 ↔ 875By similarity
Disulfide bondi877 ↔ 886By similarity
Disulfide bondi893 ↔ 903By similarity
Disulfide bondi898 ↔ 912By similarity
Disulfide bondi914 ↔ 923By similarity
Disulfide bondi930 ↔ 941By similarity
Disulfide bondi935 ↔ 950By similarity
Disulfide bondi952 ↔ 961By similarity
Disulfide bondi968 ↔ 979By similarity
Disulfide bondi973 ↔ 988By similarity
Disulfide bondi990 ↔ 999By similarity
Disulfide bondi1006 ↔ 1017By similarity
Disulfide bondi1011 ↔ 1024By similarity
Disulfide bondi1026 ↔ 1035By similarity
Disulfide bondi1042 ↔ 1063By similarity
Disulfide bondi1057 ↔ 1072By similarity
Disulfide bondi1074 ↔ 1083By similarity
Disulfide bondi1090 ↔ 1101By similarity
Disulfide bondi1095 ↔ 1110By similarity
Disulfide bondi1112 ↔ 1121By similarity
Disulfide bondi1128 ↔ 1139By similarity
Disulfide bondi1133 ↔ 1148By similarity
Disulfide bondi1150 ↔ 1159By similarity
Disulfide bondi1166 ↔ 1184By similarity
Disulfide bondi1178 ↔ 1193By similarity
Glycosylationi1181N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1195 ↔ 1204By similarity
Disulfide bondi1211 ↔ 1224By similarity
Disulfide bondi1216 ↔ 1234By similarity
Disulfide bondi1236 ↔ 1245By similarity
Disulfide bondi1252 ↔ 1263By similarity
Disulfide bondi1257 ↔ 1277By similarity
Disulfide bondi1279 ↔ 1288By similarity
Disulfide bondi1295 ↔ 1306By similarity
Disulfide bondi1300 ↔ 1315By similarity
Disulfide bondi1317 ↔ 1326By similarity
Glycosylationi1338N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1341 ↔ 1352By similarity
Disulfide bondi1346 ↔ 1363By similarity
Disulfide bondi1365 ↔ 1374By similarity
Disulfide bondi1389 ↔ 1412By similarity
Disulfide bondi1394 ↔ 1407By similarity
Disulfide bondi1403 ↔ 1419By similarity
Disulfide bondi1430 ↔ 1453By similarity
Disulfide bondi1435 ↔ 1448By similarity
Glycosylationi1440N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1444 ↔ 1460By similarity
Disulfide bondi1469 ↔ 1495By similarity
Disulfide bondi1477 ↔ 1490By similarity
Disulfide bondi1486 ↔ 1502By similarity
Modified residuei2175Omega-N-methylarginineBy similarity1

Post-translational modificationi

Synthesized in the endoplasmic reticulum as an inactive form which is proteolytically cleaved by a furin-like convertase in the trans-Golgi network before it reaches the plasma membrane to yield an active, ligand-accessible form. Cleavage results in a C-terminal fragment N(TM) and a N-terminal fragment N(EC). Following ligand binding, it is cleaved by TNF-alpha converting enzyme (TACE) to yield a membrane-associated intermediate fragment called notch extracellular truncation (NEXT). This fragment is then cleaved by presenilin dependent gamma-secretase to release a notch-derived peptide containing the intracellular domain (NICD) from the membrane (By similarity).By similarity
Phosphorylated.By similarity
Hydroxylated by HIF1AN.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei1573 – 1574Cleavage; by furin-like proteaseBy similarity2

Keywords - PTMi

Disulfide bond, Glycoprotein, Methylation, Phosphoprotein

Proteomic databases

PaxDbiQ9R172.
PRIDEiQ9R172.

Expressioni

Tissue specificityi

Expressed in postnatal central nervous system (CNS) germinal zones and, in early postnatal life, within numerous cells throughout the CNS. It is more highly localized to ventricular germinal zones.1 Publication

Interactioni

Subunit structurei

Heterodimer of a C-terminal fragment N(TM) and a N-terminal fragment N(EC) which are probably linked by disulfide bonds. Interacts with MAML1, MAML2 and MAML3 which act as transcriptional coactivators for NOTCH3. Interacts with PSMA1 (By similarity). Interacts with HIF1AN (By similarity).By similarity

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000037570.

Structurei

3D structure databases

ProteinModelPortaliQ9R172.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 79EGF-like 1PROSITE-ProRule annotationAdd BLAST39
Domaini80 – 120EGF-like 2PROSITE-ProRule annotationAdd BLAST41
Domaini121 – 158EGF-like 3PROSITE-ProRule annotationAdd BLAST38
Domaini160 – 197EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini199 – 236EGF-like 5PROSITE-ProRule annotationAdd BLAST38
Domaini238 – 274EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini276 – 314EGF-like 7PROSITE-ProRule annotationAdd BLAST39
Domaini316 – 352EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini353 – 391EGF-like 9PROSITE-ProRule annotationAdd BLAST39
Domaini393 – 431EGF-like 10; calcium-bindingPROSITE-ProRule annotationAdd BLAST39
Domaini433 – 469EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini471 – 507EGF-like 12; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini509 – 545EGF-like 13; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini547 – 582EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini584 – 620EGF-like 15; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini622 – 657EGF-like 16; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini659 – 695EGF-like 17; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini697 – 732EGF-like 18PROSITE-ProRule annotationAdd BLAST36
Domaini736 – 772EGF-like 19PROSITE-ProRule annotationAdd BLAST37
Domaini773 – 810EGF-like 20PROSITE-ProRule annotationAdd BLAST38
Domaini812 – 849EGF-like 21; calcium-bindingPROSITE-ProRule annotationAdd BLAST38
Domaini851 – 887EGF-like 22; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini889 – 924EGF-like 23; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini926 – 962EGF-like 24PROSITE-ProRule annotationAdd BLAST37
Domaini964 – 1000EGF-like 25PROSITE-ProRule annotationAdd BLAST37
Domaini1002 – 1036EGF-like 26PROSITE-ProRule annotationAdd BLAST35
Domaini1038 – 1084EGF-like 27PROSITE-ProRule annotationAdd BLAST47
Domaini1086 – 1122EGF-like 28PROSITE-ProRule annotationAdd BLAST37
Domaini1124 – 1160EGF-like 29; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini1162 – 1205EGF-like 30; calcium-bindingPROSITE-ProRule annotationAdd BLAST44
Domaini1207 – 1246EGF-like 31PROSITE-ProRule annotationAdd BLAST40
Domaini1248 – 1289EGF-like 32PROSITE-ProRule annotationAdd BLAST42
Domaini1291 – 1327EGF-like 33PROSITE-ProRule annotationAdd BLAST37
Domaini1337 – 1375EGF-like 34PROSITE-ProRule annotationAdd BLAST39
Repeati1389 – 1429LNR 1Add BLAST41
Repeati1430 – 1467LNR 2Add BLAST38
Repeati1469 – 1507LNR 3Add BLAST39
Repeati1840 – 1869ANK 1Add BLAST30
Repeati1873 – 1903ANK 2Add BLAST31
Repeati1907 – 1936ANK 3Add BLAST30
Repeati1940 – 1969ANK 4Add BLAST30
Repeati1973 – 2002ANK 5Add BLAST30

Sequence similaritiesi

Belongs to the NOTCH family.Curated
Contains 5 ANK repeats.PROSITE-ProRule annotation
Contains 34 EGF-like domains.PROSITE-ProRule annotation
Contains 3 LNR (Lin/Notch) repeats.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiENOG410KD9W. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ9R172.
KOiK02599.
PhylomeDBiQ9R172.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR022331. Notch_3.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 18 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 6 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PRINTSiPR01452. LNOTCHREPEAT.
PR01986. NOTCH3.
SMARTiSM00248. ANK. 6 hits.
SM01334. DUF3454. 1 hit.
SM00181. EGF. 34 hits.
SM00179. EGF_CA. 30 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 5 hits.
SSF90193. SSF90193. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 18 hits.
PS00022. EGF_1. 33 hits.
PS01186. EGF_2. 26 hits.
PS50026. EGF_3. 34 hits.
PS01187. EGF_CA. 16 hits.
PS50258. LNR. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q9R172-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGPGARGRRR RRRLMALPPP PPPMRALPLL LLLLAGLGAA APPCLDGSPC
60 70 80 90 100
ANGGRCTHQQ PSREAACLCL PGWVGERCQL EDPCHSGPCA GRGVCQSSVV
110 120 130 140 150
AGVARFSCRC LRGFRGPDCS LPDPCFSSPC AHGAPCSVGS DGRYACACPP
160 170 180 190 200
GYQGRNCRSD IDECRAGASC RHGGTCINTP GSFHCLCPLG YTGLLCENPI
210 220 230 240 250
VPCAPSPCRN GGTCRQSSDV TYDCACLPGF EGQNCEVNVD DCPGHRCLNG
260 270 280 290 300
GTCVDGVNTY NCQCPPEWTG QFCTEDVDEC QLQPNACHNG GTCFNLLGGH
310 320 330 340 350
SCVCVNGWTG ESCSQNIDDC ATAVCFHGAT CHDRVASFYC ACPMGKTGLL
360 370 380 390 400
CHLDDACVSN PCHEDAICDT NPVSGRAICT CPPGFTGGAC DQDVDECSIG
410 420 430 440 450
ANPCEHLGRC VNTQGSFLCQ CGRGYTGPRC ETDVNECLSG PCRNQATCLD
460 470 480 490 500
RIGQFTCICM AGFTGTFCEV DIDECQSSPC VNGGVCKDRV NGFSCTCPSG
510 520 530 540 550
FSGSTCQLDV DECASTPCRN GAKCVDQPDG YECRCAEGFE GTLCERNVDD
560 570 580 590 600
CSPDPCHHGR CVDGIASFSC ACAPGYTGIR CESQVDECRS QPCRYGGKCL
610 620 630 640 650
DLVDKYLCRC PPGTTGVNCE VNIDDCASNP CTFGVCRDGI NRYDCVCQPG
660 670 680 690 700
FTGPLCNVEI NECASSPCGE GGSCVDGENG FHCLCPPGSL PPLCLPANHP
710 720 730 740 750
CAHKPCSHGV CHDAPGGFQC VCDPGWSGPR CSQSLAPDAC ESQPCQAGGT
760 770 780 790 800
CTSDGIGFHC TCAPGFQGHQ CEVLSPCTPS LCEHGGHCES DPDQLTVCSC
810 820 830 840 850
PPGWQGPRCQ QDVDECAGAS PCGPHGTCTN LPGSFRCICH GGYTGPFCDQ
860 870 880 890 900
DIDDCDPNPC LNGGSCQDGV GSFSCSCLSG FAGPRCARDV DECLSSPCGP
910 920 930 940 950
GTCTDHVASF TCTCPPGYGG FHCETDLLDC SPSSCFNGGT CVDGVNSFSC
960 970 980 990 1000
LCRPGYTGTH CQYKVDPCFS RPCLHGGICN PTHSGFECTC REGFTGNQCQ
1010 1020 1030 1040 1050
NPVDWCSQAP CQNGGRCVQT GAYCICPPEW SGPLCDIPSL PCTEAAAHMG
1060 1070 1080 1090 1100
VRLEQLCQAG GQCIDKDHSH YCVCPEGRMG SHCEQEVDPC TAQPCQHGGT
1110 1120 1130 1140 1150
CRGYMGGYVC ECPTGYSGDS CEDDVDECAS QPCQNGGSCI DLVAHYLCSC
1160 1170 1180 1190 1200
PPGTLGVLCE INEDDCGPGP SLDSGLRCLH NGTCVDLVGG FRCNCPPGYT
1210 1220 1230 1240 1250
GLHCEADINE CRPGTCHAAH TRDCLQDPGG HFRCICLPGF TGPRCQTALF
1260 1270 1280 1290 1300
PCESQPCQHG GQCRPSLGRG GGLTFTCHCV QPFWGLRCER VARSCRELQC
1310 1320 1330 1340 1350
PVGIPCQQTA RGPRCACPPG LSGPSCRVSR ASPSGATNTS CAATPCLHGG
1360 1370 1380 1390 1400
SCLPVQSVPF FRCVCAPGWG GPRCETPSAA PEVPEEPRCP RAACQAKRGD
1410 1420 1430 1440 1450
QNCDRECNSP GCGWDGGDCS LNVDDPWRQC EALQCWRLFN NSRCDPACSS
1460 1470 1480 1490 1500
PACLYDNFDC YSGGRDRTCN PVYKKYCADH FADGRCDQGC NTEECGWDGL
1510 1520 1530 1540 1550
DCASEVPALL ARGVLVLTVL LPPEELLRSS ADFLQRLSAI LRTSLRFRLD
1560 1570 1580 1590 1600
ARGQAMVFPY HRPSPGSESR VRRELGPEVI GSVVMLEIDN RLCLKSAEND
1610 1620 1630 1640 1650
HCFPDAQSAA DYLGALSAVE RLDFPYPLRD VRGEPLEPPE QSVPLLPLLV
1660 1670 1680 1690 1700
AGAVFLLVIF VLGVMVARRK REHSTLWFPE GFALHKDIAA GHKGRREPVG
1710 1720 1730 1740 1750
QDALGMKNMT KGESLMGEVA TDWNDSECPE AKRLKVEEPG MGAEEPVDCR
1760 1770 1780 1790 1800
QWTQHHLVAA DIRVAPAMAL TPPQGDADAD GMDVNVRGPD GFTPLMLASF
1810 1820 1830 1840 1850
CGGALEPMPA EEDEADDTSA SIISDLICQG AQLGARTDRT GETALHLAAR
1860 1870 1880 1890 1900
YARADAAKRL LDAGADTNAQ DHSGRTPLHT AVTADAQGVF QILIRNRSTD
1910 1920 1930 1940 1950
LDARMADGST ALILAARLAV EGMVEELIAS HADVNAVDEL GKSALHWAAA
1960 1970 1980 1990 2000
VNNVEATLAL LKNGANKDMQ DSKEETPLFL AAREGSYEAA KLLLDHFANR
2010 2020 2030 2040 2050
EITDHLDRLP RDVAQERLHQ DIVRLLDQPS GPRSPSGPHG LGPLLCPPGA
2060 2070 2080 2090 2100
FLPGLKAVQS GTKKSRRPPG KTGLGPQGTR GRGKKLTLAC PGPLADSSVT
2110 2120 2130 2140 2150
LSPVDSLDSP RPFGGPPASP GGFPLEGPYA TTATTVSLAQ LGASRAGPLG
2160 2170 2180 2190 2200
RQPPGGCVLS LGLLNPVAVP LDWARLPPPA PPGPSFLLPL APGSQLLNPA
2210 2220 2230 2240 2250
TPVSPHERPP PYLAAPGHGE EYPAAGTHSS PTKARFLRVP SEHPYLTPSP
2260 2270 2280 2290 2300
ESPEHWASPS PPSLSDWSDS TPSPATATSA TAAGALPAQP HPISVPSLPQ
2310
SQTQLGPQPE VTPKRQVMA
Length:2,319
Mass (Da):244,301
Last modified:March 1, 2001 - v2
Checksum:i243BCA02D7C3283D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164486 mRNA. Translation: AAD46653.2.
RefSeqiNP_064472.2. NM_020087.2.
UniGeneiRn.228683.

Genome annotation databases

GeneIDi56761.
KEGGirno:56761.
UCSCiRGD:620761. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF164486 mRNA. Translation: AAD46653.2.
RefSeqiNP_064472.2. NM_020087.2.
UniGeneiRn.228683.

3D structure databases

ProteinModelPortaliQ9R172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000037570.

Proteomic databases

PaxDbiQ9R172.
PRIDEiQ9R172.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi56761.
KEGGirno:56761.
UCSCiRGD:620761. rat.

Organism-specific databases

CTDi4854.
RGDi620761. Notch3.

Phylogenomic databases

eggNOGiENOG410KD9W. Eukaryota.
COG0666. LUCA.
HOGENOMiHOG000234369.
HOVERGENiHBG052650.
InParanoidiQ9R172.
KOiK02599.
PhylomeDBiQ9R172.

Miscellaneous databases

PROiQ9R172.

Family and domain databases

Gene3Di1.25.40.20. 1 hit.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
IPR024600. DUF3454_notch.
IPR001881. EGF-like_Ca-bd_dom.
IPR013032. EGF-like_CS.
IPR000742. EGF-like_dom.
IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
IPR018097. EGF_Ca-bd_CS.
IPR009030. Growth_fac_rcpt_.
IPR022331. Notch_3.
IPR000800. Notch_dom.
IPR010660. Notch_NOD_dom.
IPR011656. Notch_NODP_dom.
[Graphical view]
PfamiPF12796. Ank_2. 2 hits.
PF11936. DUF3454. 1 hit.
PF00008. EGF. 18 hits.
PF07645. EGF_CA. 5 hits.
PF12661. hEGF. 6 hits.
PF06816. NOD. 1 hit.
PF07684. NODP. 1 hit.
PF00066. Notch. 3 hits.
[Graphical view]
PRINTSiPR01452. LNOTCHREPEAT.
PR01986. NOTCH3.
SMARTiSM00248. ANK. 6 hits.
SM01334. DUF3454. 1 hit.
SM00181. EGF. 34 hits.
SM00179. EGF_CA. 30 hits.
SM00004. NL. 3 hits.
SM01338. NOD. 1 hit.
SM01339. NODP. 1 hit.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
SSF57184. SSF57184. 5 hits.
SSF90193. SSF90193. 3 hits.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 4 hits.
PS00010. ASX_HYDROXYL. 18 hits.
PS00022. EGF_1. 33 hits.
PS01186. EGF_2. 26 hits.
PS50026. EGF_3. 34 hits.
PS01187. EGF_CA. 16 hits.
PS50258. LNR. 3 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiNOTC3_RAT
AccessioniPrimary (citable) accession number: Q9R172
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: March 1, 2001
Last modified: November 2, 2016
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.