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Protein

Protein serrate

Gene

Ser

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

Functioni

Acts as a ligand for Notch (N) receptor. Essential for proper ectodermal development. Serrate represents an element in a network of interacting molecules operating at the cell surface during the differentiation of certain tissues.

GO - Molecular functioni

  • calcium ion binding Source: InterPro
  • Notch binding Source: FlyBase
  • receptor binding Source: FlyBase

GO - Biological processi

  • compound eye development Source: FlyBase
  • crystal cell differentiation Source: FlyBase
  • cuticle pattern formation Source: FlyBase
  • dorsal/ventral lineage restriction, imaginal disc Source: FlyBase
  • eye-antennal disc development Source: FlyBase
  • germ-line stem cell population maintenance Source: FlyBase
  • glial cell proliferation Source: FlyBase
  • imaginal disc-derived leg segmentation Source: FlyBase
  • imaginal disc-derived wing morphogenesis Source: FlyBase
  • larval lymph gland hemopoiesis Source: FlyBase
  • larval salivary gland morphogenesis Source: FlyBase
  • lateral inhibition Source: FlyBase
  • lymph gland crystal cell differentiation Source: FlyBase
  • negative regulation of Notch signaling pathway Source: FlyBase
  • Notch signaling pathway Source: FlyBase
  • regulation of crystal cell differentiation Source: FlyBase
  • salivary gland development Source: FlyBase
  • salivary gland morphogenesis Source: FlyBase
  • second mitotic wave involved in compound eye morphogenesis Source: FlyBase
  • sensory organ development Source: FlyBase
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation

Enzyme and pathway databases

ReactomeiR-DME-1980148. Signaling by NOTCH3.
R-DME-1980150. Signaling by NOTCH4.
R-DME-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-DME-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
SignaLinkiP18168.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein serrate
Alternative name(s):
Protein beaded
Gene namesi
Name:Ser
Synonyms:Bd
ORF Names:CG6127
OrganismiDrosophila melanogaster (Fruit fly)
Taxonomic identifieri7227 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
Proteomesi
  • UP000000803 Componenti: Chromosome 3R

Organism-specific databases

FlyBaseiFBgn0004197. Ser.

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini80 – 1219ExtracellularSequence analysisAdd BLAST1140
Transmembranei1220 – 1245HelicalSequence analysisAdd BLAST26
Topological domaini1246 – 1404CytoplasmicSequence analysisAdd BLAST159

GO - Cellular componenti

  • apical plasma membrane Source: FlyBase
  • axolemma Source: FlyBase
  • cell surface Source: FlyBase
  • integral component of membrane Source: FlyBase
  • plasma membrane Source: FlyBase
Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 79Sequence analysisAdd BLAST79
ChainiPRO_000000771880 – 1404Protein serrateAdd BLAST1325

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Glycosylationi148N-linked (GlcNAc...)Sequence analysis1
Glycosylationi192N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi237 ↔ 246By similarity
Glycosylationi243N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi250 ↔ 262By similarity
Disulfide bondi270 ↔ 279By similarity
Disulfide bondi284 ↔ 295By similarity
Disulfide bondi288 ↔ 301By similarity
Disulfide bondi303 ↔ 312By similarity
Disulfide bondi315 ↔ 326By similarity
Disulfide bondi321 ↔ 333By similarity
Glycosylationi327N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi335 ↔ 344By similarity
Disulfide bondi351 ↔ 363By similarity
Disulfide bondi357 ↔ 373By similarity
Disulfide bondi375 ↔ 384By similarity
Disulfide bondi391 ↔ 402By similarity
Disulfide bondi396 ↔ 473By similarity
Glycosylationi408N-linked (GlcNAc...)Sequence analysis1
Glycosylationi448N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi475 ↔ 484By similarity
Disulfide bondi491 ↔ 502By similarity
Disulfide bondi496 ↔ 511By similarity
Disulfide bondi513 ↔ 522By similarity
Disulfide bondi529 ↔ 584By similarity
Glycosylationi554N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi578 ↔ 593By similarity
Disulfide bondi595 ↔ 604By similarity
Disulfide bondi611 ↔ 621By similarity
Disulfide bondi615 ↔ 630By similarity
Disulfide bondi632 ↔ 641By similarity
Disulfide bondi648 ↔ 659By similarity
Disulfide bondi653 ↔ 668By similarity
Disulfide bondi670 ↔ 679By similarity
Disulfide bondi686 ↔ 696By similarity
Disulfide bondi691 ↔ 705By similarity
Disulfide bondi707 ↔ 716By similarity
Glycosylationi735N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi766 ↔ 781By similarity
Disulfide bondi783 ↔ 792By similarity
Disulfide bondi799 ↔ 810By similarity
Disulfide bondi804 ↔ 819By similarity
Disulfide bondi821 ↔ 830By similarity
Disulfide bondi837 ↔ 848By similarity
Disulfide bondi842 ↔ 861By similarity
Disulfide bondi863 ↔ 872By similarity
Disulfide bondi879 ↔ 890By similarity
Disulfide bondi884 ↔ 899By similarity
Disulfide bondi901 ↔ 910By similarity
Disulfide bondi917 ↔ 928By similarity
Disulfide bondi922 ↔ 937By similarity
Disulfide bondi939 ↔ 948By similarity
Glycosylationi961N-linked (GlcNAc...)Sequence analysis1
Glycosylationi973N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1000N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1026N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1146N-linked (GlcNAc...)Sequence analysis1
Modified residuei1292Phosphoserine1 Publication1

Post-translational modificationi

Ubiquitinated by mind-bomb, leading to its endocytosis and subsequent degradation.Curated

Keywords - PTMi

Disulfide bond, Glycoprotein, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP18168.
PRIDEiP18168.

PTM databases

iPTMnetiP18168.

Expressioni

Tissue specificityi

Restricted exclusively to cells of ectodermal origin.

Gene expression databases

BgeeiFBgn0004197.
GenevisibleiP18168. DM.

Interactioni

GO - Molecular functioni

  • Notch binding Source: FlyBase
  • receptor binding Source: FlyBase

Protein-protein interaction databases

BioGridi68163. 20 interactors.
IntActiP18168. 2 interactors.
MINTiMINT-1639801.
STRINGi7227.FBpp0084498.

Structurei

3D structure databases

ProteinModelPortaliP18168.
SMRiP18168.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini235 – 279DSLPROSITE-ProRule annotationAdd BLAST45
Domaini280 – 313EGF-like 1PROSITE-ProRule annotationAdd BLAST34
Domaini311 – 345EGF-like 2PROSITE-ProRule annotationAdd BLAST35
Domaini347 – 385EGF-like 3PROSITE-ProRule annotationAdd BLAST39
Domaini387 – 485EGF-like 4PROSITE-ProRule annotationAdd BLAST99
Domaini487 – 523EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini525 – 605EGF-like 6; calcium-bindingPROSITE-ProRule annotationAdd BLAST81
Domaini607 – 642EGF-like 7; calcium-bindingPROSITE-ProRule annotationAdd BLAST36
Domaini644 – 680EGF-like 8; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini682 – 717EGF-like 9PROSITE-ProRule annotationAdd BLAST36
Domaini719 – 793EGF-like 10PROSITE-ProRule annotationAdd BLAST75
Domaini795 – 831EGF-like 11; calcium-bindingPROSITE-ProRule annotationAdd BLAST37
Domaini833 – 873EGF-like 12PROSITE-ProRule annotationAdd BLAST41
Domaini875 – 911EGF-like 13PROSITE-ProRule annotationAdd BLAST37
Domaini913 – 949EGF-like 14; calcium-bindingPROSITE-ProRule annotationAdd BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi403 – 472Ser-richAdd BLAST70
Compositional biasi733 – 765Thr-richAdd BLAST33

Sequence similaritiesi

Contains 1 DSL domain.PROSITE-ProRule annotation
Contains 14 EGF-like domains.PROSITE-ProRule annotation

Keywords - Domaini

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

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
ENOG410XP6K. LUCA.
InParanoidiP18168.
KOiK06052.
OrthoDBiEOG091G0A88.
PhylomeDBiP18168.

Family and domain databases

InterProiIPR001774. DSL.
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_.
IPR026219. Jagged/Serrate.
IPR011651. Notch_ligand_N.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01414. DSL. 1 hit.
PF00008. EGF. 6 hits.
PF07645. EGF_CA. 1 hit.
PF12661. hEGF. 2 hits.
PF07657. MNNL. 1 hit.
[Graphical view]
PRINTSiPR02059. JAGGEDFAMILY.
SMARTiSM00051. DSL. 1 hit.
SM00181. EGF. 14 hits.
SM00179. EGF_CA. 9 hits.
SM00215. VWC_out. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 7 hits.
PS51051. DSL. 1 hit.
PS00022. EGF_1. 14 hits.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 13 hits.
PS01187. EGF_CA. 5 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P18168-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MFRKHFRRKP ATSSSLESTI ESADSLGMSK KTATKRQRPR HRVPKIATLP
60 70 80 90 100
STIRDCRSLK SACNLIALIL ILLVHKISAA GNFELEILEI SNTNSHLLNG
110 120 130 140 150
YCCGMPAELR ATKTIGCSPC TTAFRLCLKE YQTTEQGASI STGCSFGNAT
160 170 180 190 200
TKILGGSSFV LSDPGVGAIV LPFTFRWTKS FTLILQALDM YNTSYPDAER
210 220 230 240 250
LIEETSYSGV ILPSPEWKTL DHIGRNARIT YRVRVQCAVT YYNTTCTTFC
260 270 280 290 300
RPRDDQFGHY ACGSEGQKLC LNGWQGVNCE EAICKAGCDP VHGKCDRPGE
310 320 330 340 350
CECRPGWRGP LCNECMVYPG CKHGSCNGSA WKCVCDTNWG GILCDQDLNF
360 370 380 390 400
CGTHEPCKHG GTCENTAPDK YRCTCAEGLS GEQCEIVEHP CATRPCRNGG
410 420 430 440 450
TCTLKTSNRT QAQVYRTSHG RSNMGRPVRR SSSMRSLDHL RPEGQALNGS
460 470 480 490 500
SSPGLVSLGS LQLQQQLAPD FTCDCAAGWT GPTCEINIDE CAGGPCEHGG
510 520 530 540 550
TCIDLIGGFR CECPPEWHGD VCQVDVNECE APHSAGIAAN ALLTTTATAI
560 570 580 590 600
IGSNLSSTAL LAALTSAVAS TSLAIGPCIN AKECRNQPGS FACICKEGWG
610 620 630 640 650
GVTCAENLDD CVGQCRNGAT CIDLVNDYRC ACASGFKGRD CETDIDECAT
660 670 680 690 700
SPCRNGGECV DMVGKFNCIC PLGYSGSLCE EAKENCTPSP CLEGHCLNTP
710 720 730 740 750
EGYYCHCPPD RAGKHCEQLR PLCSQPPCNE GCFANVSLAT SATTTTTTTT
760 770 780 790 800
TATTTRKMAK PSGLPCSGHG SCEMSDVGTF CKCHVGHTGT FCEHNLNECS
810 820 830 840 850
PNPCRNGGIC LDGDGDFTCE CMSGWTGKRC SERATGCYAG QCQNGGTCMP
860 870 880 890 900
GAPDKALQPH CRCAPGWTGL FCAEAIDQCR GQPCHNGGTC ESGAGWFRCV
910 920 930 940 950
CAQGFSGPDC RINVNECSPQ PCQGGATCID GIGGYSCICP PGRHGLRCEI
960 970 980 990 1000
LLSDPKSACQ NASNTISPYT ALNRSQNWLD IALTGRTEDD ENCNACVCEN
1010 1020 1030 1040 1050
GTSRCTNLWC GLPNCYKVDP LSKSSNLSGV CKQHEVCVPA LSETCLSSPC
1060 1070 1080 1090 1100
NVRGDCRALE PSRRVAPPRL PAKSSCWPNQ AVVNENCARL TILLALERVG
1110 1120 1130 1140 1150
KGASVEGLCS LVRVLLAAQL IKKPASTFGQ DPGMLMVLCD LKTGTNDTVE
1160 1170 1180 1190 1200
LTVSSSKLND PQLPVAVGLL GELLSFRQLN GIQRRKELEL QHAKLAALTS
1210 1220 1230 1240 1250
IVEVKLETAR VADGSGHSLL IGVLCGVFIV LVGFSVFISL YWKQRLAYRT
1260 1270 1280 1290 1300
SSGMNLTPSL DALRHEEEKS NNLQNEENLR RYTNPLKGST SSLRAATGME
1310 1320 1330 1340 1350
LSLNPAPELA ASAASSSALH RSQPLFPPCD FERELDSSTG LKQAHKRSSQ
1360 1370 1380 1390 1400
ILLHKTQNSD MRKNTVGSLD SPRKDFGKRS INCKSMPPSS GDEGSDVLAT

TVMV
Length:1,404
Mass (Da):150,344
Last modified:June 21, 2005 - v3
Checksum:iE988604001DAAC84
GO

Sequence cautioni

The sequence AAF56678 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti15S → SSLSS in CAA40148 (PubMed:1840519).Curated1
Sequence conflicti23A → P in CAA40148 (PubMed:1840519).Curated1
Sequence conflicti453P → S in AAA28938 (PubMed:2125287).Curated1
Sequence conflicti453P → S in CAA40148 (PubMed:1840519).Curated1
Sequence conflicti637K → T in AAA28938 (PubMed:2125287).Curated1
Sequence conflicti637K → T in CAA40148 (PubMed:1840519).Curated1
Sequence conflicti1176F → S in AAA28938 (PubMed:2125287).Curated1
Sequence conflicti1176F → S in CAA40148 (PubMed:1840519).Curated1
Sequence conflicti1348S → T in CAA40148 (PubMed:1840519).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35759 mRNA. Translation: AAA28938.1.
X56811 mRNA. Translation: CAA40148.1.
AE014297 Genomic DNA. Translation: AAF56678.2. Different initiation.
PIRiS16148.
RefSeqiNP_001287558.1. NM_001300629.1.
NP_524527.3. NM_079803.3.

Genome annotation databases

GeneIDi43275.
KEGGidme:Dmel_CG6127.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M35759 mRNA. Translation: AAA28938.1.
X56811 mRNA. Translation: CAA40148.1.
AE014297 Genomic DNA. Translation: AAF56678.2. Different initiation.
PIRiS16148.
RefSeqiNP_001287558.1. NM_001300629.1.
NP_524527.3. NM_079803.3.

3D structure databases

ProteinModelPortaliP18168.
SMRiP18168.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi68163. 20 interactors.
IntActiP18168. 2 interactors.
MINTiMINT-1639801.
STRINGi7227.FBpp0084498.

PTM databases

iPTMnetiP18168.

Proteomic databases

PaxDbiP18168.
PRIDEiP18168.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi43275.
KEGGidme:Dmel_CG6127.

Organism-specific databases

CTDi43275.
FlyBaseiFBgn0004197. Ser.

Phylogenomic databases

eggNOGiKOG1217. Eukaryota.
ENOG410XP6K. LUCA.
InParanoidiP18168.
KOiK06052.
OrthoDBiEOG091G0A88.
PhylomeDBiP18168.

Enzyme and pathway databases

ReactomeiR-DME-1980148. Signaling by NOTCH3.
R-DME-1980150. Signaling by NOTCH4.
R-DME-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-DME-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
SignaLinkiP18168.

Miscellaneous databases

GenomeRNAii43275.
PROiP18168.

Gene expression databases

BgeeiFBgn0004197.
GenevisibleiP18168. DM.

Family and domain databases

InterProiIPR001774. DSL.
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_.
IPR026219. Jagged/Serrate.
IPR011651. Notch_ligand_N.
IPR001007. VWF_dom.
[Graphical view]
PfamiPF01414. DSL. 1 hit.
PF00008. EGF. 6 hits.
PF07645. EGF_CA. 1 hit.
PF12661. hEGF. 2 hits.
PF07657. MNNL. 1 hit.
[Graphical view]
PRINTSiPR02059. JAGGEDFAMILY.
SMARTiSM00051. DSL. 1 hit.
SM00181. EGF. 14 hits.
SM00179. EGF_CA. 9 hits.
SM00215. VWC_out. 1 hit.
[Graphical view]
SUPFAMiSSF57184. SSF57184. 1 hit.
PROSITEiPS00010. ASX_HYDROXYL. 7 hits.
PS51051. DSL. 1 hit.
PS00022. EGF_1. 14 hits.
PS01186. EGF_2. 8 hits.
PS50026. EGF_3. 13 hits.
PS01187. EGF_CA. 5 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSERR_DROME
AccessioniPrimary (citable) accession number: P18168
Secondary accession number(s): Q9VB65
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: June 21, 2005
Last modified: November 30, 2016
This is version 163 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

Miscellaneousi

Miscellaneous

Separation of neuroblasts from the ectoderm into the inner part of embryo is one of the first steps of CNS development in insects, this process is under control of the neurogenic genes.
Notch and Serrate may interact at the protein level, it is conceivable that the Serrate and Delta proteins may compete for binding with the Notch protein.

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.