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Protein

Serum deprivation-response protein

Gene

Sdpr

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

Functioni

May play a role in targeting PRKCA to caveolae.1 Publication

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Serum deprivation-response protein
Alternative name(s):
Cavin-2
Phosphatidylserine-binding protein
Gene namesi
Name:SdprImported
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 9

Organism-specific databases

RGDi1359345. Sdpr.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00002389202 – 417Serum deprivation-response proteinAdd BLAST416

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylglycineBy similarity1
Modified residuei27PhosphoserineCombined sources1
Modified residuei35PhosphoserineCombined sources1
Modified residuei37PhosphoserineBy similarity1
Modified residuei51PhosphoserineCombined sources1
Modified residuei195PhosphothreonineBy similarity1
Modified residuei202PhosphoserineCombined sources1
Modified residuei203PhosphoserineCombined sources1
Modified residuei217PhosphoserineCombined sources1
Modified residuei282PhosphoserineBy similarity1
Modified residuei283PhosphoserineCombined sources1
Modified residuei286PhosphoserineBy similarity1
Modified residuei287PhosphoserineBy similarity1
Modified residuei292PhosphoserineCombined sources1
Modified residuei295PhosphoserineBy similarity1
Modified residuei326PhosphoserineCombined sources1
Modified residuei335PhosphoserineCombined sources1
Modified residuei358PhosphoserineBy similarity1
Modified residuei362PhosphoserineCombined sources1
Modified residuei367PhosphothreonineBy similarity1
Modified residuei387PhosphotyrosineBy similarity1
Modified residuei389PhosphoserineCombined sources1
Modified residuei395PhosphoserineCombined sources1

Post-translational modificationi

The N-terminus is blocked.By similarity
Phosphorylated on Ser residues.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiQ66H98.
PRIDEiQ66H98.

PTM databases

iPTMnetiQ66H98.
PhosphoSitePlusiQ66H98.

Expressioni

Gene expression databases

BgeeiENSRNOG00000025895.
GenevisibleiQ66H98. RN.

Interactioni

Subunit structurei

Interacts with MURC; this augments the transactivation of NPPA by MURC (By similarity). Binds to PRKCA in the presence of phosphatidylserine.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

BioGridi261332. 1 interactor.
IntActiQ66H98. 1 interactor.
STRINGi10116.ENSRNOP00000030025.

Family & Domainsi

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili61 – 87Sequence analysisAdd BLAST27
Coiled coili126 – 267Sequence analysisAdd BLAST142

Sequence similaritiesi

Belongs to the PTRF/SDPR family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEZA. Eukaryota.
ENOG410XP8W. LUCA.
GeneTreeiENSGT00530000063058.
HOGENOMiHOG000293135.
HOVERGENiHBG056807.
InParanoidiQ66H98.
OMAiERMDRQC.
OrthoDBiEOG091G09Y1.
PhylomeDBiQ66H98.
TreeFamiTF331031.

Family and domain databases

InterProiIPR026752. Cavin_fam.
IPR033298. SDPR.
[Graphical view]
PANTHERiPTHR15240. PTHR15240. 1 hit.
PTHR15240:SF1. PTHR15240:SF1. 1 hit.
PfamiPF15237. PTRF_SDPR. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q66H98-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEDAAQAEK FQHPNTDMLQ EKPSNPSPMP SSTPSPSLNL GSTEEAIRDN
60 70 80 90 100
SQVNAVTVHT LLDKLVNMLD AVRENQHNME QRQINLEGSV KGIQNDLTKL
110 120 130 140 150
SKYQASTSNT VSKLLEKSRK VSAHTRAVRE RLEKQCVQVK RLENNHAQLL
160 170 180 190 200
RRNHFKVLIF QEESEIPASV FVKEPVPSTA EGKELADENK SLEETLHNVD
210 220 230 240 250
LSSDDELPGD EEALEDSAEE KMEESRAEKI KRSSLKKVDS LKKAFSRQNI
260 270 280 290 300
EKKMNKLGTK IVSVERREKI KKSLTPNHQK ASSGKSSPFK VSPLSFGRKK
310 320 330 340 350
IREGESSAEN ETKLEEQVQD DHEEGSFTEG LSEASLPSGL LEGSAEDAEK
360 370 380 390 400
SALRGNNSGV GSNADLTIEE DEEEESVALQ QAQQVRYESG YMLNSKEMEE
410
SSEKHVQAAV LHVDQTA
Length:417
Mass (Da):46,386
Last modified:January 23, 2007 - v3
Checksum:iCA138577B3A4A6A0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC081956 mRNA. Translation: AAH81956.1.
RefSeqiNP_001007713.1. NM_001007712.1.
UniGeneiRn.203035.

Genome annotation databases

EnsembliENSRNOT00000028907; ENSRNOP00000030025; ENSRNOG00000025895.
GeneIDi316384.
KEGGirno:316384.
UCSCiRGD:1359345. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BC081956 mRNA. Translation: AAH81956.1.
RefSeqiNP_001007713.1. NM_001007712.1.
UniGeneiRn.203035.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi261332. 1 interactor.
IntActiQ66H98. 1 interactor.
STRINGi10116.ENSRNOP00000030025.

PTM databases

iPTMnetiQ66H98.
PhosphoSitePlusiQ66H98.

Proteomic databases

PaxDbiQ66H98.
PRIDEiQ66H98.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000028907; ENSRNOP00000030025; ENSRNOG00000025895.
GeneIDi316384.
KEGGirno:316384.
UCSCiRGD:1359345. rat.

Organism-specific databases

CTDi8436.
RGDi1359345. Sdpr.

Phylogenomic databases

eggNOGiENOG410IEZA. Eukaryota.
ENOG410XP8W. LUCA.
GeneTreeiENSGT00530000063058.
HOGENOMiHOG000293135.
HOVERGENiHBG056807.
InParanoidiQ66H98.
OMAiERMDRQC.
OrthoDBiEOG091G09Y1.
PhylomeDBiQ66H98.
TreeFamiTF331031.

Miscellaneous databases

PROiQ66H98.

Gene expression databases

BgeeiENSRNOG00000025895.
GenevisibleiQ66H98. RN.

Family and domain databases

InterProiIPR026752. Cavin_fam.
IPR033298. SDPR.
[Graphical view]
PANTHERiPTHR15240. PTHR15240. 1 hit.
PTHR15240:SF1. PTHR15240:SF1. 1 hit.
PfamiPF15237. PTRF_SDPR. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiSDPR_RAT
AccessioniPrimary (citable) accession number: Q66H98
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 23, 2007
Last modified: November 2, 2016
This is version 84 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Binds phosphatidylserine (PS) in a calcium-independent manner. PS-binding is inhibited by phosphotidic acid and phosphatidylinositol. Does not bind phosphatidylcholine (By similarity).By similarity

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.