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Protein

Serum deprivation-response protein

Gene

Sdpr

Organism
Mus musculus (Mouse)
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.By similarity

GO - Molecular functioni

GO - Biological processi

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
Synonyms:Sdr1 Publication
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 1

Organism-specific databases

MGIiMGI:99513. Sdpr.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 418417Serum deprivation-response proteinPRO_0000238919Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylglycineBy similarity
Modified residuei27 – 271PhosphoserineCombined sources
Modified residuei35 – 351PhosphoserineCombined sources
Modified residuei37 – 371PhosphoserineCombined sources
Modified residuei51 – 511PhosphoserineBy similarity
Modified residuei196 – 1961PhosphothreonineBy similarity
Modified residuei203 – 2031PhosphoserineCombined sources
Modified residuei204 – 2041PhosphoserineCombined sources
Modified residuei218 – 2181PhosphoserineCombined sources
Modified residuei283 – 2831PhosphoserineCombined sources
Modified residuei284 – 2841PhosphoserineCombined sources
Modified residuei287 – 2871PhosphoserineCombined sources
Modified residuei288 – 2881PhosphoserineCombined sources
Modified residuei293 – 2931PhosphoserineCombined sources
Modified residuei296 – 2961PhosphoserineCombined sources
Modified residuei327 – 3271PhosphoserineCombined sources
Modified residuei336 – 3361PhosphoserineCombined sources
Modified residuei359 – 3591PhosphoserineCombined sources
Modified residuei363 – 3631PhosphoserineCombined sources
Modified residuei368 – 3681PhosphothreonineCombined sources
Modified residuei388 – 3881PhosphotyrosineCombined sources
Modified residuei390 – 3901PhosphoserineCombined sources
Modified residuei396 – 3961PhosphoserineBy similarity

Post-translational modificationi

The N-terminus is blocked.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiQ63918.
PaxDbiQ63918.
PRIDEiQ63918.

PTM databases

iPTMnetiQ63918.
PhosphoSiteiQ63918.
SwissPalmiQ63918.

Expressioni

Tissue specificityi

Highly expressed in kidney, lung and heart, and expressed at lower levels in liver, spleen, thymus, stomach, intestine and uterus.1 Publication

Developmental stagei

Expression gradually increases during embryonic stages and reaches a maximum in neonates.1 Publication

Inductioni

Up-regulated in response to cardiac hypertrophy and in serum-starved but not in density-dependent growth-arrested NIH3T3 cells. Down-regulated within 6 hours after the addition of serum or epidermal growth factor to serum-starved cells.2 Publications

Gene expression databases

BgeeiQ63918.
CleanExiMM_SDPR.
GenevisibleiQ63918. MM.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

IntActiQ63918. 2 interactions.
MINTiMINT-4114971.
STRINGi10090.ENSMUSP00000055694.

Structurei

3D structure databases

ProteinModelPortaliQ63918.
SMRiQ63918. Positions 54-145.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili61 – 8727Sequence analysisAdd
BLAST
Coiled coili126 – 268143Sequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the PTRF/SDPR family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IEZA. Eukaryota.
ENOG410XP8W. LUCA.
GeneTreeiENSGT00530000063058.
HOGENOMiHOG000293135.
HOVERGENiHBG056807.
InParanoidiQ63918.
OMAiTSNHQKI.
OrthoDBiEOG71G9VF.
PhylomeDBiQ63918.
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.

Q63918-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGEDAAQAEK FQHPNTDMLQ EKPSSPSPMP SSTPSPSLNL GSTEEAIRDN
60 70 80 90 100
SQVNAVTVHT LLDKLVNMLD AVRENQHNME QRQINLEGSV KGIQNDLTKL
110 120 130 140 150
SKYQASTSNT VSKLLEKSRK VSAHTRAVRE RLERQCVQVK RLENNHAQLL
160 170 180 190 200
RRNHFKVLIF QEESEIPASV FVKEPVPSAA EGKEELADEN KSLEETLHNV
210 220 230 240 250
DLSSDDELPR DEEALEDSAE EKMEESRAEK IKRSSLKKVD SLKKAFSRQN
260 270 280 290 300
IEKKMNKLGT KIVSVERREK IKKSLTPNHQ KASSGKSSPF KVSPLSFGRK
310 320 330 340 350
KVREGESSVE NETKLEDQMQ EDREEGSFTE GLSEASLPSG LMEGSAEDAE
360 370 380 390 400
KSARRGNNSA VGSNADLTIE EDEEEEPVAL QQAQQVRYES GYMLNSEEME
410
EPSEKQVQPA VLHVDQTA
Length:418
Mass (Da):46,764
Last modified:January 23, 2007 - v3
Checksum:iEFD7B4E383785F41
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti14 – 141P → L in BAE21104 (PubMed:16141072).Curated
Sequence conflicti76 – 761Q → L in BAC29033 (PubMed:16141072).Curated
Sequence conflicti173 – 1731K → R in BAC29033 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67386 mRNA. Translation: AAB28953.1.
AK035324 mRNA. Translation: BAC29033.1.
AK084096 mRNA. Translation: BAC39116.1.
AK132324 mRNA. Translation: BAE21104.1.
BC020008 mRNA. Translation: AAH20008.1.
BC027005 mRNA. Translation: AAH27005.1.
CCDSiCCDS14940.1.
RefSeqiNP_620080.1. NM_138741.1.
UniGeneiMm.398690.

Genome annotation databases

EnsembliENSMUST00000051572; ENSMUSP00000055694; ENSMUSG00000045954.
GeneIDi20324.
KEGGimmu:20324.
UCSCiuc007axk.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S67386 mRNA. Translation: AAB28953.1.
AK035324 mRNA. Translation: BAC29033.1.
AK084096 mRNA. Translation: BAC39116.1.
AK132324 mRNA. Translation: BAE21104.1.
BC020008 mRNA. Translation: AAH20008.1.
BC027005 mRNA. Translation: AAH27005.1.
CCDSiCCDS14940.1.
RefSeqiNP_620080.1. NM_138741.1.
UniGeneiMm.398690.

3D structure databases

ProteinModelPortaliQ63918.
SMRiQ63918. Positions 54-145.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ63918. 2 interactions.
MINTiMINT-4114971.
STRINGi10090.ENSMUSP00000055694.

PTM databases

iPTMnetiQ63918.
PhosphoSiteiQ63918.
SwissPalmiQ63918.

Proteomic databases

MaxQBiQ63918.
PaxDbiQ63918.
PRIDEiQ63918.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000051572; ENSMUSP00000055694; ENSMUSG00000045954.
GeneIDi20324.
KEGGimmu:20324.
UCSCiuc007axk.1. mouse.

Organism-specific databases

CTDi8436.
MGIiMGI:99513. Sdpr.

Phylogenomic databases

eggNOGiENOG410IEZA. Eukaryota.
ENOG410XP8W. LUCA.
GeneTreeiENSGT00530000063058.
HOGENOMiHOG000293135.
HOVERGENiHBG056807.
InParanoidiQ63918.
OMAiTSNHQKI.
OrthoDBiEOG71G9VF.
PhylomeDBiQ63918.
TreeFamiTF331031.

Miscellaneous databases

ChiTaRSiSdpr. mouse.
PROiQ63918.
SOURCEiSearch...

Gene expression databases

BgeeiQ63918.
CleanExiMM_SDPR.
GenevisibleiQ63918. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "Serum deprivation response gene is induced by serum starvation but not by contact inhibition."
    Gustincich S., Schneider C.
    Cell Growth Differ. 4:753-760(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, INDUCTION.
  2. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported.
    Tissue: Embryonic headImported, Embryonic spinal ganglionImported and Urinary bladderImported.
  3. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6JImported and FVB/NImported.
    Tissue: Mammary glandImported and RetinaImported.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-218 AND SER-293, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  5. "MURC, a muscle-restricted coiled-coil protein that modulates the Rho/ROCK pathway, induces cardiac dysfunction and conduction disturbance."
    Ogata T., Ueyama T., Isodono K., Tagawa M., Takehara N., Kawashima T., Harada K., Takahashi T., Shioi T., Matsubara H., Oh H.
    Mol. Cell. Biol. 28:3424-3436(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, DEVELOPMENTAL STAGE, INDUCTION.
  6. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-288; SER-293; SER-359 AND SER-363, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-27; SER-35; SER-37; SER-203; SER-204; SER-218; SER-283; SER-284; SER-287; SER-288; SER-293; SER-296; SER-327; SER-336; SER-359; SER-363; THR-368; TYR-388 AND SER-390, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiSDPR_MOUSE
AccessioniPrimary (citable) accession number: Q63918
Secondary accession number(s): Q3V1P6, Q78EC3, Q8CBT4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2006
Last sequence update: January 23, 2007
Last modified: June 8, 2016
This is version 112 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. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  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.