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Protein

Oxysterol-binding protein-related protein 3

Gene

Osbpl3

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Phosphoinositide-binding protein which associates with both cell and endoplasmic reticulum (ER) membranes. Can bind to the ER membrane protein VAPA and recruit VAPA to plasma membrane sites, thus linking these intracellular compartments. The ORP3-VAPA complex stimulates RRAS signaling which in turn attenuates integrin beta-1 (ITGB1) activation at the cell surface. With VAPA, may regulate ER morphology. Has a role in regulation of the actin cytoskeleton, cell polarity and cell adhesion. Binds to phosphoinositides with preference for PI(3,4)P2 and PI(3,4,5)P3. Also binds 25-hydroxycholesterol and cholesterol.By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Lipid-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Oxysterol-binding protein-related protein 3
Short name:
ORP-3
Short name:
OSBP-related protein 3
Gene namesi
Name:Osbpl3
Synonyms:Orp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 6

Organism-specific databases

MGIiMGI:1918970. Osbpl3.

Subcellular locationi

  • Endoplasmic reticulum membrane By similarity; Peripheral membrane protein By similarity
  • Cytoplasmcytosol By similarity
  • Cell membrane By similarity; Peripheral membrane protein By similarity
  • Cell projectionfilopodium tip By similarity
  • Nucleus membrane By similarity; Peripheral membrane protein Curated

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Cell projection, Cytoplasm, Endoplasmic reticulum, Membrane, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 855855Oxysterol-binding protein-related protein 3PRO_0000100372Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151PhosphoserineBy similarity
Modified residuei33 – 331PhosphoserineCombined sources
Modified residuei199 – 1991PhosphoserineBy similarity
Modified residuei250 – 2501PhosphoserineBy similarity
Modified residuei272 – 2721PhosphoserineCombined sources
Modified residuei277 – 2771PhosphoserineBy similarity
Modified residuei288 – 2881PhosphoserineBy similarity
Modified residuei291 – 2911PhosphoserineBy similarity
Modified residuei340 – 3401PhosphoserineBy similarity
Modified residuei393 – 3931PhosphoserineBy similarity
Modified residuei405 – 4051PhosphoserineBy similarity
Modified residuei408 – 4081PhosphoserineBy similarity

Post-translational modificationi

Phosphorylation is enhanced in vitro by phorbol-12-myristate-13-acetate (PMA), forskolin and calcium ionophore A23187. Phosphorylation seems to be stimulated in conditions of low cell-cell (or cell-matrix) adhesion.By similarity

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9DBS9.
MaxQBiQ9DBS9.
PaxDbiQ9DBS9.
PRIDEiQ9DBS9.

PTM databases

iPTMnetiQ9DBS9.
PhosphoSiteiQ9DBS9.

Expressioni

Tissue specificityi

Expressed in spinal ganglia. Expressed in a subset of small lymphocytes (at protein level).1 Publication

Developmental stagei

Expressed at higher levels in some regions of the developing central and peripheral nervous system, including hippocampal neuroepithelium, rhinencephalon, intermediate thalamus.1 Publication

Gene expression databases

BgeeiQ9DBS9.
CleanExiMM_OSBPL3.
ExpressionAtlasiQ9DBS9. baseline and differential.
GenevisibleiQ9DBS9. MM.

Interactioni

Subunit structurei

Homodimer. Interacts with RRAS. Interacts (phosphorylated form) with VAPA.By similarity

Protein-protein interaction databases

BioGridi214879. 1 interaction.
STRINGi10090.ENSMUSP00000110112.

Structurei

3D structure databases

ProteinModelPortaliQ9DBS9.
SMRiQ9DBS9. Positions 47-146, 480-855.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini50 – 14596PHPROSITE-ProRule annotationAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi161 – 1677FFAT 1By similarity
Motifi450 – 4545FFAT 2By similarity

Domaini

The FFAT 2 motif is required for interaction with VAPA and regulation of the endoplasmic reticulum targeting of ORP3. The FFAT 1 motif may contribute to VAPA binding.By similarity
The PH domain binds phosphoinositides, with a preference for PI(3,4)P2 and PI(3,4,5)P3. The PH domain mediates targeting to the plasma membrane.By similarity

Sequence similaritiesi

Belongs to the OSBP family.Curated
Contains 1 PH domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG1737. Eukaryota.
ENOG410XP9E. LUCA.
GeneTreeiENSGT00760000119155.
HOGENOMiHOG000231072.
HOVERGENiHBG058934.
InParanoidiQ9DBS9.
OrthoDBiEOG780RKR.
TreeFamiTF320922.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 2 hits.
PfamiPF01237. Oxysterol_BP. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9DBS9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDEKNLGVS QKLVSPSRST SSCSSKQGSR QDSWEVVEGL RGEMTYTQEP
60 70 80 90 100
PVQKGFLLKK RKWPLKGWHK RFFCLEKGIL KYAKSQADIE REKLHGCIDV
110 120 130 140 150
GLSVMSVKKS SKCIDLDTEE HIYHLKVKSE ELFDEWVSKL RHHRMYRQNE
160 170 180 190 200
IAMFPRDVNH FFSGSSVTDS APGVFESVSS RKRSSLSKQN SFPPGSNLSF
210 220 230 240 250
SCGGDTRVPF WLQSSEDMEK CSKDMAHCHA YLLEMSQLLE SMDVLHRTYS
260 270 280 290 300
APAINAIQVP KPFSGPVRLH SSNPNLSTLD FGEEKSYSDG SEASSEFSKM
310 320 330 340 350
QEDLCHVAHK VYFALRSAFN SISVEREKLK QLMELDTSPS PSAQVVGLKH
360 370 380 390 400
ALSSALAQNT DLKERLRRIH AESLLLDPPA VPKPGDNLAE ENSRDEGRAL
410 420 430 440 450
VHQLSNESRL SITDSLSEFF DAQEVLLSPS SSENEISDDD SYVSDISDNL
460 470 480 490 500
SLDNLSNDLD NERQTLGPVL ESSGEARSKR RTSLPAPGPN TSSVSLWSIL
510 520 530 540 550
RNNIGKDLSK VAMPVELNEP LNTLQRLCEE LEYSELLDKA SRIPSPLERM
560 570 580 590 600
VYVAAFAISA YASSYFRAGS KPFNPVLGET YECIRQDKGF QFFAEQVSHH
610 620 630 640 650
PPISACHAES GNFVFWQDVR WKNKFWGKSM EIVPIGTTHV TLPAFGDHFE
660 670 680 690 700
WNKVTSCIHN ILSGQRWIEH YGEIDIKNLN DDSCHCKVNF IKAKYWSTNA
710 720 730 740 750
HEIEGTVFDR SGKAVHRLFG KWHESIYCGG ASSSTCVWRA NPMPKGYEQY
760 770 780 790 800
YGFTQFALEL NEMDPLSRSL LPPTDTRFRP DQRLLEEGNI EEAEVQKQRI
810 820 830 840 850
EKLQRERRRV LEENGVEHQP RFFRKSSDDA WVSNGTYLEL RKDLGFSKLD

HPVLW
Length:855
Mass (Da):96,966
Last modified:July 27, 2011 - v2
Checksum:iD9551D3265278DF8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti789 – 7891N → D in BAB23547 (PubMed:16141072).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004768 mRNA. Translation: BAB23547.1.
AC008160 Genomic DNA. No translation available.
AC124689 Genomic DNA. No translation available.
CCDSiCCDS39489.1.
RefSeqiNP_001157117.1. NM_001163645.1.
NP_082157.2. NM_027881.3.
XP_006506696.1. XM_006506633.2.
UniGeneiMm.44153.

Genome annotation databases

EnsembliENSMUST00000114468; ENSMUSP00000110112; ENSMUSG00000029822.
GeneIDi71720.
KEGGimmu:71720.
UCSCiuc009bwy.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK004768 mRNA. Translation: BAB23547.1.
AC008160 Genomic DNA. No translation available.
AC124689 Genomic DNA. No translation available.
CCDSiCCDS39489.1.
RefSeqiNP_001157117.1. NM_001163645.1.
NP_082157.2. NM_027881.3.
XP_006506696.1. XM_006506633.2.
UniGeneiMm.44153.

3D structure databases

ProteinModelPortaliQ9DBS9.
SMRiQ9DBS9. Positions 47-146, 480-855.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi214879. 1 interaction.
STRINGi10090.ENSMUSP00000110112.

PTM databases

iPTMnetiQ9DBS9.
PhosphoSiteiQ9DBS9.

Proteomic databases

EPDiQ9DBS9.
MaxQBiQ9DBS9.
PaxDbiQ9DBS9.
PRIDEiQ9DBS9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000114468; ENSMUSP00000110112; ENSMUSG00000029822.
GeneIDi71720.
KEGGimmu:71720.
UCSCiuc009bwy.2. mouse.

Organism-specific databases

CTDi26031.
MGIiMGI:1918970. Osbpl3.

Phylogenomic databases

eggNOGiKOG1737. Eukaryota.
ENOG410XP9E. LUCA.
GeneTreeiENSGT00760000119155.
HOGENOMiHOG000231072.
HOVERGENiHBG058934.
InParanoidiQ9DBS9.
OrthoDBiEOG780RKR.
TreeFamiTF320922.

Miscellaneous databases

PROiQ9DBS9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9DBS9.
CleanExiMM_OSBPL3.
ExpressionAtlasiQ9DBS9. baseline and differential.
GenevisibleiQ9DBS9. MM.

Family and domain databases

Gene3Di2.30.29.30. 1 hit.
InterProiIPR000648. Oxysterol-bd.
IPR018494. Oxysterol-bd_CS.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
[Graphical view]
PANTHERiPTHR10972. PTHR10972. 2 hits.
PfamiPF01237. Oxysterol_BP. 1 hit.
[Graphical view]
SMARTiSM00233. PH. 1 hit.
[Graphical view]
SUPFAMiSSF50729. SSF50729. 1 hit.
PROSITEiPS01013. OSBP. 1 hit.
PS50003. PH_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "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/6J.
    Tissue: Lung.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "Subfamily III of mammalian oxysterol-binding protein (OSBP) homologues: the expression and intracellular localization of ORP3, ORP6, and ORP7."
    Lehto M., Tienari J., Lehtonen S., Lehtonen E., Olkkonen V.M.
    Cell Tissue Res. 315:39-57(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
  4. "The phagosomal proteome in interferon-gamma-activated macrophages."
    Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
    Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  5. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33 AND SER-272, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Lung, Pancreas and Spleen.

Entry informationi

Entry nameiOSBL3_MOUSE
AccessioniPrimary (citable) accession number: Q9DBS9
Secondary accession number(s): E9QNI5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 11, 2002
Last sequence update: July 27, 2011
Last modified: July 6, 2016
This is version 108 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. 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.