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Protein

Secretory carrier-associated membrane protein 3

Gene

Scamp3

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

Functioni

Functions in post-Golgi recycling pathways. Acts as a recycling carrier to the cell surface.

GO - Molecular functioni

GO - Biological processi

  • intracellular protein transport Source: MGI
  • response to organic substance Source: MGI
  • response to retinoic acid Source: MGI
Complete GO annotation...

Keywords - Biological processi

Protein transport, Transport

Names & Taxonomyi

Protein namesi
Recommended name:
Secretory carrier-associated membrane protein 3
Short name:
Secretory carrier membrane protein 3
Gene namesi
Name:Scamp3
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 3

Organism-specific databases

MGIiMGI:1346346. Scamp3.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 168168CytoplasmicSequence analysisAdd
BLAST
Transmembranei169 – 18921HelicalSequence analysisAdd
BLAST
Transmembranei200 – 22021HelicalSequence analysisAdd
BLAST
Transmembranei236 – 25621HelicalSequence analysisAdd
BLAST
Transmembranei277 – 29721HelicalSequence analysisAdd
BLAST
Topological domaini298 – 34952CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Membrane

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Secretory carrier-associated membrane protein 3PRO_0000191258Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei32 – 321PhosphoserineBy similarity
Modified residuei41 – 411PhosphotyrosineBy similarity
Modified residuei53 – 531PhosphotyrosineBy similarity
Modified residuei78 – 781PhosphoserineCombined sources
Modified residuei85 – 851PhosphotyrosineCombined sources
Modified residuei87 – 871PhosphoserineBy similarity

Post-translational modificationi

Monoubiquitinated.By similarity

Keywords - PTMi

Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO35609.
MaxQBiO35609.
PaxDbiO35609.
PRIDEiO35609.

PTM databases

iPTMnetiO35609.
PhosphoSiteiO35609.
SwissPalmiO35609.

Expressioni

Gene expression databases

BgeeiO35609.
CleanExiMM_SCAMP3.
ExpressionAtlasiO35609. baseline and differential.
GenevisibleiO35609. MM.

Interactioni

Subunit structurei

Interacts with NEDD4 and NEDD4L and TSG101 (By similarity). Interacts with RNF126.By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

IntActiO35609. 2 interactions.
MINTiMINT-1865874.
STRINGi10090.ENSMUSP00000029684.

Family & Domainsi

Sequence similaritiesi

Belongs to the SCAMP family.Curated

Keywords - Domaini

Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiKOG3088. Eukaryota.
ENOG410XSJN. LUCA.
GeneTreeiENSGT00390000014393.
HOGENOMiHOG000294221.
HOVERGENiHBG071938.
InParanoidiO35609.
KOiK19995.
OrthoDBiEOG7FZ009.
TreeFamiTF313797.

Family and domain databases

InterProiIPR007273. SCAMP.
[Graphical view]
PANTHERiPTHR10687. PTHR10687. 1 hit.
PfamiPF04144. SCAMP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O35609-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQSRDTGNP FPDSGELDNP FQDPAVIQHR PSQQYATLDV YNPFENREPP
60 70 80 90 100
PAYEPPAPAP APLPPPSAPS VQSSRKLSPT EPRNYGSYST QASAAAATAE
110 120 130 140 150
LLKKQEELNR KAEELDRRER ELQHVALGGA GTRQNNWPPL PSFCPVKPCF
160 170 180 190 200
FQDISMEIPQ EFQKTVSTMY YLWMCSTLAL LLNFFACLAR FCVDTGSGSG
210 220 230 240 250
FGLSMLWLLL FTPCSFVCWY RPMYKAFRSD SSFNFFVFFF IFFVQDVFFV
260 270 280 290 300
LQAIGIPGWG FSGWVTALVV VGSKPAVAVL MLLVALLFTG IAVLGIVMLK
310 320 330 340
RIHSLYRQTG ASFQKAQQEF AAGVFSNPAV RTAAANAAAG AAENAFRAP
Length:349
Mass (Da):38,458
Last modified:July 27, 2011 - v3
Checksum:i4963A582F56A560D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti11 – 111F → S in AAB62721 (PubMed:9378760).Curated
Sequence conflicti11 – 111F → S in AAG22800 (PubMed:11050114).Curated
Sequence conflicti48 – 481E → EQ in AAH02021 (PubMed:16141072).Curated
Sequence conflicti61 – 611A → S in AAH02021 (PubMed:16141072).Curated
Sequence conflicti111 – 1111K → T in AAB62721 (PubMed:9378760).Curated
Sequence conflicti284 – 2841V → D in AAB62721 (PubMed:9378760).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005036 mRNA. Translation: AAB62721.1.
AF295403 mRNA. Translation: AAG22800.1.
AK160549 mRNA. Translation: BAE35865.1.
CH466547 Genomic DNA. Translation: EDL15232.1.
BC002021 mRNA. Translation: AAH02021.1.
CCDSiCCDS50959.1.
RefSeqiNP_001296838.1. NM_001309909.1.
NP_001296839.1. NM_001309910.1.
NP_036016.2. NM_011886.3.
UniGeneiMm.257052.

Genome annotation databases

EnsembliENSMUST00000029684; ENSMUSP00000029684; ENSMUSG00000028049.
GeneIDi24045.
KEGGimmu:24045.
UCSCiuc008pxw.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF005036 mRNA. Translation: AAB62721.1.
AF295403 mRNA. Translation: AAG22800.1.
AK160549 mRNA. Translation: BAE35865.1.
CH466547 Genomic DNA. Translation: EDL15232.1.
BC002021 mRNA. Translation: AAH02021.1.
CCDSiCCDS50959.1.
RefSeqiNP_001296838.1. NM_001309909.1.
NP_001296839.1. NM_001309910.1.
NP_036016.2. NM_011886.3.
UniGeneiMm.257052.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO35609. 2 interactions.
MINTiMINT-1865874.
STRINGi10090.ENSMUSP00000029684.

PTM databases

iPTMnetiO35609.
PhosphoSiteiO35609.
SwissPalmiO35609.

Proteomic databases

EPDiO35609.
MaxQBiO35609.
PaxDbiO35609.
PRIDEiO35609.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000029684; ENSMUSP00000029684; ENSMUSG00000028049.
GeneIDi24045.
KEGGimmu:24045.
UCSCiuc008pxw.1. mouse.

Organism-specific databases

CTDi10067.
MGIiMGI:1346346. Scamp3.

Phylogenomic databases

eggNOGiKOG3088. Eukaryota.
ENOG410XSJN. LUCA.
GeneTreeiENSGT00390000014393.
HOGENOMiHOG000294221.
HOVERGENiHBG071938.
InParanoidiO35609.
KOiK19995.
OrthoDBiEOG7FZ009.
TreeFamiTF313797.

Miscellaneous databases

NextBioi303971.
PROiO35609.
SOURCEiSearch...

Gene expression databases

BgeeiO35609.
CleanExiMM_SCAMP3.
ExpressionAtlasiO35609. baseline and differential.
GenevisibleiO35609. MM.

Family and domain databases

InterProiIPR007273. SCAMP.
[Graphical view]
PANTHERiPTHR10687. PTHR10687. 1 hit.
PfamiPF04144. SCAMP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Three mammalian SCAMPs (secretory carrier membrane proteins) are highly related products of distinct genes having similar subcellular distributions."
    Singleton D.R., Wu T.T., Castle J.D.
    J. Cell Sci. 110:2099-2107(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Novel SCAMPs lacking NPF repeats: ubiquitous and synaptic vesicle-specific forms implicate SCAMPs in multiple membrane-trafficking functions."
    Fernandez-Chacon R., Suedhof T.C.
    J. Neurosci. 20:7941-7950(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
  6. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  8. "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of the epidermal growth factor receptor."
    Smith C.J., Berry D.M., McGlade C.J.
    J. Cell Sci. 126:1366-1380(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RNF126.

Entry informationi

Entry nameiSCAM3_MOUSE
AccessioniPrimary (citable) accession number: O35609
Secondary accession number(s): Q3TUV6, Q99M48, Q9ERM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 116 of the entry and version 3 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.