SCAM3_MOUSE
ID SCAM3_MOUSE Reviewed; 349 AA.
AC O35609; Q3TUV6; Q99M48; Q9ERM9;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Secretory carrier-associated membrane protein 3;
DE Short=Secretory carrier membrane protein 3;
GN Name=Scamp3;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9378760; DOI=10.1242/jcs.110.17.2099;
RA Singleton D.R., Wu T.T., Castle J.D.;
RT "Three mammalian SCAMPs (secretory carrier membrane proteins) are highly
RT related products of distinct genes having similar subcellular
RT distributions.";
RL J. Cell Sci. 110:2099-2107(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=11050114; DOI=10.1523/jneurosci.20-21-07941.2000;
RA Fernandez-Chacon R., Suedhof T.C.;
RT "Novel SCAMPs lacking NPF repeats: ubiquitous and synaptic vesicle-specific
RT forms implicate SCAMPs in multiple membrane-trafficking functions.";
RL J. Neurosci. 20:7941-7950(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-78, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-85, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP INTERACTION WITH RNF126.
RX PubMed=23418353; DOI=10.1242/jcs.116129;
RA Smith C.J., Berry D.M., McGlade C.J.;
RT "The E3 ubiquitin ligases RNF126 and Rabring7 regulate endosomal sorting of
RT the epidermal growth factor receptor.";
RL J. Cell Sci. 126:1366-1380(2013).
CC -!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
CC recycling carrier to the cell surface.
CC -!- SUBUNIT: Interacts with NEDD4 and NEDD4L and TSG101 (By similarity).
CC Interacts with RNF126. {ECO:0000250|UniProtKB:O14828,
CC ECO:0000269|PubMed:23418353}.
CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein.
CC -!- PTM: Monoubiquitinated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SCAMP family. {ECO:0000305}.
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DR EMBL; AF005036; AAB62721.1; -; mRNA.
DR EMBL; AF295403; AAG22800.1; -; mRNA.
DR EMBL; AK160549; BAE35865.1; -; mRNA.
DR EMBL; CH466547; EDL15232.1; -; Genomic_DNA.
DR EMBL; BC002021; AAH02021.1; -; mRNA.
DR CCDS; CCDS50959.1; -.
DR RefSeq; NP_001296838.1; NM_001309909.1.
DR RefSeq; NP_001296839.1; NM_001309910.1.
DR RefSeq; NP_036016.2; NM_011886.3.
DR AlphaFoldDB; O35609; -.
DR SMR; O35609; -.
DR BioGRID; 204860; 6.
DR IntAct; O35609; 1.
DR STRING; 10090.ENSMUSP00000029684; -.
DR iPTMnet; O35609; -.
DR PhosphoSitePlus; O35609; -.
DR SwissPalm; O35609; -.
DR EPD; O35609; -.
DR jPOST; O35609; -.
DR MaxQB; O35609; -.
DR PaxDb; O35609; -.
DR PRIDE; O35609; -.
DR ProteomicsDB; 256710; -.
DR Antibodypedia; 20415; 145 antibodies from 25 providers.
DR DNASU; 24045; -.
DR Ensembl; ENSMUST00000029684; ENSMUSP00000029684; ENSMUSG00000028049.
DR GeneID; 24045; -.
DR KEGG; mmu:24045; -.
DR UCSC; uc008pxw.1; mouse.
DR CTD; 10067; -.
DR MGI; MGI:1346346; Scamp3.
DR VEuPathDB; HostDB:ENSMUSG00000028049; -.
DR eggNOG; KOG3088; Eukaryota.
DR GeneTree; ENSGT00940000160917; -.
DR HOGENOM; CLU_066546_0_0_1; -.
DR InParanoid; O35609; -.
DR OMA; RPSTHYA; -.
DR OrthoDB; 995882at2759; -.
DR TreeFam; TF313797; -.
DR BioGRID-ORCS; 24045; 5 hits in 73 CRISPR screens.
DR PRO; PR:O35609; -.
DR Proteomes; UP000000589; Chromosome 3.
DR RNAct; O35609; protein.
DR Bgee; ENSMUSG00000028049; Expressed in yolk sac and 264 other tissues.
DR ExpressionAtlas; O35609; baseline and differential.
DR Genevisible; O35609; MM.
DR GO; GO:0000139; C:Golgi membrane; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0055038; C:recycling endosome membrane; IBA:GO_Central.
DR GO; GO:0032588; C:trans-Golgi network membrane; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:MGI.
DR GO; GO:0006886; P:intracellular protein transport; TAS:MGI.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0010033; P:response to organic substance; IDA:MGI.
DR GO; GO:0032526; P:response to retinoic acid; IDA:MGI.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 1: Evidence at protein level;
KW Isopeptide bond; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport;
KW Ubl conjugation.
FT CHAIN 1..349
FT /note="Secretory carrier-associated membrane protein 3"
FT /id="PRO_0000191258"
FT TOPO_DOM 1..168
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 236..256
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 26..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 48..69
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14828"
FT MOD_RES 37
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O14828"
FT MOD_RES 41
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O14828"
FT MOD_RES 53
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:O14828"
FT MOD_RES 74
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14828"
FT MOD_RES 78
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 85
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O14828"
FT CROSSLNK 315
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1)"
FT /evidence="ECO:0000250|UniProtKB:O14828"
FT CONFLICT 11
FT /note="F -> S (in Ref. 1; AAB62721 and 2; AAG22800)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="E -> EQ (in Ref. 3; AAH02021)"
FT /evidence="ECO:0000305"
FT CONFLICT 61
FT /note="A -> S (in Ref. 3; AAH02021)"
FT /evidence="ECO:0000305"
FT CONFLICT 111
FT /note="K -> T (in Ref. 1; AAB62721)"
FT /evidence="ECO:0000305"
FT CONFLICT 284
FT /note="V -> D (in Ref. 1; AAB62721)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 349 AA; 38458 MW; 4963A582F56A560D CRC64;
MAQSRDTGNP FPDSGELDNP FQDPAVIQHR PSQQYATLDV YNPFENREPP PAYEPPAPAP
APLPPPSAPS VQSSRKLSPT EPRNYGSYST QASAAAATAE LLKKQEELNR KAEELDRRER
ELQHVALGGA GTRQNNWPPL PSFCPVKPCF FQDISMEIPQ EFQKTVSTMY YLWMCSTLAL
LLNFFACLAR FCVDTGSGSG FGLSMLWLLL FTPCSFVCWY RPMYKAFRSD SSFNFFVFFF
IFFVQDVFFV LQAIGIPGWG FSGWVTALVV VGSKPAVAVL MLLVALLFTG IAVLGIVMLK
RIHSLYRQTG ASFQKAQQEF AAGVFSNPAV RTAAANAAAG AAENAFRAP
