SCAM2_HUMAN
ID SCAM2_HUMAN Reviewed; 329 AA.
AC O15127; B2RDF0; Q9BQE8;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2001, sequence version 2.
DT 03-AUG-2022, entry version 167.
DE RecName: Full=Secretory carrier-associated membrane protein 2;
DE Short=Secretory carrier membrane protein 2;
GN Name=SCAMP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
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 SEQUENCE REVISION.
RA Singleton D.R., Wu T.T., Castle J.D.;
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Skin;
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 SUBCELLULAR LOCATION, AND INTERACTION WITH SLC9A7.
RX PubMed=15840657; DOI=10.1242/jcs.02315;
RA Lin P.J., Williams W.P., Luu Y., Molday R.S., Orlowski J., Numata M.;
RT "Secretory carrier membrane proteins interact and regulate trafficking of
RT the organellar (Na+,K+)/H+ exchanger NHE7.";
RL J. Cell Sci. 118:1885-1897(2005).
RN [7]
RP INTERACTION WITH SLC6A4.
RX PubMed=16870614; DOI=10.1074/jbc.m602848200;
RA Mueller H.K., Wiborg O., Haase J.;
RT "Subcellular redistribution of the serotonin transporter by secretory
RT carrier membrane protein 2.";
RL J. Biol. Chem. 281:28901-28909(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Platelet;
RX PubMed=18088087; DOI=10.1021/pr0704130;
RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT "Phosphoproteome of resting human platelets.";
RL J. Proteome Res. 7:526-534(2008).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-320, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-319 AND SER-320, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Functions in post-Golgi recycling pathways. Acts as a
CC recycling carrier to the cell surface.
CC -!- SUBUNIT: Interacts with SLC6A4 and SLC9A7.
CC {ECO:0000269|PubMed:15840657, ECO:0000269|PubMed:16870614}.
CC -!- INTERACTION:
CC O15127; P21333-2: FLNA; NbExp=3; IntAct=EBI-712703, EBI-9641086;
CC O15127; Q8IVJ1: SLC41A1; NbExp=3; IntAct=EBI-712703, EBI-12266234;
CC O15127; Q96T83: SLC9A7; NbExp=9; IntAct=EBI-712703, EBI-4319546;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane
CC {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15840657}. Recycling endosome membrane
CC {ECO:0000269|PubMed:15840657}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15840657}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the SCAMP family. {ECO:0000305}.
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DR EMBL; AF005038; AAB62723.2; -; mRNA.
DR EMBL; AK315516; BAG37897.1; -; mRNA.
DR EMBL; CH471136; EAW99300.1; -; Genomic_DNA.
DR EMBL; BC001376; AAH01376.1; -; mRNA.
DR EMBL; BC004385; AAH04385.1; -; mRNA.
DR CCDS; CCDS10271.1; -.
DR RefSeq; NP_005688.2; NM_005697.4.
DR AlphaFoldDB; O15127; -.
DR BioGRID; 115377; 129.
DR CORUM; O15127; -.
DR IntAct; O15127; 21.
DR MINT; O15127; -.
DR STRING; 9606.ENSP00000268099; -.
DR TCDB; 8.A.103.1.2; the secretory carrier-associated membrane protein (scamp) family.
DR GlyGen; O15127; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O15127; -.
DR PhosphoSitePlus; O15127; -.
DR SwissPalm; O15127; -.
DR BioMuta; SCAMP2; -.
DR EPD; O15127; -.
DR jPOST; O15127; -.
DR MassIVE; O15127; -.
DR MaxQB; O15127; -.
DR PaxDb; O15127; -.
DR PeptideAtlas; O15127; -.
DR PRIDE; O15127; -.
DR ProteomicsDB; 48465; -.
DR Antibodypedia; 14704; 294 antibodies from 26 providers.
DR DNASU; 10066; -.
DR Ensembl; ENST00000268099.13; ENSP00000268099.9; ENSG00000140497.16.
DR GeneID; 10066; -.
DR KEGG; hsa:10066; -.
DR MANE-Select; ENST00000268099.13; ENSP00000268099.9; NM_005697.5; NP_005688.2.
DR UCSC; uc002azb.2; human.
DR CTD; 10066; -.
DR DisGeNET; 10066; -.
DR GeneCards; SCAMP2; -.
DR HGNC; HGNC:10564; SCAMP2.
DR HPA; ENSG00000140497; Low tissue specificity.
DR MIM; 606912; gene.
DR neXtProt; NX_O15127; -.
DR OpenTargets; ENSG00000140497; -.
DR PharmGKB; PA34977; -.
DR VEuPathDB; HostDB:ENSG00000140497; -.
DR eggNOG; KOG3088; Eukaryota.
DR GeneTree; ENSGT00940000156476; -.
DR HOGENOM; CLU_066546_0_0_1; -.
DR InParanoid; O15127; -.
DR OMA; EPVDQYN; -.
DR PhylomeDB; O15127; -.
DR TreeFam; TF313797; -.
DR PathwayCommons; O15127; -.
DR SignaLink; O15127; -.
DR BioGRID-ORCS; 10066; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; SCAMP2; human.
DR GeneWiki; SCAMP2; -.
DR GenomeRNAi; 10066; -.
DR Pharos; O15127; Tbio.
DR PRO; PR:O15127; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; O15127; protein.
DR Bgee; ENSG00000140497; Expressed in rectum and 200 other tissues.
DR ExpressionAtlas; O15127; baseline and differential.
DR Genevisible; O15127; HS.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; TAS:ProtInc.
DR GO; GO:0015031; P:protein transport; IDA:UniProtKB.
DR InterPro; IPR007273; SCAMP.
DR PANTHER; PTHR10687; PTHR10687; 1.
DR Pfam; PF04144; SCAMP; 1.
PE 1: Evidence at protein level;
KW Endosome; Golgi apparatus; Membrane; Phosphoprotein; Protein transport;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..329
FT /note="Secretory carrier-associated membrane protein 2"
FT /id="PRO_0000191254"
FT TOPO_DOM 1..153
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 154..174
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 175..181
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 182..202
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 203..218
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 240..262
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 263..283
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 284..329
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 51..72
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 203..218
FT /note="Interaction with SLC9A7"
FT /evidence="ECO:0000269|PubMed:15840657"
FT MOD_RES 319
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
SQ SEQUENCE 329 AA; 36649 MW; 046ACB926FD951DD CRC64;
MSAFDTNPFA DPVDVNPFQD PSVTQLTNAP QGGLAEFNPF SETNAATTVP VTQLPGSSQP
AVLQPSVEPT QPTPQAVVSA AQAGLLRQQE ELDRKAAELE RKERELQNTV ANLHVRQNNW
PPLPSWCPVK PCFYQDFSTE IPADYQRICK MLYYLWMLHS VTLFLNLLAC LAWFSGNSSK
GVDFGLSILW FLIFTPCAFL CWYRPIYKAF RSDNSFSFFV FFFVFFCQIG IYIIQLVGIP
GLGDSGWIAA LSTLDNHSLA ISVIMMVVAG FFTLCAVLSV FLLQRVHSLY RRTGASFQQA
QEEFSQGIFS SRTFHRAASS AAQGAFQGN
