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   27-MAR-2024, entry version 176.
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   INTERACTION WITH SLC9A5.
RX   PubMed=19276089; DOI=10.1074/jbc.m807055200;
RA   Diering G.H., Church J., Numata M.;
RT   "Secretory Carrier Membrane Protein 2 Regulates Cell-surface Targeting of
RT   Brain-enriched Na+/H+ Exchanger NHE5.";
RL   J. Biol. Chem. 284:13892-13903(2009).
RN   [11]
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   [12]
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   [13]
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   [14]
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   [15]
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   [16]
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 (PubMed:15840657,
CC       PubMed:16870614). Interacts with SLC9A5; this interaction regulates
CC       SLC9A5 cell-surface targeting and SLC9A5 activity (PubMed:19276089).
CC       {ECO:0000269|PubMed:15840657, ECO:0000269|PubMed:16870614,
CC       ECO:0000269|PubMed:19276089}.
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; 152.
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; 9606-ENSP00000268099; -.
DR   PeptideAtlas; O15127; -.
DR   ProteomicsDB; 48465; -.
DR   Pumba; O15127; -.
DR   Antibodypedia; 14704; 337 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   AGR; HGNC:10564; -.
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; HSFYRRT; -.
DR   OrthoDB; 169023at2759; -.
DR   PhylomeDB; O15127; -.
DR   TreeFam; TF313797; -.
DR   PathwayCommons; O15127; -.
DR   SignaLink; O15127; -.
DR   BioGRID-ORCS; 10066; 11 hits in 1157 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 202 other cell types or tissues.
DR   ExpressionAtlas; O15127; baseline and differential.
DR   GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR   GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
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:SF7; SECRETORY CARRIER-ASSOCIATED MEMBRANE PROTEIN 2; 1.
DR   PANTHER; PTHR10687; SECRETORY CARRIER-ASSOCIATED MEMBRANE PROTEIN SCAMP; 1.
DR   Pfam; PF04144; SCAMP; 1.
DR   Genevisible; O15127; HS.
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
//