ID   SCAM5_HUMAN             Reviewed;         235 AA.
AC   Q8TAC9; B3KPJ7; B7Z762; D3DW71; Q8N3M4;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   27-MAR-2024, entry version 154.
DE   RecName: Full=Secretory carrier-associated membrane protein 5;
DE            Short=Secretory carrier membrane protein 5;
DE            Short=hSCAMP5;
GN   Name=SCAMP5;
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] (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION,
RP   TISSUE SPECIFICITY, AND INTERACTION WITH SYT1 AND SYT2.
RX   PubMed=19234194; DOI=10.4049/jimmunol.0802002;
RA   Han C., Chen T., Yang M., Li N., Liu H., Cao X.;
RT   "Human SCAMP5, a novel secretory carrier membrane protein, facilitates
RT   calcium-triggered cytokine secretion by interaction with SNARE machinery.";
RL   J. Immunol. 182:2986-2996(2009).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC   TISSUE=Brain, Synovial cell, Teratocarcinoma, and Thalamus;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Amygdala;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA   Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA   Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
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] (ISOFORM 1).
RC   TISSUE=Brain;
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   POSSIBLE FUNCTION, AND INDUCTION.
RX   PubMed=19240033; DOI=10.1074/jbc.m807620200;
RA   Noh J.-Y., Lee H., Song S., Kim N.S., Im W., Kim M., Seo H.-M.,
RA   Chung C.-W., Chang J.-W., Ferrante R.J., Yoo Y.-J., Ryu H., Jung Y.-K.;
RT   "SCAMP5 links endoplasmic reticulum stress to the accumulation of expanded
RT   polyglutamine protein aggregates via endocytosis inhibition.";
RL   J. Biol. Chem. 284:11318-11325(2009).
CC   -!- FUNCTION: Required for the calcium-dependent exocytosis of signal
CC       sequence-containing cytokines such as CCL5. Probably acts in
CC       cooperation with the SNARE machinery. May play a role in accumulation
CC       of expanded polyglutamine (polyQ) protein huntingtin (HTT) in case of
CC       endoplasmic reticulum stress by inhibiting the endocytosis pathway.
CC       {ECO:0000269|PubMed:19234194}.
CC   -!- SUBUNIT: Interacts (via C-terminal part) with SYT1 and SYT2;
CC       interaction with synaptotagmins making a link with the SNARE molecules.
CC       Interacts with SLC9A7. {ECO:0000269|PubMed:15840657,
CC       ECO:0000269|PubMed:19234194}.
CC   -!- INTERACTION:
CC       Q8TAC9; Q13520: AQP6; NbExp=3; IntAct=EBI-2695784, EBI-13059134;
CC       Q8TAC9; P53365: ARFIP2; NbExp=3; IntAct=EBI-2695784, EBI-638194;
CC       Q8TAC9; Q9HA82: CERS4; NbExp=3; IntAct=EBI-2695784, EBI-2622997;
CC       Q8TAC9; Q969F0: FATE1; NbExp=3; IntAct=EBI-2695784, EBI-743099;
CC       Q8TAC9; P39905-3: GDNF; NbExp=3; IntAct=EBI-2695784, EBI-12702062;
CC       Q8TAC9; Q7Z5P4: HSD17B13; NbExp=3; IntAct=EBI-2695784, EBI-18053395;
CC       Q8TAC9; P15941-11: MUC1; NbExp=3; IntAct=EBI-2695784, EBI-17263240;
CC       Q8TAC9; P57054: PIGP; NbExp=3; IntAct=EBI-2695784, EBI-17630288;
CC       Q8TAC9; Q9UKF7-2: PITPNC1; NbExp=3; IntAct=EBI-2695784, EBI-14223623;
CC       Q8TAC9; O95470: SGPL1; NbExp=3; IntAct=EBI-2695784, EBI-1046170;
CC       Q8TAC9; Q99961: SH3GL1; NbExp=3; IntAct=EBI-2695784, EBI-697911;
CC       Q8TAC9; Q3SXP7: SHISAL1; NbExp=3; IntAct=EBI-2695784, EBI-18037857;
CC       Q8TAC9; Q3KNW5: SLC10A6; NbExp=3; IntAct=EBI-2695784, EBI-18159983;
CC       Q8TAC9; Q9NPL8: TIMMDC1; NbExp=3; IntAct=EBI-2695784, EBI-6268651;
CC       Q8TAC9; Q96MV1: TLCD4; NbExp=3; IntAct=EBI-2695784, EBI-12947623;
CC       Q8TAC9; Q9NUH8: TMEM14B; NbExp=3; IntAct=EBI-2695784, EBI-8638294;
CC       Q8TAC9; Q9Y320: TMX2; NbExp=3; IntAct=EBI-2695784, EBI-6447886;
CC       Q8TAC9; P49638: TTPA; NbExp=3; IntAct=EBI-2695784, EBI-10210710;
CC       Q8TAC9; P46096: Syt1; Xeno; NbExp=2; IntAct=EBI-2695784, EBI-445340;
CC       Q8TAC9; P46097: Syt2; Xeno; NbExp=2; IntAct=EBI-2695784, EBI-457969;
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. Golgi
CC       apparatus membrane; Multi-pass membrane protein. Golgi apparatus,
CC       trans-Golgi network membrane; Multi-pass membrane protein. Recycling
CC       endosome membrane; Multi-pass membrane protein. Cytoplasmic vesicle,
CC       secretory vesicle, synaptic vesicle membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}. Note=Mainly localizes in Golgi
CC       apparatus membrane. Upon calcium-triggered exocytosis, it translocates
CC       to the cell membrane. Highly enriched in synaptic vesicles (By
CC       similarity). {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=Q8TAC9-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8TAC9-2; Sequence=VSP_010206;
CC       Name=3;
CC         IsoId=Q8TAC9-3; Sequence=VSP_036934;
CC   -!- TISSUE SPECIFICITY: Expressed both by neuronal and non-neuronal
CC       tissues. Expressed in brain, stomach, thyroid, spinal cord, lymph node,
CC       trachea, adrenal gland, bone marrow and in the different parts of
CC       brain. In thyroid tissues, it is expressed by the follicular epithelial
CC       cells. In the adrenal gland tissues it is detected in the zona
CC       fasciculata of the cortex region (at protein level).
CC       {ECO:0000269|PubMed:19234194}.
CC   -!- INDUCTION: By endoplasmic reticulum stress.
CC       {ECO:0000269|PubMed:19240033}.
CC   -!- SIMILARITY: Belongs to the SCAMP family. SCAMP5 subfamily.
CC       {ECO:0000305}.
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DR   EMBL; AF495715; AAM18052.1; -; mRNA.
DR   EMBL; AK056438; BAG51709.1; -; mRNA.
DR   EMBL; AK126940; BAG54404.1; -; mRNA.
DR   EMBL; AK127480; BAG54511.1; -; mRNA.
DR   EMBL; AK301505; BAH13498.1; -; mRNA.
DR   EMBL; AL834226; CAD38904.1; -; mRNA.
DR   EMBL; CH471136; EAW99277.1; -; Genomic_DNA.
DR   EMBL; CH471136; EAW99278.1; -; Genomic_DNA.
DR   EMBL; CH471136; EAW99280.1; -; Genomic_DNA.
DR   EMBL; CH471136; EAW99283.1; -; Genomic_DNA.
DR   EMBL; BC024700; AAH24700.1; -; mRNA.
DR   CCDS; CCDS45306.1; -. [Q8TAC9-1]
DR   RefSeq; NP_001171582.1; NM_001178111.1. [Q8TAC9-1]
DR   RefSeq; NP_001171583.1; NM_001178112.1. [Q8TAC9-1]
DR   RefSeq; NP_620417.1; NM_138967.3. [Q8TAC9-1]
DR   RefSeq; XP_006720484.1; XM_006720421.1. [Q8TAC9-1]
DR   RefSeq; XP_006720485.1; XM_006720422.3.
DR   RefSeq; XP_016877478.1; XM_017021989.1.
DR   AlphaFoldDB; Q8TAC9; -.
DR   SMR; Q8TAC9; -.
DR   BioGRID; 128182; 23.
DR   IntAct; Q8TAC9; 32.
DR   MINT; Q8TAC9; -.
DR   STRING; 9606.ENSP00000355387; -.
DR   TCDB; 8.A.103.1.5; the secretory carrier-associated membrane protein (scamp) family.
DR   iPTMnet; Q8TAC9; -.
DR   PhosphoSitePlus; Q8TAC9; -.
DR   SwissPalm; Q8TAC9; -.
DR   BioMuta; SCAMP5; -.
DR   DMDM; 47117253; -.
DR   EPD; Q8TAC9; -.
DR   MassIVE; Q8TAC9; -.
DR   MaxQB; Q8TAC9; -.
DR   PaxDb; 9606-ENSP00000355387; -.
DR   PeptideAtlas; Q8TAC9; -.
DR   ProteomicsDB; 73856; -. [Q8TAC9-1]
DR   ProteomicsDB; 73857; -. [Q8TAC9-2]
DR   ProteomicsDB; 73858; -. [Q8TAC9-3]
DR   Antibodypedia; 27182; 76 antibodies from 16 providers.
DR   DNASU; 192683; -.
DR   Ensembl; ENST00000361900.10; ENSP00000355387.6; ENSG00000198794.12. [Q8TAC9-1]
DR   Ensembl; ENST00000425597.8; ENSP00000406547.3; ENSG00000198794.12. [Q8TAC9-1]
DR   Ensembl; ENST00000562212.5; ENSP00000455313.1; ENSG00000198794.12. [Q8TAC9-2]
DR   GeneID; 192683; -.
DR   KEGG; hsa:192683; -.
DR   MANE-Select; ENST00000425597.8; ENSP00000406547.3; NM_138967.4; NP_620417.1.
DR   UCSC; uc002azk.3; human. [Q8TAC9-1]
DR   AGR; HGNC:30386; -.
DR   CTD; 192683; -.
DR   DisGeNET; 192683; -.
DR   GeneCards; SCAMP5; -.
DR   HGNC; HGNC:30386; SCAMP5.
DR   HPA; ENSG00000198794; Tissue enhanced (brain, retina).
DR   MIM; 613766; gene.
DR   neXtProt; NX_Q8TAC9; -.
DR   OpenTargets; ENSG00000198794; -.
DR   PharmGKB; PA134962580; -.
DR   VEuPathDB; HostDB:ENSG00000198794; -.
DR   eggNOG; KOG3088; Eukaryota.
DR   GeneTree; ENSGT00940000157577; -.
DR   InParanoid; Q8TAC9; -.
DR   OMA; MFDNTAK; -.
DR   OrthoDB; 169023at2759; -.
DR   PhylomeDB; Q8TAC9; -.
DR   TreeFam; TF313797; -.
DR   PathwayCommons; Q8TAC9; -.
DR   SignaLink; Q8TAC9; -.
DR   BioGRID-ORCS; 192683; 18 hits in 1148 CRISPR screens.
DR   ChiTaRS; SCAMP5; human.
DR   GeneWiki; SCAMP5; -.
DR   GenomeRNAi; 192683; -.
DR   Pharos; Q8TAC9; Tbio.
DR   PRO; PR:Q8TAC9; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q8TAC9; Protein.
DR   Bgee; ENSG00000198794; Expressed in right hemisphere of cerebellum and 139 other cell types or tissues.
DR   ExpressionAtlas; Q8TAC9; baseline and differential.
DR   GO; GO:0000139; C:Golgi membrane; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0055038; C:recycling endosome membrane; IDA:UniProtKB.
DR   GO; GO:0030672; C:synaptic vesicle membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0032588; C:trans-Golgi network membrane; IDA:UniProtKB.
DR   GO; GO:0044877; F:protein-containing complex binding; IDA:UniProtKB.
DR   GO; GO:0006887; P:exocytosis; IEA:UniProtKB-KW.
DR   GO; GO:0045806; P:negative regulation of endocytosis; IDA:UniProtKB.
DR   GO; GO:0045956; P:positive regulation of calcium ion-dependent exocytosis; IDA:UniProtKB.
DR   GO; GO:0001819; P:positive regulation of cytokine production; IDA:UniProtKB.
DR   GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IDA:UniProtKB.
DR   InterPro; IPR007273; SCAMP.
DR   PANTHER; PTHR10687:SF5; SECRETORY CARRIER-ASSOCIATED MEMBRANE PROTEIN 5; 1.
DR   PANTHER; PTHR10687; SECRETORY CARRIER-ASSOCIATED MEMBRANE PROTEIN SCAMP; 1.
DR   Pfam; PF04144; SCAMP; 1.
DR   Genevisible; Q8TAC9; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Cytoplasmic vesicle; Endosome;
KW   Exocytosis; Golgi apparatus; Membrane; Protein transport;
KW   Reference proteome; Synapse; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..235
FT                   /note="Secretory carrier-associated membrane protein 5"
FT                   /id="PRO_0000191262"
FT   TOPO_DOM        1..39
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        61..67
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        68..88
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        89..102
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        103..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        126..148
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        170..235
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..98
FT                   /note="MAEKVNNFPPLPKFIPLKPCFYQDFEADIPPQHVSMTKRLYYLWMLNSVTLA
FT                   VNLVGCLAWLIGGGGATNFGLAFLWLILFTPCSYVCWFRPIYKAFK -> MFLPRLRGR
FT                   YSSPACQHDQAPLLPLDV (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_036934"
FT   VAR_SEQ         132
FT                   /note="C -> CPTLASSCS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:17974005"
FT                   /id="VSP_010206"
SQ   SEQUENCE   235 AA;  26104 MW;  D3CFF3C9EF2FC6FF CRC64;
     MAEKVNNFPP LPKFIPLKPC FYQDFEADIP PQHVSMTKRL YYLWMLNSVT LAVNLVGCLA
     WLIGGGGATN FGLAFLWLIL FTPCSYVCWF RPIYKAFKTD SSFSFMAFFF TFMAQLVISI
     IQAVGIPGWG VCGWIATISF FGTNIGSAVV MLIPTVMFTV MAVFSFIALS MVHKFYRGSG
     GSFSKAQEEW TTGAWKNPHV QQAAQNAAMG AAQGAMNQPQ TQYSATPNYT YSNEM
//