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Gamma-secretase-activating protein (GSAP) (Protein pigeon homolog) [Cleaved into: Gamma-secretase-activating protein 16 kDa C-terminal form (GSAP-16K)]

 GSAP_HUMAN              Reviewed;         854 AA.
A4D1B5; A4D1B6; Q3MJC0; Q8ND73; Q9UMH3; Q9Y4L9;
20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
20-MAY-2008, sequence version 2.
25-OCT-2017, entry version 81.
RecName: Full=Gamma-secretase-activating protein;
Short=GSAP;
AltName: Full=Protein pigeon homolog;
Contains:
RecName: Full=Gamma-secretase-activating protein 16 kDa C-terminal form;
Short=GSAP-16K;
Name=GSAP; Synonyms=PION;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=12853948; DOI=10.1038/nature01782;
Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
Waterston R.H., Wilson R.K.;
"The DNA sequence of human chromosome 7.";
Nature 424:157-164(2003).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ARG-47.
PubMed=12690205; DOI=10.1126/science.1083423;
Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
Kanematsu E., Gentles S., Christopoulos C.C., Choufani S.,
Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W.,
Mural R.J., Adams M.D., Tsui L.-C.;
"Human chromosome 7: DNA sequence and biology.";
Science 300:767-772(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Brain;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 36-854 (ISOFORM 3).
TISSUE=Lymph node;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 587-854.
The European IMAGE consortium;
Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
[7]
FUNCTION, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY,
PROTEOLYTIC PROCESSING, IMATINIB-BINDING, TISSUE SPECIFICITY, AND
INTERACTION WITH APP AND THE GAMMA-SECRETASE COMPLEX.
PubMed=20811458; DOI=10.1038/nature09325;
He G., Luo W., Li P., Remmers C., Netzer W.J., Hendrick J.,
Bettayeb K., Flajolet M., Gorelick F., Wennogle L.P., Greengard P.;
"Gamma-secretase activating protein is a therapeutic target for
Alzheimer's disease.";
Nature 467:95-98(2010).
-!- FUNCTION: Regulator of gamma-secretase activity, which
specifically activates the production of amyloid-beta protein
(amyloid-beta protein 40 and amyloid-beta protein 42), without
affecting the cleavage of other gamma-secretase targets such has
Notch. The gamma-secretase complex is an endoprotease complex that
catalyzes the intramembrane cleavage of integral membrane proteins
such as Notch receptors and APP (amyloid-beta precursor protein).
Specifically promotes the gamma-cleavage of APP CTF-alpha (also
named APP-CTF) by the gamma-secretase complex to generate amyloid-
beta, while it reduces the epsilon-cleavage of APP CTF-alpha,
leading to a low production of AICD.
{ECO:0000269|PubMed:20811458}.
-!- SUBUNIT: Interacts with APP; specifically interacts with the CTF-
alpha product of APP. Interacts with the gamma-secretase complex.
{ECO:0000269|PubMed:20811458}.
-!- INTERACTION:
P05067:APP; NbExp=3; IntAct=EBI-15875313, EBI-77613;
-!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network
{ECO:0000269|PubMed:20811458}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=A4D1B5-1; Sequence=Displayed;
Name=2;
IsoId=A4D1B5-2; Sequence=VSP_033772, VSP_033773, VSP_033774;
Name=3;
IsoId=A4D1B5-3; Sequence=VSP_033773, VSP_033774;
Name=4;
IsoId=A4D1B5-4; Sequence=VSP_033771;
-!- TISSUE SPECIFICITY: Widely expressed.
{ECO:0000269|PubMed:20811458}.
-!- PTM: The protein is first synthesized as a holoprotein form of 98
kDa and rapidly processed into the gamma-secretase-activating
protein 16 kDa C-terminal form, which constitutes the predominant
form. {ECO:0000269|PubMed:20811458}.
-!- MISCELLANEOUS: The gamma-secretase regulator activity is
specifically inhibited by imatinib (also known as STI571 or
Gleevec), an anticancer drug that selectively decreases amyloid-
beta protein production. Imatinib binds PION/GSAP and acts by
preventing PION/GSAP interaction with the gamma-secretase
substrate, CTF-alpha (PubMed:20811458).
{ECO:0000305|PubMed:20811458}.
-!- MISCELLANEOUS: Its role as an activator of amyloid-beta protein
production makes it a promising therapeutic target for the
treatment of Alzheimer disease. {ECO:0000305|PubMed:20811458}.
-!- SIMILARITY: Belongs to the GSAP family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=CAD39023.2; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
-----------------------------------------------------------------------
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EMBL; AC004921; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC073635; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH236949; EAL24199.1; -; Genomic_DNA.
EMBL; CH236949; EAL24200.1; -; Genomic_DNA.
EMBL; CH471091; EAW77039.1; -; Genomic_DNA.
EMBL; BC101499; AAI01500.2; -; mRNA.
EMBL; AL834358; CAD39023.2; ALT_INIT; mRNA.
EMBL; AL079277; CAB45152.1; -; mRNA.
EMBL; AL079297; CAB45193.1; -; mRNA.
CCDS; CCDS34672.2; -. [A4D1B5-1]
RefSeq; NP_059135.2; NM_017439.3. [A4D1B5-1]
UniGene; Hs.186649; -.
ProteinModelPortal; A4D1B5; -.
BioGrid; 119901; 4.
DIP; DIP-59240N; -.
IntAct; A4D1B5; 1.
STRING; 9606.ENSP00000257626; -.
BindingDB; A4D1B5; -.
ChEMBL; CHEMBL3638343; -.
iPTMnet; A4D1B5; -.
PhosphoSitePlus; A4D1B5; -.
BioMuta; GSAP; -.
EPD; A4D1B5; -.
MaxQB; A4D1B5; -.
PaxDb; A4D1B5; -.
PRIDE; A4D1B5; -.
TopDownProteomics; A4D1B5-1; -. [A4D1B5-1]
Ensembl; ENST00000257626; ENSP00000257626; ENSG00000186088. [A4D1B5-1]
GeneID; 54103; -.
KEGG; hsa:54103; -.
UCSC; uc003ugf.3; human. [A4D1B5-1]
CTD; 54103; -.
DisGeNET; 54103; -.
EuPathDB; HostDB:ENSG00000186088.15; -.
GeneCards; GSAP; -.
H-InvDB; HIX0006796; -.
HGNC; HGNC:28042; GSAP.
HPA; HPA023994; -.
MIM; 613552; gene.
neXtProt; NX_A4D1B5; -.
OpenTargets; ENSG00000186088; -.
PharmGKB; PA164724500; -.
eggNOG; ENOG410IG5Q; Eukaryota.
eggNOG; ENOG41129DZ; LUCA.
GeneTree; ENSGT00390000012875; -.
HOVERGEN; HBG095500; -.
InParanoid; A4D1B5; -.
OMA; SATRTCW; -.
OrthoDB; EOG091G0GEP; -.
PhylomeDB; A4D1B5; -.
TreeFam; TF323853; -.
GeneWiki; Protein_pigeon_homolog; -.
GenomeRNAi; 54103; -.
PRO; PR:A4D1B5; -.
Proteomes; UP000005640; Chromosome 7.
Bgee; ENSG00000186088; -.
CleanEx; HS_PION; -.
ExpressionAtlas; A4D1B5; baseline and differential.
Genevisible; A4D1B5; HS.
GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
GO; GO:0001540; F:amyloid-beta binding; IDA:UniProtKB.
GO; GO:1902004; P:positive regulation of amyloid-beta formation; IDA:UniProtKB.
GO; GO:0030162; P:regulation of proteolysis; IDA:UniProtKB.
InterPro; IPR028010; GSAP_C_dom.
InterPro; IPR026172; GSAP_fam.
PANTHER; PTHR13630; PTHR13630; 1.
Pfam; PF14959; GSAP-16; 1.
1: Evidence at protein level;
Alternative splicing; Complete proteome; Golgi apparatus;
Polymorphism; Reference proteome.
CHAIN 1 854 Gamma-secretase-activating protein.
/FTId=PRO_0000335809.
CHAIN 734 854 Gamma-secretase-activating protein 16 kDa
C-terminal form. {ECO:0000255}.
/FTId=PRO_0000403728.
VAR_SEQ 1 606 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_033771.
VAR_SEQ 446 446 Q -> QWRQRADLNTNRVLSDFLK (in isoform 2).
{ECO:0000305}.
/FTId=VSP_033772.
VAR_SEQ 559 559 K -> V (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_033773.
VAR_SEQ 560 854 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_033774.
VARIANT 47 47 H -> R (in dbSNP:rs6949654).
{ECO:0000269|PubMed:12690205}.
/FTId=VAR_043467.
VARIANT 305 305 G -> E (in dbSNP:rs1527263).
/FTId=VAR_043468.
VARIANT 649 649 V -> I (in dbSNP:rs17151692).
/FTId=VAR_043469.
VARIANT 653 653 W -> L (in dbSNP:rs17151689).
/FTId=VAR_043470.
SEQUENCE 854 AA; 97802 MW; D7B4A3A95E2E8C3B CRC64;
MALRLVADFD LGKDVLPWLR AQRAVSEASG AGSGGADVLE NDYESLHVLN VERNGNIIYT
YKDDKGNVVF GLYDCQTRQN ELLYTFEKDL QVFSCSVNSE RTLLAASLVQ STKEGKRNEL
QPGSKCLTLL VEIHPVNNVK VLKAVDSYIW VQFLYPHIES HPLPENHLLL ISEEKYIEQF
RIHVAQEDGN RVVIKNSGHL PRDRIAEDFV WAQWDMSEQR LYYIDLKKSR SILKCIQFYA
DESYNLMFEV PLDISLSNSG FKLVNFGCDY HQYRDKFSKH LTLCVFTNHT GSLCVCYSPK
CASWGQITYS VFYIHKGHSK TFTTSLENVG SHMTKGITFL NLDYYVAVYL PGHFFHLLNV
QHPDLICHNL FLTGNNEMID MLPHCPLQSL SGSLVLDCCS GKLYRALLSQ SSLLQLLQNT
CLDCEKMAAL HCALYCGQGA QFLEAQIIQW ISENVSACHS FDLIQEFIIA SSYWSVYSET
SNMDKLLPHS SVLTWNTEIP GITLVTEDIA LPLMKVLSFK GYWEKLNSNL EYVKYAKPHF
HYNNSVVRRE WHNLISEEKT GKRRSAAYVR NILDNAVKVI SNLEARNLGP RLTPLLQEED
SHQRLLMGLM VSELKDHFLR HLQGVEKKKI EQMVLDYISK LLDLICHIVE TNWRKHNLHS
WVLHFNSRGS AAEFAVFHIM TRILEATNSL FLPLPPGFHT LHTILGVQCL PLHNLLHCID
SGVLLLTETA VIRLMKDLDN TEKNEKLKFS IIVRLPPLIG QKICRLWDHP MSSNIISRNH
VTRLLQNYKK QPRNSMINKS SFSVEFLPLN YFIEILTDIE SSNQALYPFE GHDNVDAEFV
EEAALKHTAM LLGL


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