GASP1_HUMAN
ID GASP1_HUMAN Reviewed; 1395 AA.
AC Q5JY77; O43168; Q96LA1;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 3.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=G-protein coupled receptor-associated sorting protein 1;
DE Short=GASP-1;
GN Name=GPRASP1; Synonyms=GASP, KIAA0443;
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 [LARGE SCALE MRNA], AND VARIANT GLY-315.
RC TISSUE=Brain;
RX PubMed=9455477; DOI=10.1093/dnares/4.5.307;
RA Ishikawa K., Nagase T., Nakajima D., Seki N., Ohira M., Miyajima N.,
RA Tanaka A., Kotani H., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. VIII. 78
RT new cDNA clones from brain which code for large proteins in vitro.";
RL DNA Res. 4:307-313(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1362-1395.
RC TISSUE=Heart;
RA Patzak D.;
RT "Completely sequenced partial cDNA clone from a human heart library.";
RL Submitted (JUN-2001) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH OPRD1; ADRB2 AND DRD4, DOMAIN OPRD1-BINDING, AND
RP TISSUE SPECIFICITY.
RX PubMed=12142540; DOI=10.1126/science.1073308;
RA Whistler J.L., Enquist J., Marley A., Fong J., Gladher F., Tsuruda P.,
RA Murray S.R., Von Zastrow M.;
RT "Modulation of postendocytic sorting of G protein-coupled receptors.";
RL Science 297:615-620(2002).
RN [6]
RP FUNCTION, INTERACTION WITH G PROTEIN-COUPLED RECEPTORS, AND SUBCELLULAR
RP LOCATION.
RX PubMed=15452121; DOI=10.1074/jbc.m406169200;
RA Heydorn A., Soendergaard B.P., Ersboell B., Holst B., Nielsen F.C.,
RA Haft C.R., Whistler J., Schwartz T.W.;
RT "A library of 7TM receptor C-terminal tails. Interactions with the proposed
RT post-endocytic sorting proteins ERM-binding phosphoprotein 50 (EBP50), N-
RT ethylmaleimide-sensitive factor (NSF), sorting nexin 1 (SNX1), and G
RT protein-coupled receptor-associated sorting protein (GASP).";
RL J. Biol. Chem. 279:54291-54303(2004).
RN [7]
RP TISSUE SPECIFICITY, AND INTERACTION WITH OPRD1.
RX PubMed=15086532; DOI=10.1111/j.1471-4159.2004.02411.x;
RA Simonin F., Karcher P., Boeuf J.J.-M., Matifas A., Kieffer B.L.;
RT "Identification of a novel family of G protein-coupled receptor associated
RT sorting proteins.";
RL J. Neurochem. 89:766-775(2004).
RN [8]
RP FUNCTION, AND INTERACTION WITH BECN2.
RX PubMed=23954414; DOI=10.1016/j.cell.2013.07.035;
RA He C., Wei Y., Sun K., Li B., Dong X., Zou Z., Liu Y., Kinch L.N., Khan S.,
RA Sinha S., Xavier R.J., Grishin N.V., Xiao G., Eskelinen E.L., Scherer P.E.,
RA Whistler J.L., Levine B.;
RT "Beclin 2 functions in autophagy, degradation of G protein-coupled
RT receptors, and metabolism.";
RL Cell 154:1085-1099(2013).
CC -!- FUNCTION: Modulates lysosomal sorting and functional down-regulation of
CC a variety of G-protein coupled receptors. Targets receptors for
CC degradation in lysosomes via its interaction with BECN2.
CC {ECO:0000269|PubMed:12142540, ECO:0000269|PubMed:15452121,
CC ECO:0000269|PubMed:23954414}.
CC -!- SUBUNIT: Interacts with cytoplasmic tails of a variety of G-protein
CC coupled receptors such as D2 dopamine receptor/DRD2 (By similarity),
CC delta opioid receptor/OPRD1, beta-2 adrenergic receptor/ADRB2 and D4
CC dopamine receptor/DRD4. Interacts with PER1. Interacts with BECN2; the
CC interaction is direct. {ECO:0000250, ECO:0000269|PubMed:12142540,
CC ECO:0000269|PubMed:15086532, ECO:0000269|PubMed:15452121,
CC ECO:0000269|PubMed:23954414}.
CC -!- INTERACTION:
CC Q5JY77; A8MW95: BECN2; NbExp=4; IntAct=EBI-2514717, EBI-8839517;
CC Q5JY77; P41143: OPRD1; NbExp=2; IntAct=EBI-2514717, EBI-2624456;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15452121}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain, with lower expression in
CC medulla, spinal cord and substantia nigra.
CC {ECO:0000269|PubMed:12142540, ECO:0000269|PubMed:15086532}.
CC -!- SIMILARITY: Belongs to the GPRASP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA23715.3; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB007903; BAA23715.3; ALT_INIT; mRNA.
DR EMBL; AL035427; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC114552; AAI14553.1; -; mRNA.
DR EMBL; AY044233; AAK95578.1; -; mRNA.
DR CCDS; CCDS35352.1; -.
DR PIR; T00068; T00068.
DR RefSeq; NP_001092880.1; NM_001099410.1.
DR RefSeq; NP_001092881.1; NM_001099411.1.
DR RefSeq; NP_001171656.1; NM_001184727.1.
DR RefSeq; NP_055525.3; NM_014710.4.
DR RefSeq; XP_016885470.1; XM_017029981.1.
DR RefSeq; XP_016885471.1; XM_017029982.1.
DR AlphaFoldDB; Q5JY77; -.
DR SMR; Q5JY77; -.
DR BioGRID; 115086; 34.
DR IntAct; Q5JY77; 26.
DR STRING; 9606.ENSP00000445683; -.
DR iPTMnet; Q5JY77; -.
DR PhosphoSitePlus; Q5JY77; -.
DR BioMuta; GPRASP1; -.
DR DMDM; 126302546; -.
DR EPD; Q5JY77; -.
DR jPOST; Q5JY77; -.
DR MassIVE; Q5JY77; -.
DR MaxQB; Q5JY77; -.
DR PaxDb; Q5JY77; -.
DR PeptideAtlas; Q5JY77; -.
DR PRIDE; Q5JY77; -.
DR ProteomicsDB; 63484; -.
DR Antibodypedia; 383; 135 antibodies from 28 providers.
DR DNASU; 9737; -.
DR Ensembl; ENST00000361600.9; ENSP00000355146.4; ENSG00000198932.13.
DR Ensembl; ENST00000415986.5; ENSP00000393691.1; ENSG00000198932.13.
DR Ensembl; ENST00000444152.5; ENSP00000409420.1; ENSG00000198932.13.
DR Ensembl; ENST00000537097.2; ENSP00000445683.1; ENSG00000198932.13.
DR Ensembl; ENST00000652542.1; ENSP00000498934.1; ENSG00000198932.13.
DR GeneID; 9737; -.
DR KEGG; hsa:9737; -.
DR MANE-Select; ENST00000537097.2; ENSP00000445683.1; NM_001184727.2; NP_001171656.1.
DR UCSC; uc004eji.5; human.
DR CTD; 9737; -.
DR DisGeNET; 9737; -.
DR GeneCards; GPRASP1; -.
DR HGNC; HGNC:24834; GPRASP1.
DR HPA; ENSG00000198932; Low tissue specificity.
DR MIM; 300417; gene.
DR neXtProt; NX_Q5JY77; -.
DR OpenTargets; ENSG00000198932; -.
DR PharmGKB; PA134970616; -.
DR VEuPathDB; HostDB:ENSG00000198932; -.
DR eggNOG; ENOG502S6CE; Eukaryota.
DR GeneTree; ENSGT00940000163396; -.
DR HOGENOM; CLU_008490_0_0_1; -.
DR InParanoid; Q5JY77; -.
DR OMA; WFWATEE; -.
DR OrthoDB; 860703at2759; -.
DR PhylomeDB; Q5JY77; -.
DR TreeFam; TF335652; -.
DR PathwayCommons; Q5JY77; -.
DR SignaLink; Q5JY77; -.
DR BioGRID-ORCS; 9737; 14 hits in 699 CRISPR screens.
DR GeneWiki; GPRASP1_(gene); -.
DR GenomeRNAi; 9737; -.
DR Pharos; Q5JY77; Tbio.
DR PRO; PR:Q5JY77; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q5JY77; protein.
DR Bgee; ENSG00000198932; Expressed in middle temporal gyrus and 190 other tissues.
DR Genevisible; Q5JY77; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0008333; P:endosome to lysosome transport; IMP:UniProtKB.
DR GO; GO:1990172; P:G protein-coupled receptor catabolic process; IMP:UniProtKB.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR006911; ARM-rpt_dom.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR043374; BHLHb9/GASP-1/GASP-2.
DR PANTHER; PTHR46414; PTHR46414; 1.
DR Pfam; PF04826; Arm_2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1395
FT /note="G-protein coupled receptor-associated sorting
FT protein 1"
FT /id="PRO_0000239050"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 45..83
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 269..288
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 899..1395
FT /note="OPRD1-binding"
FT COMPBIAS 10..24
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 297
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U4C1"
FT MOD_RES 631
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U4C1"
FT MOD_RES 899
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920R4"
FT VARIANT 315
FT /note="A -> G (in dbSNP:rs17339512)"
FT /evidence="ECO:0000269|PubMed:9455477"
FT /id="VAR_026579"
FT VARIANT 779
FT /note="I -> V (in dbSNP:rs17292748)"
FT /id="VAR_049263"
FT VARIANT 1093
FT /note="P -> S (in dbSNP:rs2235804)"
FT /id="VAR_049264"
SQ SEQUENCE 1395 AA; 156865 MW; 89733CB9A59BC151 CRC64;
MTGAEIESGA QVKPEKKPGE EVVGGAEIEN DVPLVVRPKV RTQAQIMPGA RPKNKSKVMP
GASTKVETSA VGGARPKSKA KAIPVSRFKE EAQMWAQPRF GAERLSKTER NSQTNIIASP
LVSTDSVLVA KTKYLSEDRE LVNTDTESFP RRKAHYQAGF QPSFRSKEET NMGSWCCPRP
TSKQEASPNS DFKWVDKSVS SLFWSGDEVT AKFHPGNRVK DSNRSMHMAN QEANTMSRSQ
TNQELYIASS SGSEDESVKT PWFWARDKTN TWSGPREDPN SRSRFRSKKE VYVESSSGSE
HEDHLESWFG AGKEAKFRSK MRAGKEANNR ARHRAKREAC IDFMPGSIDV IKKESCFWPE
ENANTFSRPM IKKEARARAM TKEEAKTKAR ARAKQEARSE EEALIGTWFW ATDESSMADE
ASIESSLQVE DESIIGSWFW TEEEASMGTG ASSKSRPRTD GERIGDSLFG AREKTSMKTG
AEATSESILA ADDEQVIIGS WFWAGEEVNQ EAEEETIFGS WFWVIDAASV ESGVGVSCES
RTRSEEEEVI GPWFWSGEQV DIEAGIGEEA RPGAEEETIF GSWFWAENQT YMDCRAETSC
DTMQGAEEEE PIIGSWFWTR VEACVEGDVN SKSSLEDKEE AMIPCFGAKE EVSMKHGTGV
RCRFMAGAEE TNNKSCFWAE KEPCMYPAGG GSWKSRPEEE EDIVNSWFWS RKYTKPEAII
GSWLWATEES NIDGTGEKAK LLTEEETIIN SWFWKEDEAI SEATDREESR PEAEEGDIIG
SWFWAGEEDR LEPAAETREE DRLAAEKEGI VGSWFGAREE TIRREAGSCS KSSPKAEEEE
VIIGSWFWEE EASPEAVAGV GFESKPGTEE EEITVGSWFW PEEEASIQAG SQAVEEMESE
TEEETIFGSW FWDGKEVSEE AGPCCVSKPE DDEEMIVESW FWSRDKAIKE TGTVATCESK
PENEEGAIVG SWFEAEDEVD NRTDNGSNCG SRTLADEDEA IVGSWFWAGD EAHFESNPSP
VFRAICRSTC SVEQEPDPSR RPQSWEEVTV QFKPGPWGRV GFPSISPFRF PKEAASLFCE
MFGGKPRNMV LSPEGEDQES LLQPDQPSPE FPFQYDPSYR SVQEIREHLR AKESTEPESS
SCNCIQCELK IGSEEFEELL LLMEKIRDPF IHEISKIAMG MRSASQFTRD FIRDSGVVSL
IETLLNYPSS RVRTSFLENM IRMAPPYPNL NIIQTYICKV CEETLAYSVD SPEQLSGIRM
IRHLTTTTDY HTLVANYMSG FLSLLATGNA KTRFHVLKML LNLSENLFMT KELLSAEAVS
EFIGLFNREE TNDNIQIVLA IFENIGNNIK KETVFSDDDF NIEPLISAFH KVEKFAKELQ
GKTDNQNDPE GDQEN
