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   05-FEB-2025, entry version 147.
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; 37.
DR   IntAct; Q5JY77; 26.
DR   STRING; 9606.ENSP00000498934; -.
DR   GlyGen; Q5JY77; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q5JY77; -.
DR   PhosphoSitePlus; Q5JY77; -.
DR   BioMuta; GPRASP1; -.
DR   DMDM; 126302546; -.
DR   jPOST; Q5JY77; -.
DR   MassIVE; Q5JY77; -.
DR   PaxDb; 9606-ENSP00000445683; -.
DR   PeptideAtlas; Q5JY77; -.
DR   ProteomicsDB; 63484; -.
DR   Antibodypedia; 383; 159 antibodies from 29 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   AGR; HGNC:24834; -.
DR   CTD; 9737; -.
DR   DisGeNET; 9737; -.
DR   GeneCards; GPRASP1; -.
DR   HGNC; HGNC:24834; GPRASP1.
DR   HPA; ENSG00000198932; Tissue enhanced (brain).
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; 9664939at2759; -.
DR   PhylomeDB; Q5JY77; -.
DR   TreeFam; TF335652; -.
DR   PathwayCommons; Q5JY77; -.
DR   SignaLink; Q5JY77; -.
DR   BioGRID-ORCS; 9737; 14 hits in 773 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 192 other cell types or tissues.
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   FunFam; 1.25.10.10:FF:000258; G-protein coupled receptor-associated sorting protein 2; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR006911; ARM-rpt_dom.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR043374; GASP1-3.
DR   PANTHER; PTHR46414:SF3; G-PROTEIN COUPLED RECEPTOR-ASSOCIATED SORTING PROTEIN 1; 1.
DR   PANTHER; PTHR46414; PROTEIN BHLHB9-RELATED; 1.
DR   Pfam; PF04826; Arm_2; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Phosphoprotein; Proteomics identification; 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        269..281
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        457..469
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
//