GASP1_RAT
ID GASP1_RAT Reviewed; 1346 AA.
AC Q920R4;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=G-protein coupled receptor-associated sorting protein 1;
DE Short=GASP-1;
DE AltName: Full=Per1-interacting protein;
GN Name=Gprasp1; Synonyms=Pips;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, AND INTERACTION WITH
RP PER1.
RX PubMed=11597585; DOI=10.1016/s0006-8993(01)02857-8;
RA Matsuki T., Kiyama A., Kawabuchi M., Okada M., Nagai K.;
RT "A novel protein interacts with a clock-related protein, rPer1.";
RL Brain Res. 916:1-10(2001).
RN [2]
RP FUNCTION, TISSUE SPECIFICITY, AND INTERACTION WITH DRD2.
RX PubMed=16049099; DOI=10.1073/pnas.0502418102;
RA Bartlett S.E., Enquist J., Hopf F.W., Lee J.H., Gladher F., Kharazia V.,
RA Waldhoer M., Mailliard W.S., Armstrong R., Bonci A., Whistler J.L.;
RT "Dopamine responsiveness is regulated by targeted sorting of D2
RT receptors.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11521-11526(2005).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-860 AND SER-862, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 (By
CC similarity). {ECO:0000250, ECO:0000269|PubMed:16049099}.
CC -!- SUBUNIT: Interacts with cytoplasmic tails of a variety of G-protein
CC coupled receptors such as delta opioid receptor/OPRD1, beta-2
CC adrenergic receptor/ADRB2 and D4 dopamine receptor/DRD4. Interacts with
CC BECN2; the interaction is direct (By similarity) and with D2 dopamine
CC receptor/DRD2. Interacts with PER1. {ECO:0000250,
CC ECO:0000269|PubMed:11597585, ECO:0000269|PubMed:16049099}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:11597585}.
CC -!- TISSUE SPECIFICITY: Expressed in the brain.
CC {ECO:0000269|PubMed:16049099}.
CC -!- SIMILARITY: Belongs to the GPRASP family. {ECO:0000305}.
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DR EMBL; AB051807; BAB64314.1; -; mRNA.
DR RefSeq; NP_599213.1; NM_134386.1.
DR AlphaFoldDB; Q920R4; -.
DR STRING; 10116.ENSRNOP00000066239; -.
DR iPTMnet; Q920R4; -.
DR PhosphoSitePlus; Q920R4; -.
DR jPOST; Q920R4; -.
DR PaxDb; Q920R4; -.
DR PRIDE; Q920R4; -.
DR GeneID; 171407; -.
DR KEGG; rno:171407; -.
DR CTD; 9737; -.
DR RGD; 621343; Gprasp1.
DR eggNOG; ENOG502S6CE; Eukaryota.
DR InParanoid; Q920R4; -.
DR PhylomeDB; Q920R4; -.
DR PRO; PR:Q920R4; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0008333; P:endosome to lysosome transport; ISS:UniProtKB.
DR GO; GO:1990172; P:G protein-coupled receptor catabolic process; ISS:UniProtKB.
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..1346
FT /note="G-protein coupled receptor-associated sorting
FT protein 1"
FT /id="PRO_0000239052"
FT REGION 1..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 144..177
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 192..258
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..399
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 461..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 984..1004
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..206
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 345..399
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..480
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 987..1001
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U4C1"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U4C1"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5U4C1"
FT MOD_RES 860
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
SQ SEQUENCE 1346 AA; 151349 MW; C6B07255D167E951 CRC64;
MTGAEVEPGA QAKAENKPGD ENANAAEVEP EVPLVVRPKV RTQMMTGARP KVKPKGTPGA
RPKGETSSPG GAYAKCKPRS IPISRSKHDA QVWAPSKFRG ESMSKMGKQC QISAADSPLV
SNDSGAVAQA KCLSVDRELA NMDTESIPKK ASSPARFQPS FGPEEGTSMG SWYRPRPIPK
GEAYENSDFK WADKSSGSSS FWNRDETSTR FRPRKSMKSN TRFRHMAKQE ANTMSRHKNK
QEFYNISSSD SEDESAKTPW FWAKDKPKVW SRPKEEPNTR SWFRSKKEVR VESTSGSECE
NHTKSLFWSG EEAKCRSKPR ARKGVNMRAR HQAKREAYSD VTSGSVDKNK KDSWFLPEEK
ANAFSKSKTK KEPRTRAMPR EEVKTKARAS TKQEARPEEE VLVGAWVLDT QDNTMGERIS
MKTTCVEEEP IVGDWFWSEE EASVDSETGL KSRPRAKEEQ VSSFCLGSGK KTSMESGPKA
TSKSMPVAKD DEVIIGSWFW ADDEEISLQA DDESIFGSWF WGTGEKSLRS VGVSCEKMPK
SGEKEVTDSW FWAGEVNTEA EMEEQASSAS TKGTIFVPWF WSEKQAHMDL GTEPCSDIMA
GAEEEPIIGP WFWAKVDNSV EAEVNSKSSL EDEEEPIRSP WFGAREQPNM KYAAGVGYKP
MAEAEEANKK SCVWAKEPCL YPTNRESLKS TLGEKEDTVD PWLWSNNYPR TETITGSWLW
AAEEGNIDDE TGEEIKLPTL EDNVFNSWSW KENEETVVEA PNREESKPEA EEEDIIGSWF
WAGDEDRFQP AAKIKEENKI APEDEDTVGS WFWGKEEASV EAVKGGTFES VSGIKEEKAT
GSWFWTDKAK IGAGPQTVET GSETEDEAIF ESLIWAAKKD SMQTGVNRVS KPKDEGEGIE
SWLWSGDKAT TESKTVTVSE SSPENGKESI VKFGSRAKDE VINKTGSGDN CKFSTEAESI
VGPWFWEGDE ASFESNPVPV CKAACEPESS TEHEPDPSRR PQSWDEVTVQ FKPGPWGKAG
FPSLNPFRFP KEAASLFAEM FGGKPKLVEV GTEREPEPQF PFQYDPSYRS VREIREHLKA
RESAQAENWS CNCIQCELRI GSEEFEELLL MMDRNRDPFI HEISKIAMGM RGASQFTRDF
IRNSGVISLI EALMNYPSSR ARTAFLENMI QMAPTYPDLN MIETYVCQVC EDTFDYDLDS
SDQLSGLTMI THLTTTFDYH KVVVAYLAGF YYLLNSGNTT TRFHVLKLLL NLSESLVMTK
RLLITDSVSE FMALFNREDS DENIQIILAI FENISKNIQK EALFADDEEE EEEEEAVNLE
PLISAFREAE KFAKELKRKT DDQKSP
