GASP1_MOUSE
ID GASP1_MOUSE Reviewed; 1347 AA.
AC Q5U4C1; A2AGB6; Q8BKR8; Q8BUN4; Q8BYK9; Q8CHF4; Q8R095;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=G-protein coupled receptor-associated sorting protein 1;
DE Short=GASP-1;
GN Name=Gprasp1; Synonyms=Kiaa0443;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Eye;
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 [LARGE SCALE MRNA] OF 1-379 AND 943-1347 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Embryo, Hippocampus, and Hypothalamus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP TISSUE SPECIFICITY.
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 [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295; SER-619 AND SER-626, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
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:23954414}.
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 as well as D2
CC dopamine receptor/DRD2. Interacts with PER1 (By similarity). Interacts
CC with BECN2; the interaction is direct. {ECO:0000250,
CC ECO:0000269|PubMed:23954414}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5U4C1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5U4C1-2; Sequence=VSP_019080;
CC -!- TISSUE SPECIFICITY: Expressed in the brain, with higher expression in
CC the hippocampus, hypothalamus and olfactory bulb.
CC {ECO:0000269|PubMed:15086532}.
CC -!- SIMILARITY: Belongs to the GPRASP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC41425.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB093241; BAC41425.1; ALT_INIT; mRNA.
DR EMBL; AL683822; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC027187; AAH27187.1; -; mRNA.
DR EMBL; BC085157; AAH85157.1; -; mRNA.
DR EMBL; AK039156; BAC30259.1; -; mRNA.
DR EMBL; AK050919; BAC34459.2; -; mRNA.
DR EMBL; AK083192; BAC38803.1; -; mRNA.
DR CCDS; CCDS30409.1; -. [Q5U4C1-1]
DR RefSeq; NP_001004359.1; NM_001004359.2. [Q5U4C1-1]
DR RefSeq; NP_001005385.1; NM_001005385.1. [Q5U4C1-1]
DR RefSeq; NP_080357.4; NM_026081.5. [Q5U4C1-1]
DR AlphaFoldDB; Q5U4C1; -.
DR BioGRID; 212084; 3.
DR IntAct; Q5U4C1; 2.
DR STRING; 10090.ENSMUSP00000108769; -.
DR iPTMnet; Q5U4C1; -.
DR PhosphoSitePlus; Q5U4C1; -.
DR EPD; Q5U4C1; -.
DR MaxQB; Q5U4C1; -.
DR PaxDb; Q5U4C1; -.
DR PeptideAtlas; Q5U4C1; -.
DR PRIDE; Q5U4C1; -.
DR ProteomicsDB; 271633; -. [Q5U4C1-1]
DR ProteomicsDB; 271634; -. [Q5U4C1-2]
DR Antibodypedia; 383; 135 antibodies from 28 providers.
DR DNASU; 67298; -.
DR Ensembl; ENSMUST00000113144; ENSMUSP00000108769; ENSMUSG00000043384. [Q5U4C1-1]
DR Ensembl; ENSMUST00000113145; ENSMUSP00000108770; ENSMUSG00000043384. [Q5U4C1-1]
DR Ensembl; ENSMUST00000113147; ENSMUSP00000108772; ENSMUSG00000043384. [Q5U4C1-1]
DR Ensembl; ENSMUST00000166554; ENSMUSP00000132225; ENSMUSG00000043384. [Q5U4C1-1]
DR GeneID; 67298; -.
DR KEGG; mmu:67298; -.
DR UCSC; uc009uhn.1; mouse. [Q5U4C1-1]
DR CTD; 9737; -.
DR MGI; MGI:1917418; Gprasp1.
DR VEuPathDB; HostDB:ENSMUSG00000043384; -.
DR eggNOG; ENOG502S6CE; Eukaryota.
DR GeneTree; ENSGT00940000163396; -.
DR HOGENOM; CLU_008490_0_0_1; -.
DR InParanoid; Q5U4C1; -.
DR OMA; WFWATEE; -.
DR PhylomeDB; Q5U4C1; -.
DR TreeFam; TF335652; -.
DR BioGRID-ORCS; 67298; 2 hits in 73 CRISPR screens.
DR ChiTaRS; Gprasp1; mouse.
DR PRO; PR:Q5U4C1; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q5U4C1; protein.
DR Bgee; ENSMUSG00000043384; Expressed in central gray substance of midbrain and 244 other tissues.
DR Genevisible; Q5U4C1; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
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 Alternative splicing; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..1347
FT /note="G-protein coupled receptor-associated sorting
FT protein 1"
FT /id="PRO_0000239051"
FT REGION 1..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 145..174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 188..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..344
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 364..396
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 460..485
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..167
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 257..281
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 MOD_RES 295
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 619
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 626
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 860
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q920R4"
FT MOD_RES 862
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q920R4"
FT VAR_SEQ 1..473
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019080"
FT CONFLICT 942
FT /note="V -> L (in Ref. 1; BAC41425)"
FT /evidence="ECO:0000305"
FT CONFLICT 943
FT /note="I -> F (in Ref. 4; BAC30259)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1347 AA; 151745 MW; 1FD29E59CBF91B59 CRC64;
MTRAEVEPGA QAKAENKPGD ENANAAEVEP EAPLVVRPKV RTQIMTGARP KVKPKGTPGA
RPKGETSTPG GAYAKCKPKA IPIARSKHDA QVWAPNKFRG ESMSKMGKQC QISAADPPLL
SNDSGMVAQA KCLPVDRELA NMDTESIPKK ANSPAGFQPS YGSEEGTNMG SWYRARPVPK
GEAYENSDFK WADKPSGSPS FWNRDEASTR FRPRKSMKAN NRFRHMAKQE ANTMPRHKNK
QEFYNISSSD SEDESGKTPW FWPKDKTKVW SKPKEEPNSR SWFRSKKEVR VESTSGSECE
NPTKSLFWSG EEAKSRSKPR ARKGVNMRAR QQAKREACSD AMSGAIDTNK KESWFLPEEK
ANVFSKSKTK KEPRTRAVPK EEVKTKARAS TKQEARPEEE VLVGAWFWDT QESTMADRIS
IKTTFVEEEP IVGDWFWSEE EASVDSETCH TSRPRAKEEQ VSSFCLGSGK KSSMESGPKA
TSKSMPVAKE DEVVIGSWFW ADDEEINLQA DDESIFGSWF WGTGENSLRS VGVNCEKMPK
AGEKEVTDSW FWAGDVNTEA EVEEQARSAS TKATIFVPWF WSEKQPNMDL GSEPCSDIMA
GAEEEPIIGP WFWAKVDNSV EAEVNSKSSL EDEEEPIRSP WFGAREQTDM KYAAGIRYKP
MAEAEDANKK SCVWAKEPCL YPTNRECLKS TLGEKEDTVD PWLWSNNYPR TKTITGSWLW
AAEEGNIDDE TGEKIKLPTL EDNAFNSWFW KENEESIVEA PKREEFRPEA EEEDIIGSWF
WAGDEDRFEP AAKINEENKI ASEDEDTVGS WFWGNEEASL EAVRRGTFES APGIKEEKVT
GSWFWTDKAK VGAGSQTVET GSETEEEAIF ESLIWAAKKD SIQAGVKRVS KPKDDGNIAV
GSWLWSSDKA TKEAKTLIVS EASPENGKES VVKFGSRAKD EVINKTGSGD NCKHSTEAET
IVGAWFWEGD EASFESNPVP VCKAVCEPES SAEHEPDPSR RPQSWDEVTV QFKAGPWGKA
GFPPMNPFRF PKEAASLFAE MFGGKPKLVE VGPEREPEPQ FPFQYDPSYR SVREIREHLK
ARESAQPENW SCNCIQCELR IGSEEFEELL LLMDRNRDPF IHEISKIAMG MRGASQFTRD
FIRNSGVVSL IEALLNYPSS RVRTRFLENM VRMAPPYPDL NMIETYVCQI CEDTFDYDLD
SPDQLSGLTM ITHLTATSDY HKVVVNYLAG FFYLLNSGNT KTRFHVLKLL LNLSENLVMT
KRLLVTDSVS EFMDLINREE SDENIQIVLA IFETISKHIQ KEALFSDDDD DDEEEDAVNL
EPFISAFREA EKIAKELKRK PGNQKAP
