GRIN1_MOUSE
ID GRIN1_MOUSE Reviewed; 932 AA.
AC Q3UNH4; Q6PGF9; Q9QZY2;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2006, sequence version 2.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=G protein-regulated inducer of neurite outgrowth 1;
DE Short=GRIN1;
GN Name=Gprin1;
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].
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 92-932, TISSUE SPECIFICITY, INTERACTION WITH
RP GNAI1; GNAO1 AND GNAZ, SUBCELLULAR LOCATION, AND FUNCTION.
RC TISSUE=Brain;
RX PubMed=10480904; DOI=10.1074/jbc.274.38.26931;
RA Chen L.T., Gilman A.G., Kozasa T.;
RT "A candidate target for G protein action in brain.";
RL J. Biol. Chem. 274:26931-26938(1999).
RN [4]
RP PROTEIN SEQUENCE OF 312-325; 774-787 AND 813-833, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-795, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [6]
RP INTERACTION WITH GNAO1, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP 923-CYS-CYS-924, AND PALMITOYLATION AT CYS-923 AND CYS-924.
RX PubMed=15585744; DOI=10.1124/mol.104.003913;
RA Nakata H., Kozasa T.;
RT "Functional characterization of Galphao signaling through G protein-
RT regulated inducer of neurite outgrowth 1.";
RL Mol. Pharmacol. 67:695-702(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-795, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain cortex;
RX PubMed=17114649; DOI=10.1074/mcp.m600046-mcp200;
RA Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,
RA Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D., Gerrits B.,
RA Panse C., Schlapbach R., Mansuy I.M.;
RT "Qualitative and quantitative analyses of protein phosphorylation in naive
RT and stimulated mouse synaptosomal preparations.";
RL Mol. Cell. Proteomics 6:283-293(2007).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-190; SER-369; SER-495;
RP SER-519; SER-714; SER-817 AND SER-836, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
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).
CC -!- FUNCTION: May be involved in neurite outgrowth.
CC {ECO:0000269|PubMed:10480904}.
CC -!- SUBUNIT: Interacts with activated forms of GNAI1, GNAO1 and GNAZ.
CC {ECO:0000269|PubMed:10480904, ECO:0000269|PubMed:15585744}.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Lipid-anchor. Cell projection,
CC growth cone {ECO:0000250}. Note=Highly enriched in growth cone.
CC -!- TISSUE SPECIFICITY: Expressed specifically in brain (at protein level).
CC {ECO:0000269|PubMed:10480904}.
CC -!- PTM: Palmitoylation on Cys-923 and/or Cys-924 is required for membrane
CC targeting. {ECO:0000269|PubMed:15585744}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD55371.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK138306; BAE23617.1; -; mRNA.
DR EMBL; AK144210; BAE25773.1; -; mRNA.
DR EMBL; BC057044; AAH57044.1; -; mRNA.
DR EMBL; AF146569; AAD55371.1; ALT_INIT; mRNA.
DR CCDS; CCDS26534.1; -.
DR RefSeq; NP_001303639.1; NM_001316710.1.
DR RefSeq; NP_036144.2; NM_012014.4.
DR AlphaFoldDB; Q3UNH4; -.
DR BioGRID; 205060; 3.
DR IntAct; Q3UNH4; 2.
DR MINT; Q3UNH4; -.
DR STRING; 10090.ENSMUSP00000115539; -.
DR iPTMnet; Q3UNH4; -.
DR PhosphoSitePlus; Q3UNH4; -.
DR SwissPalm; Q3UNH4; -.
DR MaxQB; Q3UNH4; -.
DR PaxDb; Q3UNH4; -.
DR PeptideAtlas; Q3UNH4; -.
DR PRIDE; Q3UNH4; -.
DR ProteomicsDB; 269834; -.
DR Antibodypedia; 45999; 122 antibodies from 24 providers.
DR DNASU; 26913; -.
DR Ensembl; ENSMUST00000099506; ENSMUSP00000097106; ENSMUSG00000069227.
DR Ensembl; ENSMUST00000135343; ENSMUSP00000115539; ENSMUSG00000069227.
DR GeneID; 26913; -.
DR KEGG; mmu:26913; -.
DR UCSC; uc007qpa.1; mouse.
DR CTD; 114787; -.
DR MGI; MGI:1349455; Gprin1.
DR VEuPathDB; HostDB:ENSMUSG00000069227; -.
DR eggNOG; ENOG502S6S7; Eukaryota.
DR GeneTree; ENSGT00940000162796; -.
DR HOGENOM; CLU_346336_0_0_1; -.
DR InParanoid; Q3UNH4; -.
DR OMA; TKAPSWE; -.
DR OrthoDB; 612273at2759; -.
DR PhylomeDB; Q3UNH4; -.
DR TreeFam; TF337047; -.
DR BioGRID-ORCS; 26913; 2 hits in 74 CRISPR screens.
DR PRO; PR:Q3UNH4; -.
DR Proteomes; UP000000589; Chromosome 13.
DR RNAct; Q3UNH4; protein.
DR Bgee; ENSMUSG00000069227; Expressed in cortical plate and 139 other tissues.
DR Genevisible; Q3UNH4; MM.
DR GO; GO:0030426; C:growth cone; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; IDA:MGI.
DR GO; GO:0031175; P:neuron projection development; IDA:MGI.
DR InterPro; IPR026646; GPRIN2-like/GPRIN3.
DR InterPro; IPR032745; GRIN_C.
DR PANTHER; PTHR15718; PTHR15718; 2.
DR Pfam; PF15235; GRIN_C; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Cell projection; Direct protein sequencing; Lipoprotein;
KW Membrane; Palmitate; Phosphoprotein; Reference proteome.
FT CHAIN 1..932
FT /note="G protein-regulated inducer of neurite outgrowth 1"
FT /id="PRO_0000235978"
FT REGION 1..149
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 178..808
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 821..932
FT /note="Interaction with GNAO1"
FT REGION 866..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 67..81
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..244
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..282
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..358
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 406..445
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 474..492
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..565
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..592
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 22
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2K8"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2K8"
FT MOD_RES 190
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 369
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 377
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2K8"
FT MOD_RES 393
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2K8"
FT MOD_RES 495
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 714
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 795
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:16452087"
FT MOD_RES 817
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 836
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 917
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z2K8"
FT LIPID 923
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:15585744"
FT LIPID 924
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:15585744"
FT MUTAGEN 923..924
FT /note="CC->AA: Abolishes membrane targeting."
FT /evidence="ECO:0000269|PubMed:15585744"
FT CONFLICT 215
FT /note="E -> G (in Ref. 3; AAD55371)"
FT /evidence="ECO:0000305"
FT CONFLICT 458
FT /note="K -> R (in Ref. 1; BAE25773)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 932 AA; 95496 MW; 2AB823F6A8CBF311 CRC64;
MRDCCSSPKA IPAPPRHALD QSLGMDPRHT SSSGAAEGAS CSERPAGSLA CPSPNCSPLP
ETPRAHGALT SDNSGTTLFG KPEPMSSAEA TPTASEIRNP VFSGKMDGNS LKQADSTSTR
KEEAGSLRNE ESMLKGKAEP MIYGKGEPGT VGRVDCTASG AENSGSLGKV DMPCSSKVDI
VSPGGDNAGS LRKVETISSG KMDPKTENVM HSRRERPGST GEGDLVSLRE NDMKPPDNTD
SASTKKTDPE FSGKLTPGSS GKTELVSSVT VAPVTSENVN PVCSGGAGPA AVGNSETLSS
VKKDPQLLGK KEAVSSGEGG SVSVRMAETV SARQPEGMFP AKTDSTSSNS TGPSGRADPV
SLRNSELVSP VKPERLSSGQ AERVSLVKTE TLSSGKEDPR SSRRVDHTTV TGNMQTSQKG
NPESSGKTDL GSSSSGDTRS LGTWGSLSAA KAEVTEGKGD PQPWKKASLP ASEKTDPLAS
SKAGSASQGK AETVSPGEVD AMTLGKTVPT SSGKTALVSP GKVDLMTSER AEGIPELQAS
EKGNPVNSTR VDTGATGSTE PKSGVKVITQ IPGATSPGKV ETPSLQKEQP QLSEKTDPSR
KVDPPTTVEP VSLGKADSAS PSPRKAESQT SAKTVPQAPD KATSSLRQSD GTPYSSAQPQ
RDTRSIGSLP EREPSASTSQ KDLAAAAAQK SPSAEAAAPP PGPRTRDNFT KAPSWDAGAP
PPREDAGTQA GAQACVSVAV SPMSPQDGAG GPAFSFQAAP RAPSPAPRPP SRRDAGLQVS
LGAAETRSVA TGPMTPQAAA PPAVPPVFPE VRVRPGSVLA AALAPQEATE PVRDVSWDEK
GMTWEVYGAS MEVEVLGMAI QKHLERQIEE HGRQGAPAPA PPPAVRAGPG RAGSVRTAPA
EGAAKRPPGL FRALLQSVRR PRCCSRAGPT AE
