GPSM1_MOUSE
ID GPSM1_MOUSE Reviewed; 673 AA.
AC Q6IR34; A2AIX7; A2AIX8; A2AIX9; Q61366; Q8BUK4; Q8BX78; Q8R0R9;
DT 17-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 20-APR-2010, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=G-protein-signaling modulator 1;
DE AltName: Full=Activator of G-protein signaling 3;
GN Name=Gpsm1; Synonyms=Ags3; ORFNames=C10a;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, and Embryonic heart;
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 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 GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [5]
RP PROTEIN SEQUENCE OF 46-63, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=OF1; TISSUE=Hippocampus;
RA Lubec G., Sunyer B., Chen W.-Q.;
RL Submitted (JAN-2009) to UniProtKB.
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 419-673.
RC TISSUE=Erythroleukemia;
RA Miller I.J., Bieker J.J.;
RT "Subtractive cloning of murine erythroleukemia mRNAs.";
RL Submitted (SEP-1993) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP INTERACTION WITH STK11/LKB1 AND MACF1, AND PHOSPHORYLATION.
RX PubMed=12719437; DOI=10.1074/jbc.c200686200;
RA Blumer J.B., Bernard M.L., Peterson Y.K., Nezu J., Chung P., Dunican D.J.,
RA Knoblich J.A., Lanier S.M.;
RT "Interaction of activator of G-protein signaling 3 (AGS3) with LKB1, a
RT serine/threonine kinase involved in cell polarity and cell cycle
RT progression: phosphorylation of the G-protein regulatory (GPR) motif as a
RT regulatory mechanism for the interaction of GPR motifs with Gi alpha.";
RL J. Biol. Chem. 278:23217-23220(2003).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-653, 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 [9]
RP FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, AND INTERACTION WITH
RP GNAI3.
RX PubMed=16009138; DOI=10.1016/j.cell.2005.05.009;
RA Sanada K., Tsai L.-H.;
RT "G protein betagamma subunits and AGS3 control spindle orientation and
RT asymmetric cell fate of cerebral cortical progenitors.";
RL Cell 122:119-131(2005).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-410; SER-490 AND SER-491, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Heart, Kidney, Lung, Pancreas, Spleen, 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 [11]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-418, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
CC -!- FUNCTION: Guanine nucleotide dissociation inhibitor (GDI) which
CC functions as a receptor-independent activator of heterotrimeric G-
CC protein signaling. Keeps G(i/o) alpha subunit in its GDP-bound form
CC thus uncoupling heterotrimeric G-proteins signaling from G protein-
CC coupled receptors. Controls spindle orientation and asymmetric cell
CC fate of cerebral cortical progenitors. May also be involved in
CC macroautophagy in intestinal cells. May play a role in drug addiction.
CC {ECO:0000269|PubMed:16009138}.
CC -!- SUBUNIT: Interacts with GNAI1 and GNAI2 preferentially in their GDP-
CC bound state. May also interact with GNAO1. Interacts with
CC INSC/inscuteable and FRMPD1 (By similarity). Interacts with GNAI3.
CC Interacts with STK11/LKB1 and MACF1. {ECO:0000250,
CC ECO:0000269|PubMed:12719437, ECO:0000269|PubMed:16009138}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol. Endoplasmic reticulum
CC membrane; Peripheral membrane protein; Cytoplasmic side. Golgi
CC apparatus membrane {ECO:0000250}; Peripheral membrane protein
CC {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q6IR34-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6IR34-2; Sequence=VSP_039033;
CC Name=3;
CC IsoId=Q6IR34-3; Sequence=VSP_039029;
CC Name=4;
CC IsoId=Q6IR34-4; Sequence=VSP_039030, VSP_039031, VSP_039032;
CC Name=5;
CC IsoId=Q6IR34-5; Sequence=VSP_039030;
CC -!- TISSUE SPECIFICITY: Expressed in neural progenitor cells (at protein
CC level). {ECO:0000269|PubMed:16009138}.
CC -!- DEVELOPMENTAL STAGE: Expressed in brain at 14 dpc.
CC {ECO:0000269|PubMed:16009138}.
CC -!- DOMAIN: The GoLoco domains are essential for the GDI activity toward
CC G(i/o) alpha. The GoLoco domains mediate interaction with G(i/o) alpha
CC (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylation regulates interaction with G(i/o) alpha.
CC {ECO:0000269|PubMed:12719437}.
CC -!- SIMILARITY: Belongs to the GPSM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26486.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH71197.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK048691; BAC33422.1; -; mRNA.
DR EMBL; AK084631; BAC39236.1; -; mRNA.
DR EMBL; AL732541; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH466542; EDL08301.1; -; Genomic_DNA.
DR EMBL; CH466542; EDL08300.1; -; Genomic_DNA.
DR EMBL; BC026486; AAH26486.1; ALT_INIT; mRNA.
DR EMBL; BC071197; AAH71197.1; ALT_INIT; mRNA.
DR EMBL; L23316; AAB00119.1; -; mRNA.
DR CCDS; CCDS15800.1; -. [Q6IR34-1]
DR CCDS; CCDS57158.1; -. [Q6IR34-2]
DR CCDS; CCDS57159.1; -. [Q6IR34-5]
DR RefSeq; NP_001186075.1; NM_001199146.1. [Q6IR34-2]
DR RefSeq; NP_001186076.1; NM_001199147.1. [Q6IR34-5]
DR RefSeq; NP_700459.2; NM_153410.5. [Q6IR34-1]
DR RefSeq; XP_006498316.1; XM_006498253.3.
DR AlphaFoldDB; Q6IR34; -.
DR SMR; Q6IR34; -.
DR BioGRID; 212469; 13.
DR CORUM; Q6IR34; -.
DR IntAct; Q6IR34; 13.
DR MINT; Q6IR34; -.
DR STRING; 10090.ENSMUSP00000065000; -.
DR iPTMnet; Q6IR34; -.
DR PhosphoSitePlus; Q6IR34; -.
DR EPD; Q6IR34; -.
DR jPOST; Q6IR34; -.
DR MaxQB; Q6IR34; -.
DR PaxDb; Q6IR34; -.
DR PeptideAtlas; Q6IR34; -.
DR PRIDE; Q6IR34; -.
DR ProteomicsDB; 271074; -. [Q6IR34-1]
DR ProteomicsDB; 271075; -. [Q6IR34-2]
DR ProteomicsDB; 271076; -. [Q6IR34-3]
DR ProteomicsDB; 271077; -. [Q6IR34-4]
DR ProteomicsDB; 271078; -. [Q6IR34-5]
DR Antibodypedia; 32122; 212 antibodies from 27 providers.
DR DNASU; 67839; -.
DR Ensembl; ENSMUST00000066889; ENSMUSP00000067964; ENSMUSG00000026930. [Q6IR34-5]
DR Ensembl; ENSMUST00000066936; ENSMUSP00000065000; ENSMUSG00000026930. [Q6IR34-1]
DR Ensembl; ENSMUST00000078616; ENSMUSP00000077686; ENSMUSG00000026930. [Q6IR34-2]
DR GeneID; 67839; -.
DR KEGG; mmu:67839; -.
DR UCSC; uc008iun.2; mouse. [Q6IR34-1]
DR UCSC; uc008iuo.2; mouse. [Q6IR34-2]
DR UCSC; uc008iup.2; mouse. [Q6IR34-5]
DR CTD; 26086; -.
DR MGI; MGI:1915089; Gpsm1.
DR VEuPathDB; HostDB:ENSMUSG00000026930; -.
DR eggNOG; KOG1130; Eukaryota.
DR GeneTree; ENSGT00940000154667; -.
DR HOGENOM; CLU_012445_1_0_1; -.
DR InParanoid; Q6IR34; -.
DR OMA; RLSTETW; -.
DR OrthoDB; 733786at2759; -.
DR PhylomeDB; Q6IR34; -.
DR TreeFam; TF328344; -.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 67839; 0 hits in 76 CRISPR screens.
DR ChiTaRS; Gpsm1; mouse.
DR PRO; PR:Q6IR34; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q6IR34; protein.
DR Bgee; ENSMUSG00000026930; Expressed in rostral migratory stream and 242 other tissues.
DR ExpressionAtlas; Q6IR34; baseline and differential.
DR Genevisible; Q6IR34; MM.
DR GO; GO:0005938; C:cell cortex; ISO:MGI.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; ISO:MGI.
DR GO; GO:0000139; C:Golgi membrane; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; ISO:MGI.
DR GO; GO:0001965; F:G-protein alpha-subunit binding; ISO:MGI.
DR GO; GO:0005092; F:GDP-dissociation inhibitor activity; ISO:MGI.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0000132; P:establishment of mitotic spindle orientation; IBA:GO_Central.
DR GO; GO:0034260; P:negative regulation of GTPase activity; ISO:MGI.
DR GO; GO:1905098; P:negative regulation of guanyl-nucleotide exchange factor activity; ISO:MGI.
DR GO; GO:0007399; P:nervous system development; IEA:UniProtKB-KW.
DR GO; GO:0016239; P:positive regulation of macroautophagy; ISO:MGI.
DR GO; GO:0008277; P:regulation of G protein-coupled receptor signaling pathway; ISO:MGI.
DR Gene3D; 1.25.40.10; -; 3.
DR InterPro; IPR003109; GoLoco_motif.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF02188; GoLoco; 4.
DR SMART; SM00390; GoLoco; 4.
DR SMART; SM00028; TPR; 6.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50877; GOLOCO; 4.
DR PROSITE; PS50005; TPR; 6.
DR PROSITE; PS50293; TPR_REGION; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cytoplasm; Developmental protein;
KW Differentiation; Direct protein sequencing; Endoplasmic reticulum;
KW Golgi apparatus; Membrane; Methylation; Neurogenesis; Phosphoprotein;
KW Reference proteome; Repeat; TPR repeat.
FT CHAIN 1..673
FT /note="G-protein-signaling modulator 1"
FT /id="PRO_0000252403"
FT REPEAT 28..61
FT /note="TPR 1"
FT REPEAT 66..99
FT /note="TPR 2"
FT REPEAT 106..139
FT /note="TPR 3"
FT REPEAT 146..178
FT /note="TPR 4"
FT REPEAT 180..199
FT /note="TPR 5"
FT REPEAT 206..239
FT /note="TPR 6"
FT REPEAT 246..279
FT /note="TPR 7"
FT REPEAT 286..319
FT /note="TPR 8"
FT REPEAT 326..359
FT /note="TPR 9"
FT DOMAIN 493..515
FT /note="GoLoco 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 546..568
FT /note="GoLoco 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 594..616
FT /note="GoLoco 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT DOMAIN 628..650
FT /note="GoLoco 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00097"
FT REGION 1..507
FT /note="Mediates association with membranes"
FT /evidence="ECO:0000250"
FT REGION 361..485
FT /note="Interaction with STK11/LKB1"
FT /evidence="ECO:0000250"
FT REGION 420..475
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 508..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 644..673
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..437
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 453..471
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 410
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 418
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 442
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YR5"
FT MOD_RES 467
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YR5"
FT MOD_RES 469
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q86YR5"
FT MOD_RES 490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 491
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 543
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R080"
FT MOD_RES 567
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9R080"
FT MOD_RES 653
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747"
FT VAR_SEQ 1..23
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000305"
FT /id="VSP_039029"
FT VAR_SEQ 1..22
FT /note="MASPAPPVAEELPGPASRRLYS -> MLASAMEGQPLALSLAEKAVCKVVYG
FT APRPRPLLLPVGLELWLYVQKMRNLQRK (in isoform 4 and isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039030"
FT VAR_SEQ 251..271
FT /note="NLGNAHIFLGRFDVAAEHYKK -> QPYPTLDSVGSRLSTVAMIPQ (in
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039031"
FT VAR_SEQ 272..673
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039032"
FT VAR_SEQ 424..483
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_039033"
FT CONFLICT 668
FT /note="C -> Y (in Ref. 6; AAB00119)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 673 AA; 74362 MW; 60D284A5340604E7 CRC64;
MASPAPPVAE ELPGPASRRL YSRMEASCLE LALEGERLCK AGDFKAGVAF FEAAVQVGTE
DLKTLSAIYS QLGNAYFYLK EYARALQFHK HDLLLARTIG DRMGEAKASG NLGNTLKVLG
RFDEAIVCCQ RHLDIAQEQG DKVGEARALY NIGNVYHAKG KQLSWNAAQD PGHLPPDVRE
TLHRASEFYE RNLSLVKELG DRAAQGRAYG NLGNTHYLLG NFTEATTFHK ERLAIAKEFG
DKAAERRAYS NLGNAHIFLG RFDVAAEHYK KTLQLSRQLR DQAVEAQACY SLGNTYTLLQ
DYERAAEYHL RHLVIAQELA DRVGEGRACW SLGNAYVSMG SPAQALTFAK KHLQISQEIG
DRNGELTARM NIAHLQLALG RLTSPAAAEK PDLAGYEAQG ARPKRTQRLS AETWDLLRLP
LDREQNGETH HTGDWRGPGR DSLPLPMRSR KYQEGPDAIE RRPREGSHSP LDSADVRVQV
PRTGIPRAPS SDEECFFDLL SKFQSSRMDD QRCPLEEGQA GAAEATAAPS VEDRAAQSSV
TASPQTEEFF DLIASSQSRR LDDQRASVGS LPGLRITLNN VGHLRGDGDA QEPGDEFFNM
LIKYQSSRID DQRCPPPDVL PRGPTMPDED FFSLIQRVQA KRMDEQRVDL AGSPEQEASG
LPDPQQQCPP GAS
