MYO1G_HUMAN
ID MYO1G_HUMAN Reviewed; 1018 AA.
AC B0I1T2; Q8TEI9; Q8TES2; Q96BE2; Q96RI5; Q96RI6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Unconventional myosin-Ig;
DE Contains:
DE RecName: Full=Minor histocompatibility antigen HA-2 {ECO:0000303|PubMed:11544309};
DE Short=mHag HA-2;
GN Name=MYO1G; Synonyms=HA2;
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] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 193-1018 (ISOFORM 3), AND VARIANT THR-489.
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS THR-489
RP AND ARG-861.
RC TISSUE=Spleen;
RA Yamakawa H., Kikuno R.F., Nagase T., Ohara O.;
RT "Multiplex amplification and cloning of 5'-ends of cDNA by ligase-free
RT recombination: preparation of full-length cDNA clones encoding motor
RT proteins.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 33-665 (ISOFORM 4), IDENTIFICATION AS THE
RP MINOR HISTOCOMPATIBILITY ANTIGEN HA-2, VARIANTS HA-2M MET-49 AND THR-489,
RP CHARACTERIZATION OF VARIANT HA-2M MET-49, AND TISSUE SPECIFICITY.
RX PubMed=11544309; DOI=10.4049/jimmunol.167.6.3223;
RA Pierce R.A., Field E.D., Mutis T., Golovina T.N., Von Kap-Herr C.,
RA Wilke M., Pool J., Shabanowitz J., Pettenati M.J., Eisenlohr L.C.,
RA Hunt D.F., Goulmy E., Engelhard V.H.;
RT "The HA-2 minor histocompatibility antigen is derived from a diallelic gene
RT encoding a novel human class I myosin protein.";
RL J. Immunol. 167:3223-3230(2001).
RN [5]
RP PROTEIN SEQUENCE OF 41-49 (ISOFORM 1).
RX PubMed=7539551; DOI=10.1126/science.7539551;
RA den Haan J.M.M., Sherman N.E., Blokland E., Huczko E., Koning F.,
RA Drijfhout J.W., Skipper J., Shabanowitz J., Hunt D.F., Engelhard V.H.,
RA Goulmy E.;
RT "Identification of a graft versus host disease-associated human minor
RT histocompatibility antigen.";
RL Science 268:1476-1480(1995).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 723-1018 (ISOFORM 1), AND VARIANT
RP ARG-861.
RC TISSUE=B-cell;
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 [7]
RP SUBCELLULAR LOCATION.
RX PubMed=19968988; DOI=10.1016/j.febslet.2009.11.096;
RA Olety B., Walte M., Honnert U., Schillers H., Bahler M.;
RT "Myosin 1G (Myo1G) is a haematopoietic specific myosin that localises to
RT the plasma membrane and regulates cell elasticity.";
RL FEBS Lett. 584:493-499(2010).
RN [8]
RP SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND MUTAGENESIS OF LYS-815;
RP ARG-826; ARG-876; ARG-880; ARG-885; LYS-898; ARG-903; ARG-906; ARG-909;
RP ARG-934; ARG-945; ARG-947 AND ARG-953.
RX PubMed=20071333; DOI=10.1074/jbc.m109.086959;
RA Patino-Lopez G., Aravind L., Dong X., Kruhlak M.J., Ostap E.M., Shaw S.;
RT "Myosin 1G is an abundant class I myosin in lymphocytes whose localization
RT at the plasma membrane depends on its ancient divergent pleckstrin homology
RT (PH) domain (Myo1PH).";
RL J. Biol. Chem. 285:8675-8686(2010).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: Unconventional myosin required during immune response for
CC detection of rare antigen-presenting cells by regulating T-cell
CC migration. Unconventional myosins are actin-based motor molecules with
CC ATPase activity and serve in intracellular movements. Acts as a
CC regulator of T-cell migration by generating membrane tension, enforcing
CC cell-intrinsic meandering search, thereby enhancing detection of rare
CC antigens during lymph-node surveillance, enabling pathogen eradication.
CC Also required in B-cells, where it regulates different
CC membrane/cytoskeleton-dependent processes. Involved in Fc-gamma
CC receptor (Fc-gamma-R) phagocytosis. {ECO:0000250|UniProtKB:Q5SUA5}.
CC -!- FUNCTION: [Minor histocompatibility antigen HA-2]: Constitutes the
CC minor histocompatibility antigen HA-2. More generally, minor
CC histocompatibility antigens (mHags) refer to immunogenic peptide which,
CC when complexed with MHC, can generate an immune response after
CC recognition by specific T-cells. The peptides are derived from
CC polymorphic intracellular proteins, which are cleaved by normal
CC pathways of antigen processing. The binding of these peptides to MHC
CC class I or class II molecules and their expression on the cell surface
CC can stimulate T-cell responses and thereby trigger graft rejection or
CC graft-versus-host disease (GVHD) after hematopoietic stem cell
CC transplantation from HLA-identical sibling donor. GVHD is a frequent
CC complication after bone marrow transplantation (BMT), due to mismatch
CC of minor histocompatibility antigen in HLA-matched sibling marrow
CC transplants. HA-2 is restricted to MHC class I HLA-A*0201.
CC {ECO:0000269|PubMed:11544309, ECO:0000305}.
CC -!- SUBUNIT: Interacts with calmodulin; via its IQ motifs. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19968988,
CC ECO:0000269|PubMed:20071333}; Peripheral membrane protein
CC {ECO:0000269|PubMed:19968988, ECO:0000269|PubMed:20071333}. Cell
CC projection, phagocytic cup {ECO:0000250|UniProtKB:Q5SUA5}.
CC Note=Recruited to Fc-gamma receptor (Fc-gamma-R) phagocytic cup. In T-
CC cells, transiently accumulates in discrete areas at the plasma membrane
CC of migrating cells or when membranes are deformed (By similarity).
CC Localization at the membrane is not highly dependent on
CC phosphatidylinositol 4,5-bisphosphate levels. Released from the
CC membrane in the presence of ATP. May be enriched in peripheral
CC processes, such as microvilli or ruffles.
CC {ECO:0000250|UniProtKB:Q5SUA5, ECO:0000269|PubMed:20071333}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=B0I1T2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=B0I1T2-2; Sequence=VSP_034208, VSP_034209;
CC Name=3;
CC IsoId=B0I1T2-3; Sequence=VSP_034210;
CC Name=4;
CC IsoId=B0I1T2-4; Sequence=VSP_034211, VSP_034212;
CC -!- TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells.
CC {ECO:0000269|PubMed:11544309, ECO:0000269|PubMed:20071333}.
CC -!- DOMAIN: The myosin tail domain mediates binding to
CC phosphatidylinositol-3,4-bisphosphate (PtdIns(3,4)P2),
CC phosphatidylinositol-4,5-bisphosphate (PtdIns(4,5)P2) and
CC phosphatidylinositol-3,4,5-trisphosphate (PtdIns(3,4,5)P3) and binds to
CC membranous compartments. It is required for recruitment to Fc-gamma
CC receptor (Fc-gamma-R) phagocytic cups. {ECO:0000250|UniProtKB:Q5SUA5}.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000305}.
CC -!- CAUTION: Represents an unconventional myosin. This protein should not
CC be confused with the conventional myosin-1 (MYH1). {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84876.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR EMBL; AK074050; BAB84876.1; ALT_SEQ; mRNA.
DR EMBL; AK074135; BAB84961.1; -; mRNA.
DR EMBL; AB290179; BAG06733.1; -; mRNA.
DR EMBL; AC004847; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF380932; AAK58092.1; -; mRNA.
DR EMBL; AF380933; AAK58093.1; -; mRNA.
DR EMBL; BC015693; AAH15693.2; -; mRNA.
DR CCDS; CCDS34629.1; -. [B0I1T2-1]
DR RefSeq; NP_149043.2; NM_033054.2. [B0I1T2-1]
DR AlphaFoldDB; B0I1T2; -.
DR SMR; B0I1T2; -.
DR BioGRID; 122031; 11.
DR IntAct; B0I1T2; 10.
DR MINT; B0I1T2; -.
DR STRING; 9606.ENSP00000258787; -.
DR GlyGen; B0I1T2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; B0I1T2; -.
DR MetOSite; B0I1T2; -.
DR PhosphoSitePlus; B0I1T2; -.
DR SwissPalm; B0I1T2; -.
DR BioMuta; MYO1G; -.
DR CPTAC; CPTAC-1620; -.
DR EPD; B0I1T2; -.
DR jPOST; B0I1T2; -.
DR MassIVE; B0I1T2; -.
DR MaxQB; B0I1T2; -.
DR PaxDb; B0I1T2; -.
DR PeptideAtlas; B0I1T2; -.
DR PRIDE; B0I1T2; -.
DR ProteomicsDB; 2548; -. [B0I1T2-1]
DR ProteomicsDB; 2549; -. [B0I1T2-2]
DR ProteomicsDB; 2550; -. [B0I1T2-3]
DR ProteomicsDB; 2551; -. [B0I1T2-4]
DR Antibodypedia; 13492; 77 antibodies from 15 providers.
DR DNASU; 64005; -.
DR Ensembl; ENST00000258787.12; ENSP00000258787.7; ENSG00000136286.16. [B0I1T2-1]
DR GeneID; 64005; -.
DR KEGG; hsa:64005; -.
DR MANE-Select; ENST00000258787.12; ENSP00000258787.7; NM_033054.3; NP_149043.2.
DR UCSC; uc003tmh.3; human. [B0I1T2-1]
DR CTD; 64005; -.
DR DisGeNET; 64005; -.
DR GeneCards; MYO1G; -.
DR HGNC; HGNC:13880; MYO1G.
DR HPA; ENSG00000136286; Tissue enhanced (bone marrow, lymphoid tissue).
DR MIM; 600642; gene.
DR neXtProt; NX_B0I1T2; -.
DR OpenTargets; ENSG00000136286; -.
DR VEuPathDB; HostDB:ENSG00000136286; -.
DR eggNOG; KOG0160; Eukaryota.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000158053; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; B0I1T2; -.
DR OMA; NGIMEAR; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; B0I1T2; -.
DR TreeFam; TF312960; -.
DR PathwayCommons; B0I1T2; -.
DR SignaLink; B0I1T2; -.
DR BioGRID-ORCS; 64005; 31 hits in 1071 CRISPR screens.
DR ChiTaRS; MYO1G; human.
DR GenomeRNAi; 64005; -.
DR Pharos; B0I1T2; Tbio.
DR PRO; PR:B0I1T2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; B0I1T2; protein.
DR Bgee; ENSG00000136286; Expressed in granulocyte and 156 other tissues.
DR ExpressionAtlas; B0I1T2; baseline and differential.
DR Genevisible; B0I1T2; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0030175; C:filopodium; IEA:Ensembl.
DR GO; GO:0030027; C:lamellipodium; IEA:Ensembl.
DR GO; GO:0031256; C:leading edge membrane; IEA:Ensembl.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0001891; C:phagocytic cup; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; ISS:UniProtKB.
DR GO; GO:0043325; F:phosphatidylinositol-3,4-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; ISS:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0071976; P:cell gliding; IEA:Ensembl.
DR GO; GO:0031589; P:cell-substrate adhesion; IEA:Ensembl.
DR GO; GO:0006887; P:exocytosis; IEA:Ensembl.
DR GO; GO:0038096; P:Fc-gamma receptor signaling pathway involved in phagocytosis; ISS:UniProtKB.
DR GO; GO:0120117; P:T cell meandering migration; IEA:Ensembl.
DR GO; GO:0002456; P:T cell mediated immunity; ISS:UniProtKB.
DR GO; GO:0072678; P:T cell migration; ISS:UniProtKB.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_TH1.
DR InterPro; IPR036072; MYSc_Myo1.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Actin-binding; Adaptive immunity; Alternative splicing;
KW ATP-binding; Calmodulin-binding; Cell membrane; Cell projection;
KW Direct protein sequencing; Immunity; Lipid-binding; Membrane;
KW Motor protein; Myosin; Nucleotide-binding; Reference proteome.
FT CHAIN 1..1018
FT /note="Unconventional myosin-Ig"
FT /id="PRO_0000340316"
FT PEPTIDE 41..49
FT /note="Minor histocompatibility antigen HA-2"
FT /evidence="ECO:0000269|PubMed:7539551"
FT /id="PRO_0000340317"
FT DOMAIN 9..707
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 710..739
FT /note="IQ"
FT DOMAIN 824..1017
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 584..606
FT /note="Actin-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:25944712"
FT VAR_SEQ 207..230
FT /note="LLRGSEDKQLHELHLERNPAVYNF -> VSPEGKGRWKNGVGKGRAASWTSL
FT (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_034208"
FT VAR_SEQ 231..1018
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_034209"
FT VAR_SEQ 526..1018
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_034210"
FT VAR_SEQ 652..722
FT /note="KMTCEYTWPNHLLGSDKAAVSALLEQHGLQGDVAFGHSKLFIRSPRTLVTLE
FT QSRARLIPIIVLLLQKAWR -> WHLTPITPWAIVPVWSPRGRSRGSPNSTSQTSIQAG
FT TSTLLASRHQNIWEDMCVSTCMWGHTGGNMGMRAV (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11544309"
FT /id="VSP_034211"
FT VAR_SEQ 723..1018
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:11544309"
FT /id="VSP_034212"
FT VARIANT 49
FT /note="V -> M (in allele HA-2M; the HA-2V allele constitute
FT the HA-2 epitope while HA-2M is not recognized by HA-2
FT cytotoxic T lymphocytes; dbSNP:rs61739531)"
FT /evidence="ECO:0000269|PubMed:11544309"
FT /id="VAR_044013"
FT VARIANT 489
FT /note="M -> T (in dbSNP:rs3735485)"
FT /evidence="ECO:0000269|PubMed:11544309, ECO:0000269|Ref.1,
FT ECO:0000269|Ref.2"
FT /id="VAR_044014"
FT VARIANT 798
FT /note="R -> Q (in dbSNP:rs2107737)"
FT /id="VAR_050212"
FT VARIANT 861
FT /note="Q -> R (in dbSNP:rs7792760)"
FT /evidence="ECO:0000269|PubMed:15489334, ECO:0000269|Ref.2"
FT /id="VAR_044015"
FT MUTAGEN 815
FT /note="K->A: Reduced membrane association."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 826
FT /note="R->A: Reduced membrane association."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 876
FT /note="R->A: No effect on membrane localization."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 880
FT /note="R->A: No effect on membrane localization."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 883
FT /note="K->A: No effect on membrane localization; when
FT associated with R-885."
FT MUTAGEN 885
FT /note="R->A: No effect on membrane localization; when
FT associated with K-883."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 898
FT /note="K->A: Reduced membrane association."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 903
FT /note="R->A: No effect on membrane localization; when
FT associated with R-906."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 906
FT /note="R->A: No effect on membrane localization; when
FT associated with R-903."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 909
FT /note="R->A: No effect on membrane localization."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 934
FT /note="R->A: No effect on membrane localization."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 945
FT /note="R->A: No effect on membrane localization."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 947
FT /note="R->A: No effect on membrane localization."
FT /evidence="ECO:0000269|PubMed:20071333"
FT MUTAGEN 953
FT /note="R->A: No effect on membrane localization."
FT /evidence="ECO:0000269|PubMed:20071333"
FT CONFLICT 369
FT /note="N -> K (in Ref. 1; BAB84961)"
FT /evidence="ECO:0000305"
FT CONFLICT 377
FT /note="P -> L (in Ref. 4; AAK58092/AAK58093)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1018 AA; 116442 MW; 3EB4ACC3D99A86E9 CRC64;
MEDEEGPEYG KPDFVLLDQV TMEDFMRNLQ LRFEKGRIYT YIGEVLVSVN PYQELPLYGP
EAIARYQGRE LYERPPHLYA VANAAYKAMK HRSRDTCIVI SGESGAGKTE ASKHIMQYIA
AVTNPSQRAE VERVKDVLLK STCVLEAFGN ARTNRNHNSS RFGKYMDINF DFKGDPIGGH
IHSYLLEKSR VLKQHVGERN FHAFYQLLRG SEDKQLHELH LERNPAVYNF THQGAGLNMT
VHSALDSDEQ SHQAVTEAMR VIGFSPEEVE SVHRILAAIL HLGNIEFVET EEGGLQKEGL
AVAEEALVDH VAELTATPRD LVLRSLLART VASGGRELIE KGHTAAEASY ARDACAKAVY
QRLFEWVVNR INSVMEPRGR DPRRDGKDTV IGVLDIYGFE VFPVNSFEQF CINYCNEKLQ
QLFIQLILKQ EQEEYEREGI TWQSVEYFNN ATIVDLVERP HRGILAVLDE ACSSAGTITD
RIFLQTLDMH HRHHLHYTSR QLCPTDKTME FGRDFRIKHY AGDVTYSVEG FIDKNRDFLF
QDFKRLLYNS TDPTLRAMWP DGQQDITEVT KRPLTAGTLF KNSMVALVEN LASKEPFYVR
CIKPNEDKVA GKLDENHCRH QVAYLGLLEN VRVRRAGFAS RQPYSRFLLR YKMTCEYTWP
NHLLGSDKAA VSALLEQHGL QGDVAFGHSK LFIRSPRTLV TLEQSRARLI PIIVLLLQKA
WRGTLARWRC RRLRAIYTIM RWFRRHKVRA HLAELQRRFQ AARQPPLYGR DLVWPLPPAV
LQPFQDTCHA LFCRWRARQL VKNIPPSDMP QIKAKVAAMG ALQGLRQDWG CRRAWARDYL
SSATDNPTAS SLFAQRLKTL QDKDGFGAVL FSSHVRKVNR FHKIRNRALL LTDQHLYKLD
PDRQYRVMRA VPLEAVTGLS VTSGGDQLVV LHARGQDDLV VCLHRSRPPL DNRVGELVGV
LAAHCQGEGR TLEVRVSDCI PLSHRGVRRL ISVEPRPEQP EPDFRCARGS FTLLWPSR
