RBCC

MYO1G (HA2) [Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Unconventional myosin-Ig; Minor histocompatibility antigen HA-2; mHag HA-2

UniProt B0I1T2
ID MYO1G_HUMAN Reviewed; 1018 AA.
AC B0I1T2; Q8TEI9; Q8TES2; Q96BE2; Q96RI5; Q96RI6;
DT 10-JUN-2008, integrated into UniProtKB/Swiss-Prot.
read moreDT 11-JAN-2011, sequence version 2.
DT 22-JAN-2014, entry version 51.
DE RecName: Full=Unconventional myosin-Ig;
DE Contains:
DE RecName: Full=Minor histocompatibility antigen HA-2;
DE Short=mHag HA-2;
GN Name=MYO1G; Synonyms=HA2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 193-1018 (ISOFORM 3), AND VARIANT
RP 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
RT spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS
RP THR-489 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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
RP THE MINOR HISTOCOMPATIBILITY ANTIGEN HA-2, VARIANTS HA-2M MET-49 AND
RP THR-489, CHARACTERIZATION OF VARIANT HA-2M MET-49, AND TISSUE
RP SPECIFICITY.
RX PubMed=11544309;
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
RT gene 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
RP VARIANT 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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
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;
RP ARG-909; 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.,
RA Shaw S.;
RT "Myosin 1G is an abundant class I myosin in lymphocytes whose
RT localization at the plasma membrane depends on its ancient divergent
RT pleckstrin homology (PH) domain (Myo1PH).";
RL J. Biol. Chem. 285:8675-8686(2010).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase
CC activity. Unconventional myosins serve in intracellular movements.
CC Their highly divergent tails are presumed to bind to membranous
CC compartments, which would be moved relative to actin filaments (By
CC similarity).
CC -!- FUNCTION: Precursor of the minor histocompatibility antigen HA-2.
CC More generally, minor histocompatibility antigens (mHags) refer to
CC immunogenic peptide which, when complexed with MHC, can generate
CC an immune response after recognition by specific T-cells. The
CC peptides are derived from polymorphic intracellular proteins,
CC which are cleaved by normal pathways of antigen processing. The
CC binding of these peptides to MHC class I or class II molecules and
CC their expression on the cell surface can stimulate T-cell
CC responses and thereby trigger graft rejection or graft-versus-host
CC disease (GVHD) after hematopoietic stem cell transplantation from
CC HLA-identical sibling donor. GVHD is a frequent complication after
CC bone marrow transplantation (BMT), due to mismatch of minor
CC histocompatibility antigen in HLA-matched sibling marrow
CC transplants. HA-2 is restricted to MHC class I HLA-A*0201.
CC -!- SUBUNIT: Binds calmodulin through its IQ motifs (By similarity).
CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein.
CC Note=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 -!- 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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=B0I1T2-3; Sequence=VSP_034210;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=B0I1T2-4; Sequence=VSP_034211, VSP_034212;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Specifically expressed in hematopoietic cells.
CC -!- SIMILARITY: Contains 1 IQ domain.
CC -!- SIMILARITY: Contains 1 myosin head-like domain.
CC -!- CAUTION: Represents a unconventional myosin. This protein should
CC not be confused with the conventional myosin-1 (MYH1).
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB84876.1; Type=Erroneous translation; Note=Wrong choice of CDS;
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
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 RefSeq; NP_149043.2; NM_033054.2.
DR UniGene; Hs.37617; -.
DR ProteinModelPortal; B0I1T2; -.
DR SMR; B0I1T2; 7-733.
DR IntAct; B0I1T2; 4.
DR MINT; MINT-7307233; -.
DR STRING; 9606.ENSP00000258787; -.
DR PhosphoSite; B0I1T2; -.
DR PaxDb; B0I1T2; -.
DR PRIDE; B0I1T2; -.
DR Ensembl; ENST00000258787; ENSP00000258787; ENSG00000136286.
DR GeneID; 64005; -.
DR KEGG; hsa:64005; -.
DR UCSC; uc003tmg.2; human.
DR CTD; 64005; -.
DR GeneCards; GC07M045003; -.
DR H-InvDB; HIX0006659; -.
DR HGNC; HGNC:13880; MYO1G.
DR HPA; HPA021252; -.
DR MIM; 613445; gene.
DR neXtProt; NX_B0I1T2; -.
DR eggNOG; COG5022; -.
DR HOGENOM; HOG000260264; -.
DR HOVERGEN; HBG062373; -.
DR InParanoid; B0I1T2; -.
DR KO; K10356; -.
DR OMA; EQHGLQG; -.
DR OrthoDB; EOG7V49XQ; -.
DR GenomeRNAi; 64005; -.
DR NextBio; 65808; -.
DR PRO; PR:B0I1T2; -.
DR ArrayExpress; B0I1T2; -.
DR Bgee; B0I1T2; -.
DR CleanEx; HS_MYO1G; -.
DR Genevestigator; B0I1T2; -.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003774; F:motor activity; IEA:InterPro.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR010926; Myosin_tail_2.
DR InterPro; IPR027417; P-loop_NTPase.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 1.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; FALSE_NEG.
PE 1: Evidence at protein level;
KW Actin-binding; Alternative splicing; ATP-binding; Calmodulin-binding;
KW Cell membrane; Complete proteome; Direct protein sequencing; Membrane;
KW Motor protein; Myosin; Nucleotide-binding; Polymorphism;
KW Reference proteome.
FT CHAIN 1 1018 Unconventional myosin-Ig.
FT /FTId=PRO_0000340316.
FT PEPTIDE 41 49 Minor histocompatibility antigen HA-2.
FT /FTId=PRO_0000340317.
FT DOMAIN 13 683 Myosin head-like.
FT DOMAIN 710 739 IQ.
FT NP_BIND 102 109 ATP (By similarity).
FT VAR_SEQ 207 230 LLRGSEDKQLHELHLERNPAVYNF -> VSPEGKGRWKNGV
FT GKGRAASWTSL (in isoform 2).
FT /FTId=VSP_034208.
FT VAR_SEQ 231 1018 Missing (in isoform 2).
FT /FTId=VSP_034209.
FT VAR_SEQ 526 1018 Missing (in isoform 3).
FT /FTId=VSP_034210.
FT VAR_SEQ 652 722 KMTCEYTWPNHLLGSDKAAVSALLEQHGLQGDVAFGHSKLF
FT IRSPRTLVTLEQSRARLIPIIVLLLQKAWR -> WHLTPIT
FT PWAIVPVWSPRGRSRGSPNSTSQTSIQAGTSTLLASRHQNI
FT WEDMCVSTCMWGHTGGNMGMRAV (in isoform 4).
FT /FTId=VSP_034211.
FT VAR_SEQ 723 1018 Missing (in isoform 4).
FT /FTId=VSP_034212.
FT VARIANT 49 49 V -> M (in allele HA-2M; the HA-2V allele
FT constitute the HA-2 epitope while HA-2M
FT is not recognized by HA-2 cytotoxic T
FT lymphocytes; dbSNP:rs61739531).
FT /FTId=VAR_044013.
FT VARIANT 489 489 M -> T (in dbSNP:rs3735485).
FT /FTId=VAR_044014.
FT VARIANT 798 798 R -> Q (in dbSNP:rs2107737).
FT /FTId=VAR_050212.
FT VARIANT 861 861 Q -> R (in dbSNP:rs7792760).
FT /FTId=VAR_044015.
FT MUTAGEN 815 815 K->A: Reduced membrane association.
FT MUTAGEN 826 826 R->A: Reduced membrane association.
FT MUTAGEN 876 876 R->A: No effect on membrane localization.
FT MUTAGEN 880 880 R->A: No effect on membrane localization.
FT MUTAGEN 883 883 K->A: No effect on membrane localization;
FT when associated with R-885.
FT MUTAGEN 885 885 R->A: No effect on membrane localization;
FT when associated with K-883.
FT MUTAGEN 898 898 K->A: Reduced membrane association.
FT MUTAGEN 903 903 R->A: No effect on membrane localization;
FT when associated with R-906.
FT MUTAGEN 906 906 R->A: No effect on membrane localization;
FT when associated with R-903.
FT MUTAGEN 909 909 R->A: No effect on membrane localization.
FT MUTAGEN 934 934 R->A: No effect on membrane localization.
FT MUTAGEN 945 945 R->A: No effect on membrane localization.
FT MUTAGEN 947 947 R->A: No effect on membrane localization.
FT MUTAGEN 953 953 R->A: No effect on membrane localization.
FT CONFLICT 369 369 N -> K (in Ref. 1; BAB84961).
FT CONFLICT 377 377 P -> L (in Ref. 4; AAK58092/AAK58093).
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
//

MIM 613445
*RECORD*
*FIELD* NO
613445
*FIELD* TI
*613445 MYOSIN IG; MYO1G
;;HA2 GENE; HA2
*FIELD* TX

DESCRIPTION

MYO1G is a plasma membrane-associated class I myosin (see 601478) that
read moreis abundant in T and B lymphocytes and mast cells (Pierce et al., 2001;
Patino-Lopez et al., 2010).

CLONING

By searching databases using the minor histocompatibility antigen HA2
nonapeptide as probe, followed by RT-PCR of mRNA from HA2-positive cell
lines, Pierce et al. (2001) cloned human MYO1G. The deduced 633-amino
acid protein is a class I myosin. RT-PCR analysis revealed 2 allelic
forms of MYO1G, one in which the HA2 epitope ends with val (HA2V), and
one in which the HA2 epitope ends with met (HA2M). RT-PCR showed that
high MYO1G expression was restricted to hematopoietic cells.

GENE FUNCTION

Pierce et al. (2001) found that recognition by cytotoxic lymphocytes was
similar for both H2AM and H2AV. However, binding of H2AM to HLA-A*0201
(see 142800) was much less than that of H2AV, and H2AM was not presented
on the cell surface by cells expressing the peptide endogenously.

By Western blot, immunofluorescence microscopy, and mutation analyses,
Patino-Lopez et al. (2010) demonstrated that membrane localization of
MYO1G required its divergent pleckstrin homology domain.

GENE STRUCTURE

Pierce et al. (2001) determined that the MYO1G gene contains 14 exons.

MAPPING

Using FISH, Pierce et al. (2001) mapped the MYO1G gene to chromosome
7p13-p12.

*FIELD* RF
1. Patino-Lopez, G.; Aravind, L.; Dong, X.; Kruhlak, M. J.; Ostap,
E. M.; Shaw, S.: Myosin 1G is an abundant class I myosin in lymphocytes
whose localization at the plasma membrane depends on its ancient divergent
pleckstrin homology (PH) domain (Myo1PH). J. Biol. Chem. 285: 8675-8686,
2010.

2. Pierce, R. A.; Field, E. D.; Mutis, T.; Golovina, T. N.; Von Kap-Herr,
C.; Wilke, M.; Pool, J.; Shabanowitz, J.; Pettenati, M. J.; Eisenlohr,
L. C.; Hunt, D. F.; Goulmy, E.; Engelhard, V. H.: The HA-2 minor
histocompatibility antigen is derived from a diallelic gene encoding
a novel human class I myosin protein. J. Immun. 167: 3223-3230,
2001.

*FIELD* CD
Paul J. Converse: 6/15/2010

*FIELD* ED
mgross: 06/15/2010

RBCC Red Blood Cell Collection

Full text data of MYO1G