ID H3BMM1_HUMAN Unreviewed; 1301 AA.
AC H3BMM1;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Myosin IXA {ECO:0000313|Ensembl:ENSP00000454446.1};
GN Name=MYO9A {ECO:0000313|Ensembl:ENSP00000454446.1};
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 {ECO:0000313|Ensembl:ENSP00000454446.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000454446.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M., Stewart S.,
RA Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R.,
RA Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [2] {ECO:0007829|PubMed:21269460}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [3] {ECO:0007829|PubMed:23186163}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=23186163;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [4] {ECO:0000313|Ensembl:ENSP00000454446.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SIMILARITY: Belongs to the TRAFAC class myosin-kinesin ATPase
CC superfamily. Myosin family. {ECO:0000256|PROSITE-ProRule:PRU00782}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00782}.
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DR EMBL; AC020779; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022872; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC090454; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104938; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR MassIVE; H3BMM1; -.
DR MaxQB; H3BMM1; -.
DR PeptideAtlas; H3BMM1; -.
DR ProteomicsDB; 40947; -.
DR Antibodypedia; 26536; 42 antibodies from 14 providers.
DR Ensembl; ENST00000566885.5; ENSP00000454446.1; ENSG00000066933.17.
DR UCSC; uc010biq.5; human.
DR HGNC; HGNC:7608; MYO9A.
DR VEuPathDB; HostDB:ENSG00000066933; -.
DR GeneTree; ENSGT00940000154905; -.
DR HOGENOM; CLU_006326_0_0_1; -.
DR ChiTaRS; MYO9A; human.
DR Proteomes; UP000005640; Chromosome 15.
DR Bgee; ENSG00000066933; Expressed in calcaneal tendon and 211 other cell types or tissues.
DR ExpressionAtlas; H3BMM1; baseline and differential.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0005096; F:GTPase activator activity; IEA:InterPro.
DR GO; GO:0000146; F:microfilament motor activity; IEA:InterPro.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR Gene3D; 1.20.5.190; -; 3.
DR Gene3D; 1.20.58.530; -; 1.
DR Gene3D; 6.20.240.20; -; 1.
DR Gene3D; 3.40.850.10; Kinesin motor domain; 1.
DR Gene3D; 1.20.120.720; Myosin VI head, motor domain, U50 subdomain; 1.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
DR InterPro; IPR036961; Kinesin_motor_dom_sf.
DR InterPro; IPR046987; Myo9.
DR InterPro; IPR001609; Myosin_head_motor_dom.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR46184:SF3; UNCONVENTIONAL MYOSIN-IXA; 1.
DR PANTHER; PTHR46184; UNCONVENTIONAL MYOSIN-IXB-LIKE PROTEIN; 1.
DR Pfam; PF00612; IQ; 4.
DR Pfam; PF00063; Myosin_head; 2.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 5.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS50096; IQ; 4.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
PE 1: Evidence at protein level;
KW Actin-binding {ECO:0000256|PROSITE-ProRule:PRU00782};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Motor protein {ECO:0000256|ARBA:ARBA00023175};
KW Myosin {ECO:0000256|ARBA:ARBA00023123, ECO:0000256|PROSITE-
KW ProRule:PRU00782}; Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Proteomics identification {ECO:0007829|EPD:H3BMM1,
KW ECO:0007829|MaxQB:H3BMM1};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640}.
FT DOMAIN 1..636
FT /note="Myosin motor"
FT /evidence="ECO:0000259|PROSITE:PS51456"
FT REGION 518..540
FT /note="Actin-binding"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00782"
FT REGION 843..870
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 919..1006
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1291
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1107..1146
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 939..962
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 976..1004
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1301 AA; 150169 MW; 57F3098B717822B6 CRC64;
MEMVGFLPKT RRQIFSLLSA ILHLGNICYK KKTYRDDSID ICNPEVLPIV SELLEVKEEM
LFEALVTRKT VTVGEKLILP YKLAEAVTVR NSMAKSLYSA LFDWIVFRIN HALLNSKDLE
HNTKTLSIGV LDIFGFEDYE NNSFEQFCIN FANERLQHYF NQHIFKLEQE EYRTEGISWH
NIDYIDNTCC INLISKKPTG LLHLLDEESN FPQATNQTLL DKFKHQHEDN SYIEFPAVME
PAFIIKHYAG KVKYGVKDFR EKNTDHMRPD IVALLRSSKN AFISGMIGID PVAVFRWAIL
RAFFRAMVAF REAGKRNIHR KTGHDDTAPC AILKSMDSFS FLQHPVHQRS LEILQRCKEE
KYSKATNPDK LLSHIHLEME TRSILHQGIT RKNPRTPLSD LQGMNALNEK NQHDTFDIAW
NGRTGIRQSR LSSGTSLLDK DGIFANSTSS KLLERAHGIL TRNKNFKSKP ALPKHLLEVN
SLKHLTRLTL QDRITKSLLH LHKKKKPPSI SAQFQASLSK LMETLGQAEP YFVKCIRSNA
EKLPLRFSDV LVLRQLRYTG MLETVRIRQS GYSSKYSFQD FVSHFHVLLP RNIIPSKFNI
QDFFRKINLN PDNYQVGKTM VFLKEQERQH LQDLLHQEVL RRIILLQRWF RVLLCRQHFL
HLRQASVIIQ RFWRNYLNQK QVRDAAVQKD AFVMASAAAL LQASWRAHLE RQRYLELRAA
AIVIQQKWRD YYRRRHMAAI CIQARWKAYR ESKRYQEQRK KIILLQSTCR GFRARQRFKA
LKEQRLRETK PEVGLVNIKG YGSLEIQGSD PSGWEDCSFD NRIKAIEECK SVIESNRISR
ESSVDCLKES PNKQQERAQS QSGVDLQEDV LVRERPRSLE DLHQKKVGRA KRESRRMREL
EQAIFSLELL KVRSLGGISP SEDRRWSTEL VPEGLQSPRG TPDSESSQGS LELLSYEESQ
KSKLESVISD EGDLQFPSPK ISSSPKFDSR DNALSASNET SSAEHLKDGT MKEMVVCSSE
SITCKPQLKD SFISNSLPTF FYIPQQDPLK TNSQLDTSIQ RNKLLENEDT AGEALTLDIN
RETRRYHCSG KDQIVPSLNT ESSNPVLKKL EKLNTEKEER QKQLQQQNEK EMMEQIRQQT
DILEKERKAF KTIEKPRIGE CLVAPSSYQS KQRVERPSSL LSLNTSNKGE LNVLGSLSLK
DAALAQKDSS SAHLPPKDRP VTVFFERKGS PCQSSTVKEL SKTDRMGTQL NVACKLSNNR
ISKREHFRPT QSYSHNSDDL SREGNARPIF FTPKDNMSIP L
//
