MYO1F_HUMAN
ID MYO1F_HUMAN Reviewed; 1098 AA.
AC O00160; Q8WWN7;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 200.
DE RecName: Full=Unconventional myosin-If;
DE AltName: Full=Myosin-Ie;
GN Name=MYO1F;
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 [MRNA].
RX PubMed=11804589; DOI=10.1016/s1097-2765(02)00434-3;
RA Krugmann S., Anderson K.E., Ridley S.H., Risso N., McGregor A.,
RA Coadwell J., Davidson K., Eguinoa A., Ellson C.D., Lipp P., Manifava M.,
RA Ktistakis N., Painter G., Thuring J.W., Cooper M.A., Lim Z.-Y.,
RA Holmes A.B., Dove S.K., Michell R.H., Grewal A., Nazarian A.,
RA Erdjument-Bromage H., Tempst P., Stephens L.R., Hawkins P.T.;
RT "Identification of ARAP3, a novel PI3K effector regulating both Arf and Rho
RT GTPases, by selective capture on phosphoinositide affinity matrices.";
RL Mol. Cell 9:95-108(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Blood;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 318-1098.
RC TISSUE=Retina;
RX PubMed=9119401; DOI=10.1006/geno.1996.4526;
RA Crozet F., El-Amraoui A., Blanchard S., Lenoir M., Ripoll C., Vago P.,
RA Hamel C., Fizames C., Levi-Acobas F., Depetris D., Mattei M.-G., Weil D.,
RA Pujol R., Petit C.;
RT "Cloning of the genes encoding two murine and human cochlear unconventional
RT type I myosins.";
RL Genomics 40:332-341(1997).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1023, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=T-cell;
RX PubMed=19367720; DOI=10.1021/pr800500r;
RA Carrascal M., Ovelleiro D., Casas V., Gay M., Abian J.;
RT "Phosphorylation analysis of primary human T lymphocytes using sequential
RT IMAC and titanium oxide enrichment.";
RL J. Proteome Res. 7:5167-5176(2008).
RN [7]
RP VARIANT VAL-502.
RX PubMed=22938506; DOI=10.1186/1750-1172-7-60;
RA Baek J.I., Oh S.K., Kim D.B., Choi S.Y., Kim U.K., Lee K.Y., Lee S.H.;
RT "Targeted massive parallel sequencing: the effective detection of novel
RT causative mutations associated with hearing loss in small families.";
RL Orphanet J. Rare Dis. 7:60-60(2012).
CC -!- FUNCTION: Myosins are actin-based motor molecules with ATPase activity.
CC Unconventional myosins serve in intracellular movements. Their highly
CC divergent tails are presumed to bind to membranous compartments, which
CC would be moved relative to actin filaments (By similarity).
CC {ECO:0000250}.
CC -!- INTERACTION:
CC O00160; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-741792, EBI-745689;
CC O00160; Q9BWG6: SCNM1; NbExp=3; IntAct=EBI-741792, EBI-748391;
CC O00160; P78314-3: SH3BP2; NbExp=3; IntAct=EBI-741792, EBI-12304031;
CC -!- DISEASE: Note=Defects in MYO1F has been found in a patient with a form
CC of non-syndromic sensorineural hearing loss.
CC {ECO:0000269|PubMed:22938506}.
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}.
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DR EMBL; AJ310570; CAC83948.1; -; mRNA.
DR EMBL; AK092877; BAC03995.1; -; mRNA.
DR EMBL; AC092298; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC092316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124902; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC130469; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028071; AAH28071.1; -; mRNA.
DR EMBL; X98411; CAA67058.1; -; mRNA.
DR CCDS; CCDS42494.1; -.
DR RefSeq; NP_036467.2; NM_012335.3.
DR AlphaFoldDB; O00160; -.
DR SMR; O00160; -.
DR BioGRID; 110638; 45.
DR IntAct; O00160; 16.
DR STRING; 9606.ENSP00000344871; -.
DR iPTMnet; O00160; -.
DR PhosphoSitePlus; O00160; -.
DR BioMuta; MYO1F; -.
DR EPD; O00160; -.
DR jPOST; O00160; -.
DR MassIVE; O00160; -.
DR MaxQB; O00160; -.
DR PaxDb; O00160; -.
DR PeptideAtlas; O00160; -.
DR PRIDE; O00160; -.
DR ProteomicsDB; 47747; -.
DR Antibodypedia; 53112; 65 antibodies from 19 providers.
DR DNASU; 4542; -.
DR Ensembl; ENST00000613525.4; ENSP00000481682.1; ENSG00000142347.19.
DR Ensembl; ENST00000644032.2; ENSP00000494550.1; ENSG00000142347.19.
DR GeneID; 4542; -.
DR KEGG; hsa:4542; -.
DR MANE-Select; ENST00000644032.2; ENSP00000494550.1; NM_012335.4; NP_036467.2.
DR UCSC; uc002mkg.4; human.
DR CTD; 4542; -.
DR DisGeNET; 4542; -.
DR GeneCards; MYO1F; -.
DR HGNC; HGNC:7600; MYO1F.
DR HPA; ENSG00000142347; Group enriched (bone marrow, lung, lymphoid tissue).
DR MIM; 601480; gene.
DR neXtProt; NX_O00160; -.
DR OpenTargets; ENSG00000142347; -.
DR PharmGKB; PA31402; -.
DR VEuPathDB; HostDB:ENSG00000142347; -.
DR eggNOG; KOG0162; Eukaryota.
DR GeneTree; ENSGT00940000158870; -.
DR HOGENOM; CLU_000192_7_6_1; -.
DR InParanoid; O00160; -.
DR OMA; NGWWLCK; -.
DR OrthoDB; 122881at2759; -.
DR PhylomeDB; O00160; -.
DR TreeFam; TF312960; -.
DR PathwayCommons; O00160; -.
DR SignaLink; O00160; -.
DR BioGRID-ORCS; 4542; 29 hits in 1069 CRISPR screens.
DR ChiTaRS; MYO1F; human.
DR GeneWiki; MYO1F; -.
DR GenomeRNAi; 4542; -.
DR Pharos; O00160; Tbio.
DR PRO; PR:O00160; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O00160; protein.
DR Bgee; ENSG00000142347; Expressed in granulocyte and 159 other tissues.
DR ExpressionAtlas; O00160; baseline and differential.
DR Genevisible; O00160; HS.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016461; C:unconventional myosin complex; NAS:UniProtKB.
DR GO; GO:0003779; F:actin binding; NAS:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; NAS:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IEA:UniProtKB-KW.
DR GO; GO:0000146; F:microfilament motor activity; IBA:GO_Central.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0030050; P:vesicle transport along actin filament; IBA:GO_Central.
DR CDD; cd01378; MYSc_Myo1; 1.
DR CDD; cd11827; SH3_MyoIe_If_like; 1.
DR Gene3D; 3.40.850.10; -; 1.
DR InterPro; IPR035507; Ie/If_SH3.
DR InterPro; IPR000048; IQ_motif_EF-hand-BS.
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 InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00242; MYSc; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS50096; IQ; 1.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS50002; SH3; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW Actin-binding; ATP-binding; Calmodulin-binding; Deafness; Disease variant;
KW Motor protein; Myosin; Non-syndromic deafness; Nucleotide-binding;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..1098
FT /note="Unconventional myosin-If"
FT /id="PRO_0000123452"
FT DOMAIN 17..690
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 693..722
FT /note="IQ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 728..917
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT DOMAIN 1041..1098
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 579..589
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT REGION 913..1009
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1021..1044
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 110..117
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1023
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19367720"
FT VARIANT 502
FT /note="I -> V (probable disease-associated variant found in
FT a patient with non-syndromic sensorineural hearing loss;
FT dbSNP:rs200797032)"
FT /evidence="ECO:0000269|PubMed:22938506"
FT /id="VAR_079873"
FT VARIANT 960
FT /note="P -> L (in dbSNP:rs2288411)"
FT /id="VAR_056179"
FT CONFLICT 259
FT /note="A -> V (in Ref. 2; BAC03995)"
FT /evidence="ECO:0000305"
FT CONFLICT 534..536
FT /note="TSE -> SSD (in Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 592..593
FT /note="RP -> HA (in Ref. 1; CAC83948 and 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 602
FT /note="K -> Q (in Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 759
FT /note="R -> K (in Ref. 1; CAC83948 and 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 797
FT /note="V -> M (in Ref. 1; CAC83948 and 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="Q -> P (in Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 809
FT /note="V -> I (in Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 814
FT /note="V -> L (in Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 922
FT /note="S -> N (in Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 927
FT /note="R -> G (in Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 930
FT /note="M -> L (in Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 948..951
FT /note="APPR -> GAPQ (in Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 958..967
FT /note="VPPSARGGPL -> APLCPQGGAPC (in Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 971..990
FT /note="IMSGGGTHRPPRGPPSTSLG -> KFIWPRGHPQASPALRPHPWD (in
FT Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 1031
FT /note="Missing (in Ref. 5; CAA67058)"
FT /evidence="ECO:0000305"
FT CONFLICT 1090..1098
FT /note="FPGNYVEKI -> GSPSARSPA (in Ref. 2; BAC03995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1098 AA; 124844 MW; 75C2B1306F74C7C5 CRC64;
MGSKERFHWQ SHNVKQSGVD DMVLLPQITE DAIAANLRKR FMDDYIFTYI GSVLISVNPF
KQMPYFTDRE IDLYQGAAQY ENPPHIYALT DNMYRNMLID CENQCVIISG ESGAGKTVAA
KYIMGYISKV SGGGEKVQHV KDIILQSNPL LEAFGNAKTV RNNNSSRFGK YFEIQFSRGG
EPDGGKISNF LLEKSRVVMQ NENERNFHIY YQLLEGASQE QRQNLGLMTP DYYYYLNQSD
TYQVDGTDDR SDFGETLSAM QVIGIPPSIQ QLVLQLVAGI LHLGNISFCE DGNYARVESV
DLLAFPAYLL GIDSGRLQEK LTSRKMDSRW GGRSESINVT LNVEQAAYTR DALAKGLYAR
LFDFLVEAIN RAMQKPQEEY SIGVLDIYGF EIFQKNGFEQ FCINFVNEKL QQIFIELTLK
AEQEEYVQEG IRWTPIQYFN NKVVCDLIEN KLSPPGIMSV LDDVCATMHA TGGGADQTLL
QKLQAAVGTH EHFNSWSAGF VIHHYAGKVS YDVSGFCERN RDVLFSDLIE LMQTSEQAFL
RMLFPEKLDG DKKGRPSTAG SKIKKQANDL VATLMRCTPH YIRCIKPNET KRPRDWEENR
VKHQVEYLGL KENIRVRRAG FAYRRQFAKF LQRYAILTPE TWPRWRGDER QGVQHLLRAV
NMEPDQYQMG STKVFVKNPE SLFLLEEVRE RKFDGFARTI QKAWRRHVAV RKYEEMREEA
SNILLNKKER RRNSINRNFV GDYLGLEERP ELRQFLGKRE RVDFADSVTK YDRRFKPIKR
DLILTPKCVY VIGREKVKKG PEKGQVCEVL KKKVDIQALR GVSLSTRQDD FFILQEDAAD
SFLESVFKTE FVSLLCKRFE EATRRPLPLT FSDTLQFRVK KEGWGGGGTR SVTFSRGFGD
LAVLKVGGRT LTVSVGDGLP KSSKPTRKGM AKGKPRRSSQ APTRAAPAPP RGMDRNGVPP
SARGGPLPLE IMSGGGTHRP PRGPPSTSLG ASRRPRARPP SEHNTEFLNV PDQGMAGMQR
KRSVGQRPVP GVGRPKPQPR THGPRCRALY QYVGQDVDEL SFNVNEVIEI LMEDPSGWWK
GRLHGQEGLF PGNYVEKI
