MYO1B_RAT
ID MYO1B_RAT Reviewed; 1136 AA.
AC Q05096;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 170.
DE RecName: Full=Unconventional myosin-Ib;
DE AltName: Full=Myosin I alpha;
DE Short=MMI-alpha;
DE Short=MMIa;
DE AltName: Full=Myosin heavy chain myr 1;
GN Name=Myo1b; Synonyms=Myo1a, Myr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS A; B AND C).
RC STRAIN=Sprague-Dawley;
RX PubMed=8449985; DOI=10.1083/jcb.120.6.1393;
RA Ruppert C., Kroschewski R., Baehler M.;
RT "Identification, characterization and cloning of myr 1, a mammalian myosin-
RT I.";
RL J. Cell Biol. 120:1393-1403(1993).
CC -!- FUNCTION: Motor protein that may participate in process critical to
CC neuronal development and function such as cell migration, neurite
CC outgrowth and vesicular transport. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=A;
CC IsoId=Q05096-1; Sequence=Displayed;
CC Name=B;
CC IsoId=Q05096-2; Sequence=VSP_003348;
CC Name=C;
CC IsoId=Q05096-3; Sequence=VSP_003349;
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; X68199; CAA48287.1; -; mRNA.
DR PIR; A45439; A45439.
DR PIR; C45439; C45439.
DR RefSeq; NP_446438.1; NM_053986.1. [Q05096-1]
DR PDB; 4L79; X-ray; 2.30 A; A=1-728.
DR PDB; 5V7X; X-ray; 3.14 A; A=1-728.
DR PDB; 6C1D; EM; 3.20 A; P=6-728.
DR PDB; 6C1G; EM; 3.80 A; P=6-728.
DR PDB; 6C1H; EM; 3.90 A; P=6-728.
DR PDBsum; 4L79; -.
DR PDBsum; 5V7X; -.
DR PDBsum; 6C1D; -.
DR PDBsum; 6C1G; -.
DR PDBsum; 6C1H; -.
DR AlphaFoldDB; Q05096; -.
DR SMR; Q05096; -.
DR BioGRID; 250654; 1.
DR STRING; 10116.ENSRNOP00000059455; -.
DR BindingDB; Q05096; -.
DR ChEMBL; CHEMBL4295803; -.
DR iPTMnet; Q05096; -.
DR PhosphoSitePlus; Q05096; -.
DR PaxDb; Q05096; -.
DR PeptideAtlas; Q05096; -.
DR PRIDE; Q05096; -.
DR Ensembl; ENSRNOT00000068433; ENSRNOP00000061523; ENSRNOG00000048152. [Q05096-1]
DR GeneID; 117057; -.
DR KEGG; rno:117057; -.
DR UCSC; RGD:70994; rat. [Q05096-1]
DR CTD; 4430; -.
DR RGD; 70994; Myo1b.
DR eggNOG; KOG0164; Eukaryota.
DR GeneTree; ENSGT00940000155752; -.
DR HOGENOM; CLU_000192_7_7_1; -.
DR InParanoid; Q05096; -.
DR OMA; PLYGNEY; -.
DR OrthoDB; 122881at2759; -.
DR PRO; PR:Q05096; -.
DR Proteomes; UP000002494; Chromosome 9.
DR Bgee; ENSRNOG00000048152; Expressed in lung and 19 other tissues.
DR Genevisible; Q05096; RN.
DR GO; GO:0015629; C:actin cytoskeleton; IBA:GO_Central.
DR GO; GO:0005884; C:actin filament; ISO:RGD.
DR GO; GO:0045177; C:apical part of cell; IDA:RGD.
DR GO; GO:0005903; C:brush border; IDA:RGD.
DR GO; GO:0071944; C:cell periphery; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005769; C:early endosome; ISO:RGD.
DR GO; GO:0010008; C:endosome membrane; ISO:RGD.
DR GO; GO:0030175; C:filopodium; IDA:UniProtKB.
DR GO; GO:0005902; C:microvillus; IBA:GO_Central.
DR GO; GO:0016459; C:myosin complex; IEA:UniProtKB-KW.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0032588; C:trans-Golgi network membrane; IEA:Ensembl.
DR GO; GO:0003779; F:actin binding; IDA:UniProtKB.
DR GO; GO:0051015; F:actin filament binding; IDA:RGD.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0005516; F:calmodulin binding; IDA:UniProtKB.
DR GO; GO:0003774; F:cytoskeletal motor activity; IDA:UniProtKB.
DR GO; GO:0000146; F:microfilament motor activity; IDA:UniProtKB.
DR GO; GO:0005547; F:phosphatidylinositol-3,4,5-trisphosphate binding; IDA:UniProtKB.
DR GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IDA:UniProtKB.
DR GO; GO:0051017; P:actin filament bundle assembly; IDA:UniProtKB.
DR GO; GO:0007015; P:actin filament organization; ISO:RGD.
DR GO; GO:0030048; P:actin filament-based movement; IDA:UniProtKB.
DR GO; GO:0007399; P:nervous system development; NAS:RGD.
DR GO; GO:0006892; P:post-Golgi vesicle-mediated transport; ISO:RGD.
DR GO; GO:0033572; P:transferrin transport; ISO:RGD.
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; 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 Pfam; PF00612; IQ; 2.
DR Pfam; PF00063; Myosin_head; 1.
DR Pfam; PF06017; Myosin_TH1; 1.
DR PRINTS; PR00193; MYOSINHEAVY.
DR SMART; SM00015; IQ; 6.
DR SMART; SM00242; MYSc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS50096; IQ; 5.
DR PROSITE; PS51456; MYOSIN_MOTOR; 1.
DR PROSITE; PS51757; TH1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Actin-binding; Alternative splicing; ATP-binding;
KW Calmodulin-binding; Isopeptide bond; Motor protein; Myosin;
KW Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Ubl conjugation.
FT CHAIN 1..1136
FT /note="Unconventional myosin-Ib"
FT /id="PRO_0000123444"
FT DOMAIN 15..701
FT /note="Myosin motor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00782"
FT DOMAIN 704..729
FT /note="IQ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 730..750
FT /note="IQ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 750..778
FT /note="IQ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 780..807
FT /note="IQ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 808..837
FT /note="IQ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 837..866
FT /note="IQ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00116"
FT DOMAIN 952..1136
FT /note="TH1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01093"
FT REGION 592..599
FT /note="Actin-binding"
FT /evidence="ECO:0000255"
FT BINDING 108..115
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O43795"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43795"
FT CROSSLNK 287
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0000250|UniProtKB:O43795"
FT VAR_SEQ 794..852
FT /note="Missing (in isoform C)"
FT /evidence="ECO:0000303|PubMed:8449985"
FT /id="VSP_003349"
FT VAR_SEQ 794..823
FT /note="Missing (in isoform B)"
FT /evidence="ECO:0000303|PubMed:8449985"
FT /id="VSP_003348"
FT TURN 10..13
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 20..22
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 28..40
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 45..48
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 51..55
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 66..72
FT /evidence="ECO:0007829|PDB:4L79"
FT TURN 77..79
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 80..82
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 84..98
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 102..109
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 112..128
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 133..144
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 146..153
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 161..164
FT /evidence="ECO:0007829|PDB:5V7X"
FT STRAND 166..174
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 180..188
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 206..214
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 217..222
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 233..235
FT /evidence="ECO:0007829|PDB:5V7X"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:6C1D"
FT HELIX 247..260
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 265..281
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:5V7X"
FT STRAND 292..295
FT /evidence="ECO:0007829|PDB:6C1D"
FT STRAND 299..301
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 304..313
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 331..334
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 337..339
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 342..370
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 381..387
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 395..397
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 399..429
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 442..450
FT /evidence="ECO:0007829|PDB:4L79"
FT TURN 452..454
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 456..465
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 472..482
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 489..491
FT /evidence="ECO:0007829|PDB:5V7X"
FT TURN 492..494
FT /evidence="ECO:0007829|PDB:4L79"
FT TURN 498..501
FT /evidence="ECO:0007829|PDB:6C1D"
FT STRAND 507..514
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 517..522
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 526..530
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 536..543
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 544..547
FT /evidence="ECO:0007829|PDB:6C1D"
FT HELIX 548..553
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 555..557
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 558..561
FT /evidence="ECO:0007829|PDB:5V7X"
FT HELIX 570..586
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 588..596
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 609..619
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 621..629
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 633..637
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 638..645
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 646..648
FT /evidence="ECO:0007829|PDB:5V7X"
FT TURN 650..655
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 660..670
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 677..680
FT /evidence="ECO:0007829|PDB:4L79"
FT STRAND 682..688
FT /evidence="ECO:0007829|PDB:4L79"
FT HELIX 690..728
FT /evidence="ECO:0007829|PDB:4L79"
SQ SEQUENCE 1136 AA; 131918 MW; 69D6C2A84E9070E2 CRC64;
MAKKEVKSSL LDNMIGVGDT VLLEPLNEET FIDNLKKRFD HNEIYTYIGS VVISVNPYRS
LPIYSPEKVE DYRNRNFYEL SPHIFALSDE AYRSLRDQDK DQCILITGES GAGKTEASKL
VMSYVAAVCG KGAEVNQVKE QLLQSTPVLE AFGNAKTVRN DNSSRFGKYM DIEFDFKGDP
LGGVISNYLL EKSRVVKQPR GERNFHVFYQ LLSGASEELL HKLKLERDFS RYNYLSLDSA
KVNGVDDAAN FRTVRNAMQI VGFSDPEAES VLEVVAAVLK LGNIEFKPES RMNGLDESKI
KDKNELKEIC ELTSIDQVVL ERAFSFRTVE AKQEKVSTTL NVAQAYYARD ALAKNLYSRL
FSWLVNRINE SIKAQTKVRK KVMGVLDIYG FEIFEDNSFE QFIINYCNEK LQQIFIELTL
KEEQEEYIRE DIEWTHIDYF NNAIICDLIE NNTNGILAML DEECLRPGTV TDETFLEKLN
QVCATHQHFE SRMSKCSRFL NDTTLPHSCF RIQHYAGKVL YQVEGFVDKN NDLLYRDLSQ
AMWKAGHALI KSLFPEGNPA KVNLKRPPTA GSQFKASVAT LMKNLQTKNP NYIRCIKPND
KKAAHIFSES LVCHQIRYLG LLENVRVRRA GYAFRQAYEP CLERYKMLCK QTWPHWKGPA
RSGVEVLFNE LEIPVEEYSF GRSKIFIRNP RTLFQLEDLR KQRLEDLATL IQKIYRGWKC
RTHFLLMKRS QVVIAAWYRR YAQQKRYQQI KSSALVIQSY IRGWKARKIL RELKHQKRCK
EAATTIAAYW HGTQARKERR RLKDEARNKH AIAVIWAFWL GSKARRELKR LKEEARRKHA
VAVIWAYWLG LKVRREYRKF FRANAGKKIY EFTLQRIVQK YLLEMKNKMP SLSPIDKNWP
SRPYLFLDST HKELKRIFHL WRCKKYRDQF TDQQKLIYEE KLEASELFKD KKALYPSSVG
QPFQGAYLEI NKNPKYKKLK DAIEEKIIIA EVVNKINRAN GKSTSRIFLL TNNNLLLADQ
KSGQIKSEVP LVDVTKVSMS SQNDGFFAVH LKEGSEAASK GDFLFSSDHL IEMATKLYRT
TLSQTKQKLN IEISDEFLVQ FRQDKVCVKF IQGNQKNGSV PTCKRKNNRL LEVAVP
