Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for P10569

Entry ID Method Resolution Chain Position Source
AF-P10569-F1 Predicted AlphaFoldDB

No variants for P10569

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P10569

No associated diseases with P10569

4 regional properties for P10569

Type Name Position InterPro Accession
domain SH3 domain 976 - 1035 IPR001452
domain Myosin head, motor domain 1 - 667 IPR001609
domain Class I myosin tail homology domain 693 - 892 IPR010926
domain Class I myosin, motor domain 21 - 653 IPR036072

Functions

Description
EC Number
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cell leading edge The area of a motile cell closest to the direction of movement.
myosin complex A protein complex, formed of one or more myosin heavy chains plus associated light chains and other proteins, that functions as a molecular motor; uses the energy of ATP hydrolysis to move actin filaments or to move vesicles or other cargo on fixed actin filaments; has magnesium-ATPase activity and binds actin. Myosin classes are distinguished based on sequence features of the motor, or head, domain, but also have distinct tail regions that are believed to bind specific cargoes.
plasma membrane The membrane surrounding a cell that separates the cell from its external environment. It consists of a phospholipid bilayer and associated proteins.
plasma membrane bounded cell projection A prolongation or process extending from a cell and that is bounded by plasma membrane, e.g. a cilium, lamellipodium, or axon.

3 GO annotations of molecular function

Name Definition
actin binding Binding to monomeric or multimeric forms of actin, including actin filaments.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
cytoskeletal motor activity Generation of force resulting in movement, for example along a microfilament or microtubule, or in torque resulting in membrane scission or rotation of a flagellum. The energy required is obtained either from the hydrolysis of a nucleoside triphosphate or by an electrochemical proton gradient (proton-motive force).

4 GO annotations of biological process

Name Definition
actin cytoskeleton organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of cytoskeletal structures comprising actin filaments and their associated proteins.
cellular component assembly The aggregation, arrangement and bonding together of a cellular component.
endocytosis A vesicle-mediated transport process in which cells take up external materials or membrane constituents by the invagination of a small region of the plasma membrane to form a new membrane-bounded vesicle.
locomotion Self-propelled movement of a cell or organism from one location to another.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAYTSKHGVD DMVMLTSISN DAINDNLKKR FAADLIYTYI GHVLISVNPY KQINNLYTER
70 80 90 100 110 120
TLKDYRGKYR YELPPHVYAL ADDMYRTMLS ESEDQCVIIS GESGAGKTEA SKKIMQYIAA
130 140 150 160 170 180
VSGATGDVMR VKDVILEAFG NAKTIRNNNS SRFGKYMEIQ FDLKGDPVGG RISNYLLEKS
190 200 210 220 230 240
RVVYQTNGER NFHIFYQLLA ARARRPEAKF GLQTPDYYFY LNQGKTYTVD GMDDNQEFQD
250 260 270 280 290 300
TWNAMKVIGF TAEEQHEIFR LVTAILYLGN VQFVDDGKGG STIADSRPVA VETALLYRTI
310 320 330 340 350 360
TTGEQGRGRS SVYSCPQDPL GAIYSRDALS KALYSRMFDY IIQRVNDAMY IDDPEALTTG
370 380 390 400 410 420
ILDIYGFEIF GKNGFEQLCI NFVNEKLQQI FIQLTLKAEQ EEYGAEGIQW ENIDYFNNKI
430 440 450 460 470 480
CCDLIEEKRP PGLMTILDDV CNFPKGTDDK FREKLLGAFP THAHLAATSQ PDEFVIKHYA
490 500 510 520 530 540
GDVVYNVDGF CDKNKDLLFK DLIGLAECTS STFFAGLFPE AKEVATSKKK PTTAGFKIKE
550 560 570 580 590 600
SINILVATLS KCTPHYIRCI KPNEKKAANA FNNSLVLHQV KYLGLLENVR IRRAGYAYRQ
610 620 630 640 650 660
SYDKFFYRYR VVCPKTWSGW NGDMVSGAEA ILNHVGMSLG KEYQKGKTKI FIRQPESVFS
670 680 690 700 710 720
LEELRDRTVF SYANKIQRFL RKTAMRKYYY EVKKGGNDAL VNKKERRRLS LERPFKTDYI
730 740 750 760 770 780
NYRQNFKLKD CIGDKGTEKV LFADLCNNLD KSFWGSKVER RIMVLTSNAM FLVAIDPNKD
790 800 810 820 830 840
KIEKKVKPFL YVLKRRIDFN KIGSITLSPL QDNFMLISVN GEHSNLLECR RKTELIGVLL
850 860 870 880 890 900
KHNPSVRIQF ADTFNVTLKG GKTCVVKFIR DPQGGDGKVK GTKVSVAPGL PPSSAPNIQA
910 920 930 940 950 960
PQETSGGASF TVAEQSYKDQ ILGAKGGGGG GGRGRGGPSP SGAVSPRPSP GGGGGGPSPF
970 980 990 1000 1010 1020
GGRPSPSGPP AAASAPGPEQ ARALYDFAAE NPDELTFNEG AVVTVINKSN PDWWEGELNG
1030 1040 1050 1060 1070 1080
QRGVFPASYV ELIPRAAAPA PGPSGGPRPA PPGGKSGRAA PMGGPGPMRG RGGPAPGGPG
1090 1100 1110 1120 1130 1140
RGGAPPPGAG RAGPPGGRGM PAPGGAAPRG RGAPPPGAGG PPGGGRGGAP PPGGMRGRGG
1150 1160
PGPAPPGGMA RGGMMPPRGR AGPPPPGM