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

4 structures for P36006

Entry ID Method Resolution Chain Position Source
1RUW X-ray 180 A A 1121-1189 PDB
1VA7 X-ray 290 A A/B/C/D 1121-1189 PDB
2BTT NMR - A 1121-1189 PDB
AF-P36006-F1 Predicted AlphaFoldDB

24 variants for P36006

Variant ID(s) Position Change Description Diseaes Association Provenance
s11-200052 38 I>V No SGRP
s11-199509 219 G>S No SGRP
s11-199439 242 K>R No SGRP
s11-199433 244 M>T No SGRP
s11-199289 293 I>N No SGRP
s11-199268 300 I>N No SGRP
s11-198815 451 R>K No SGRP
s11-198797 457 T>I No SGRP
s11-198535 544 Q>H No SGRP
s11-198032 712 D>G No SGRP
s11-197499 890 S>P No SGRP
s11-197363 935 S>L No SGRP
s11-197328 947 I>V No SGRP
s11-197169 1000 H>N No SGRP
s11-197010 1053 H>N No SGRP
s11-196965 1068 A>T No SGRP
s11-196915 1084 M>I No SGRP
s11-196913 1085 P>Q No SGRP
s11-196805 1121 K>R No SGRP
s11-196799 1123 P>L No SGRP
s11-196623 1182 D>Y No SGRP
s11-196559 1203 S>L No SGRP
s11-196403 1255 A>V No SGRP
s11-196394 1258 A>V No SGRP

No associated diseases with P36006

5 regional properties for P36006

Type Name Position InterPro Accession
domain SH3 domain 1120 - 1182 IPR001452
domain Myosin head, motor domain 30 - 716 IPR001609
domain Class I myosin tail homology domain 760 - 961 IPR010926
domain Fungal myosin-I, SH3 domain 1125 - 1179 IPR035535
domain Class I myosin, motor domain 50 - 702 IPR036072

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytoskeleton, actin patch
  • Localizes to cortical patch-like protein structures that assemble actin patches
  • Enriched at sites of polarized growth
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
actin cortical patch An endocytic patch that consists of an actin-containing structure found at the plasma membrane in cells; formed of networks of branched actin filaments that lie just beneath the plasma membrane and assemble, move, and disassemble rapidly. An example of this is the actin cortical patch found in Saccharomyces cerevisiae.
actin cytoskeleton The part of the cytoskeleton (the internal framework of a cell) composed of actin and associated proteins. Includes actin cytoskeleton-associated complexes.
cell periphery The part of a cell encompassing the cell cortex, the plasma membrane, and any external encapsulating structures.
cell tip The region at the end of the longest axis of a cylindrical or elongated cell.
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.

5 GO annotations of molecular function

Name Definition
actin filament binding Binding to an actin filament, also known as F-actin, a helical filamentous polymer of globular G-actin subunits.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
hydrolase activity Catalysis of the hydrolysis of various bonds, e.g. C-O, C-N, C-C, phosphoric anhydride bonds, etc.
microfilament motor activity A motor activity that generates movement along a microfilament, driven by ATP hydrolysis.
myosin binding Binding to a myosin; myosins are any of a superfamily of molecular motor proteins that bind to actin and use the energy of ATP hydrolysis to generate force and movement along actin filaments.

9 GO annotations of biological process

Name Definition
actin cortical patch localization Any process in which actin cortical patches are transported to, or maintained in, a specific location. An actin cortical patch is a discrete actin-containing structure found just beneath the plasma membrane in fungal cells.
actin filament 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. Includes processes that control the spatial distribution of actin filaments, such as organizing filaments into meshworks, bundles, or other structures, as by cross-linking.
bipolar cellular bud site selection The process of defining subsequent sites of bud emergence such that budding takes place at alternating poles of a budding cell.
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.
exocytosis A process of secretion by a cell that results in the release of intracellular molecules (e.g. hormones, matrix proteins) contained within a membrane-bounded vesicle. Exocytosis can occur either by full fusion, when the vesicle collapses into the plasma membrane, or by a kiss-and-run mechanism that involves the formation of a transient contact, a pore, between a granule (for exemple of chromaffin cells) and the plasma membrane. The latter process most of the time leads to only partial secretion of the granule content. Exocytosis begins with steps that prepare vesicles for fusion with the membrane (tethering and docking) and ends when molecules are secreted from the cell.
fungal-type cell wall organization A process that is carried out at the cellular level which results in the assembly, arrangement of constituent parts, or disassembly of the fungal-type cell wall.
positive regulation of Arp2/3 complex-mediated actin nucleation Any process that activates or increases the frequency, rate or extent of Arp2/3 complex-mediated actin nucleation.
response to osmotic stress Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating an increase or decrease in the concentration of solutes outside the organism or cell.
vesicle transport along actin filament Movement of a vesicle along an actin filament, mediated by motor proteins.

3 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q12965 MYO1E Unconventional myosin-Ie Homo sapiens (Human) PR
O00160 MYO1F Unconventional myosin-If Homo sapiens (Human) PR
E9Q634 Myo1e Unconventional myosin-Ie Mus musculus (Mouse) PR
10 20 30 40 50 60
MAVIKKGARR KDVKEPKKRS AKIKKATFDA NKKKEVGISD LTLLSKISDE SINENLKKRF
70 80 90 100 110 120
KNGIIYTYIG HVLISVNPFR DLGIYTNAVL ESYKGKNRLE VPPHVFAIAE SMYYNLKSYN
130 140 150 160 170 180
ENQCVIISGE SGAGKTEAAK RIMQYIAAAS NSHSESIGKI KDMVLATNPL LESFGCAKTL
190 200 210 220 230 240
RNNNSSRHGK YLEIKFNSQF EPCAGNITNY LLEKQRVVGQ IKNERNFHIF YQFTKGASDT
250 260 270 280 290 300
YKQMFGVQMP EQYIYTAAAG CTTADTIDDV KDYEGTLEAM RTIGLVQEEQ DQIFRMLAAI
310 320 330 340 350 360
LWIGNISFIE NEEGNAQVGD TSVTDFVAYL LQVDASLLVK CLVERIMQTS HGMKRGSVYH
370 380 390 400 410 420
VPLNPVQATA VRDALAKAIY NNLFDWIVDR VNVSLQAFPG ADKSIGILDI YGFEIFEHNS
430 440 450 460 470 480
FEQICINYVN EKLQQIFIQL TLKAEQETYE REKIKWTPIK YFDNKVVCDL IEAKNPPGIL
490 500 510 520 530 540
AAMNDSIATA HADSNAADQA FAQRLNLFNS NPYFELRANK FVIKHYAGDV TYDINGITDK
550 560 570 580 590 600
NKDQLQKDLI ELIGTTTNTF LSTIFPDDVD KDSKRRPPTA GDKIIKSANE LVETLSKAEP
610 620 630 640 650 660
SYIRTIKPNQ TKSPNDYDDH QVLHQVKYLG LQENVRIRRA GFAYRQTFEK FVERFYLLSP
670 680 690 700 710 720
DCSYAGDYTW DGDTLEAVKL ILRDAMIPEK EFQLGVTSVF IKTPESLFAL EDMRDKYWYN
730 740 750 760 770 780
MAARIQRAWR RFLQRRIDAA IKIQRTIREK KGGNKYVKLR DYGTKLLAGK KERRSMSLLG
790 800 810 820 830 840
YRAFMGDYLS CNESKTKGSY IRRQVGIKDK VVFSIKGECL HSKFGRSAQR LKKVFILTKK
850 860 870 880 890 900
TFYIIGQTRE QNAMKYTQDY KIDVGKIKQV SLTNLQDDWM GVILVNSTQS DPLINTPFKT
910 920 930 940 950 960
ELMTRLKKLN EKIMIKVGPT IEYHKQPNKL HTVRSKISDS APKYGDIYKS STIYVRRGHP
970 980 990 1000 1010 1020
ANSKSNKKPK NPGGLSGKPI KSKKSKHKST HKHTHSHRSH RDAAKKQPLP SQKPVNPLSL
1030 1040 1050 1060 1070 1080
AATAAQAAYN PKPDKTVPIK SSAIPAAKVS SKHSSKPSSK EKVAVKKASS SHKSSSAKQN
1090 1100 1110 1120 1130 1140
QVSMPPSKGV EKNKEPLKET TATATANIPI PPPPPPMGQP KDPKFEAAYD FPGSGSSSEL
1150 1160 1170 1180 1190 1200
PLKKGDIVFI SRDEPSGWSL AKLLDGSKEG WVPTAYMTPY KDTRNTVPVA ATGAVNDVTN
1210 1220 1230 1240 1250 1260
QKSSQIDNTI SSAQEGVQFG SATVGPTSDN QSNPVGTFSD GLASALAARA NKMRAESADD
1270
DDNDDGDDDD DW