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

11 structures for O55029

Entry ID Method Resolution Chain Position Source
5A1U EM 1300 A D 1-905 PDB
5A1V EM 2100 A D/L/U 1-905 PDB
5A1W EM 1800 A D 1-905 PDB
5A1X EM 2300 A D/L 1-905 PDB
5A1Y EM 2100 A D/L 1-905 PDB
5NZR EM 920 A C 1-905 PDB
5NZS EM 1010 A C 1-905 PDB
5NZT EM 1700 A C/H 1-905 PDB
5NZU EM 1500 A C 1-905 PDB
5NZV EM 1730 A C/J 1-905 PDB
AF-O55029-F1 Predicted AlphaFoldDB

42 variants for O55029

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3389068674 22 D>V No EVA
rs3389045375 28 P>Q No EVA
rs3389010518 46 T>I No EVA
rs3389059086 79 M>L No EVA
rs3389045343 98 H>N No EVA
rs3389053362 105 I>F No EVA
rs3389065106 105 I>M No EVA
rs3389063176 116 T>I No EVA
rs3389066102 122 L>P No EVA
rs3389063141 132 W>R No EVA
rs3389073344 136 Q>R No EVA
rs3389060515 137 V>M No EVA
rs3389066079 147 Q>* No EVA
rs3389065930 150 I>L No EVA
rs3389053443 171 Q>* No EVA
rs3389065102 172 L>R No EVA
rs3389073368 205 G>C No EVA
rs3389066054 268 N>H No EVA
rs3389040470 275 W>G No EVA
rs3389040439 328 K>T No EVA
rs3389074239 332 D>N No EVA
rs3389060565 353 I>L No EVA
rs3389068616 365 R>K No EVA
rs3389060575 384 R>G No EVA
rs3389067489 386 K>* No EVA
rs244687417 411 I>V No EVA
rs3389073370 433 I>S No EVA
rs3389068693 460 R>S No EVA
rs3389073365 484 S>L No EVA
rs3389066082 487 I>T No EVA
rs3389062947 516 V>D No EVA
rs3389059145 532 D>G No EVA
rs3389066059 540 V>M No EVA
rs3400456225 685 L>Q No EVA
rs3399993906 687 Q>S No EVA
rs3389040478 700 L>P No EVA
rs3389074288 703 A>V No EVA
rs3389060581 704 T>I No EVA
rs3389068653 747 R>T No EVA
rs3389060572 779 K>N No EVA
rs3389059113 820 P>T No EVA
rs3389066080 885 N>D No EVA

No associated diseases with O55029

7 regional properties for O55029

Type Name Position InterPro Accession
repeat WD40 repeat 4 - 85 IPR001680-1
repeat WD40 repeat 88 - 127 IPR001680-2
repeat WD40 repeat 131 - 266 IPR001680-3
domain Coatomer, WD associated region 319 - 762 IPR006692
repeat G-protein beta WD-40 repeat 158 - 172 IPR020472-1
repeat G-protein beta WD-40 repeat 202 - 216 IPR020472-2
repeat G-protein beta WD-40 repeat 244 - 258 IPR020472-3

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm, cytosol
  • Golgi apparatus membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cytoplasmic vesicle, COPI-coated vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side
  • The coatomer is cytoplasmic or polymerized on the cytoplasmic side of the Golgi, as well as on the vesicles/buds originating from it
  • Shows only a slight preference for the cis-Golgi apparatus, compared with the trans-Golgi
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
COPI vesicle coat One of two multimeric complexes that forms a membrane vesicle coat. The mammalian COPI subunits are called alpha-, beta-, beta'-, gamma-, delta-, epsilon- and zeta-COP. Vesicles with COPI coats are found associated with Golgi membranes at steady state.
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
Golgi apparatus A membrane-bound cytoplasmic organelle of the endomembrane system that further processes the core oligosaccharides (e.g. N-glycans) added to proteins in the endoplasmic reticulum and packages them into membrane-bound vesicles. The Golgi apparatus operates at the intersection of the secretory, lysosomal, and endocytic pathways.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.

2 GO annotations of molecular function

Name Definition
protein kinase C binding Binding to protein kinase C.
structural molecule activity The action of a molecule that contributes to the structural integrity of a complex or its assembly within or outside a cell.

5 GO annotations of biological process

Name Definition
endoplasmic reticulum to Golgi vesicle-mediated transport The directed movement of substances from the endoplasmic reticulum (ER) to the Golgi, mediated by COP II vesicles. Small COP II coated vesicles form from the ER and then fuse directly with the cis-Golgi. Larger structures are transported along microtubules to the cis-Golgi.
intra-Golgi vesicle-mediated transport The directed movement of substances within the Golgi, mediated by small transport vesicles. These either fuse with the cis-Golgi or with each other to form the membrane stacks known as the cis-Golgi reticulum (network).
intracellular protein transport The directed movement of proteins in a cell, including the movement of proteins between specific compartments or structures within a cell, such as organelles of a eukaryotic cell.
retrograde vesicle-mediated transport, Golgi to endoplasmic reticulum The directed movement of substances from the Golgi back to the endoplasmic reticulum, mediated by vesicles bearing specific protein coats such as COPI or COG.
toxin transport The directed movement of a toxin into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore.

8 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P41811 SEC27 Coatomer subunit beta' Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) PR
P35605 COPB2 Coatomer subunit beta' Bos taurus (Bovine) PR
O62621 beta'COP Coatomer subunit beta' Drosophila melanogaster (Fruit fly) PR
P53621 COPA Coatomer subunit alpha Homo sapiens (Human) PR
P35606 COPB2 Coatomer subunit beta' Homo sapiens (Human) PR
Q8CIE6 Copa Coatomer subunit alpha Mus musculus (Mouse) PR
O35142 Copb2 Coatomer subunit beta' Rattus norvegicus (Rat) PR
Q9CAA0 At1g79990 Coatomer subunit beta'-1 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MPLRLDIKRK LTARSDRVKS VDLHPTEPWM LASLYNGSVC VWNHETQTLV KTFEVCDLPV
70 80 90 100 110 120
RAAKFVARKN WVVTGADDMQ IRVFNYNTLE RVHMFEAHSD YIRCIAVHPT QPFILTSSDD
130 140 150 160 170 180
MLIKLWDWDK KWSCSQVFEG HTHYVMQIVI NPKDNNQFAS ASLDRTIKVW QLGSSSPNFT
190 200 210 220 230 240
LEGHEKGVNC IDYYSGGDKP YLISGADDRL VKIWDYQNKT CVQTLEGHAQ NVSCASFHPE
250 260 270 280 290 300
LPIIITGSED GTVRIWHSST YRLESTLNYG MERVWCVASL RGSNNVALGY DEGSIIVKLG
310 320 330 340 350 360
REEPAMSMDA NGKIIWAKHS EVQQANLKAM GDTEIKDGER LPLAVKDMGS CEIYPQTIQH
370 380 390 400 410 420
NPNGRFVVVC GDGEYIIYTA MALRNKSFGS AQEFAWAHDS SEYAIRESNS IVKIFKNFKE
430 440 450 460 470 480
KKSFKPDFGA ESIYGGFLLG VRSVNGLAFY DWENTELIRR IEIQPKHIFW SDSGELVCIA
490 500 510 520 530 540
TEESFFILKY LSEKVLAAQE THEGVTEDGI EDAFEVLGEI QEIVKTGLWV GDCFIYTSSV
550 560 570 580 590 600
NRLNYYVGGE IVTIAHLDRT MYLLGYIPKD NRLYLGDKEL NIVSYSLLVS VLEYQTAVMR
610 620 630 640 650 660
RDFSMADKVL PTIPKEQRTR VAHFLEKQGF KQQALTVSTD PEHRFELALQ LGELKIAYQL
670 680 690 700 710 720
AVEAESEQKW KQLAELAISK CQFSLAQECL HHAQDYGGLL LLATASGNAS MVNKLAEGAE
730 740 750 760 770 780
RDGKNNVAFM SYFLQGKLDA CLELLIRTGR LPEAAFLART YLPSQVSRVV KLWRENLSKV
790 800 810 820 830 840
NQKAAESLAD PTEYENLFPG LKEAFVVEEW VKETHADLWP AKQYPLVTPN EERNVMEEAK
850 860 870 880 890 900
GFQPSRPTAQ QEPDGKPASS PVIMASQTTH KEEKSLLELE VDLDNLELED IDTTDINLDE
DILDD