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 Q22498

Entry ID Method Resolution Chain Position Source
AF-Q22498-F1 Predicted AlphaFoldDB

No variants for Q22498

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q22498

No associated diseases with Q22498

3 regional properties for Q22498

Type Name Position InterPro Accession
domain Clathrin/coatomer adaptor, adaptin-like, N-terminal 23 - 532 IPR002553
domain Coatomer, gamma subunit, appendage, Ig-like subdomain 607 - 752 IPR013040
domain Coatomer subunit gamma, C-terminal 754 - 869 IPR032154

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasm
  • 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
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.
endoplasmic reticulum The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached).
endoplasmic reticulum-Golgi intermediate compartment A complex system of membrane-bounded compartments located between endoplasmic reticulum (ER) and the Golgi complex, with a distinctive membrane protein composition; involved in ER-to-Golgi and Golgi-to-ER transport.
Golgi membrane The lipid bilayer surrounding any of the compartments of the Golgi apparatus.

1 GO annotations of molecular function

Name Definition
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.
organelle transport along microtubule The directed movement of an organelle along a microtubule, mediated by motor proteins. This process begins with the attachment of an organelle to a microtubule, and ends when the organelle reaches its final destination.
protein secretion The controlled release of proteins from a cell.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MKTNKKDEET GGNVYAHLDK TSVLQEARAF NETPINARKC CFILSKLIYI IQQGESIGRT
70 80 90 100 110 120
EATEAFFGVT KLWQSKDVSL RRMVYLAVKE LAEVSDDVII VTSSLTKDMT GREDLYRAAA
130 140 150 160 170 180
IRALCKITDT GMLQTIERYM KQAIVDRNSA ISSSAIVSSI HLMRKSSEVV RRWANEVQEA
190 200 210 220 230 240
VSSDNHMVQY HALALLYQIR ANDRLAVNKL VQKFSKNALR SPYAVCYLIR IATRCLVDDD
250 260 270 280 290 300
QPDSSVFTFI ESCLRHKSEM VVYEAARAIV SLPQTTPSEI QPAITALQMC CTSPKAAVRF
310 320 330 340 350 360
AAVRTLNKVA MAHPNAVMSC NVDLEKFITD PNRSIATLAI TTLLKTGAES SVERLMQQIA
370 380 390 400 410 420
GFVNEISDEF KIVVVDAIRS LCSRYPRKHT VMMPFLAKML RSDGSYDYKK AIVETIIAII
430 440 450 460 470 480
EENPDAKVAG LAHLCEFIED CEHDNLSTRV LHLLGREAPK TPNPSSYIRF IYNRVILEST
490 500 510 520 530 540
KVRAAAVTAL AKFGAQCVDL RPSIQVLLKR CLLDSDDEVR DRATFYLKML TEAAEGLIHN
550 560 570 580 590 600
FILDGLQVSP SGLERSILDY LRSGSYSSPF DLRVVPVTQQ ALSQPEKRVP QLVEEEEKPK
610 620 630 640 650 660
APKVEPYAAQ LAAIPQFAAL GPVFKSSTRI ALTESIAEYT VHMIKHTFAN AMVLQFECKN
670 680 690 700 710 720
TMNDQLLLDV SVELEDPDGE WETGNTVQID KLPYGEVHSA FSLLEFPDSG AISGSLGAIL
730 740 750 760 770 780
KFKVMDVDPT SGEPDSDDTY EQTYVLEEVD VNVSDSVQGV AKSSFGSAWE ALGDDATREE
790 800 810 820 830 840
TFQLSTVENI PDAVKKISEI LGLVPCERSD RVPEGKTQHT VFLSGVFRGG YDVLSKATVA
850 860
VDPNDNSIAM NIIIKSNEPL VADLVISAVV