Q5ZK03

PR
Gene name
SEC23A
Protein name
Protein transport protein Sec23A
Names
SEC23-related protein A
Species
Gallus gallus (Chicken)
KEGG Pathway
gga:416724
EC number
Protein Class

Descriptions

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

Autoinhibitory domains (AIDs)

173-256 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for Q5ZK03

Entry ID Method Resolution Chain Position Source
AF-Q5ZK03-F1 Predicted AlphaFoldDB

9 variants for Q5ZK03

Variant ID(s) Position Change Description Diseaes Association Provenance
rs733799119 26 S>A No Ensembl
rs315821041 30 E>G No Ensembl
rs737972367 176 H>P No Ensembl
rs316099761 297 T>R No Ensembl
rs740920837 430 V>G No Ensembl
rs313266496 440 L>I No Ensembl
rs735915837 534 Y>D No Ensembl
rs736794929 540 E>G No Ensembl
rs739413046 664 E>G No Ensembl

No associated diseases with Q5ZK03

6 regional properties for Q5ZK03

Type Name Position InterPro Accession
domain Zinc finger, Sec23/Sec24-type 58 - 98 IPR006895
domain Sec23/Sec24, trunk domain 127 - 392 IPR006896
domain Sec23/Sec24, helical domain 520 - 618 IPR006900
domain Gelsolin-like domain 634 - 720 IPR007123
domain Sec23/Sec24 beta-sandwich 403 - 506 IPR012990
domain Sec23, C-terminal 612 - 732 IPR037550

Functions

Description
EC Number
Subcellular Localization
  • Cytoplasmic vesicle, COPII-coated vesicle membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Endoplasmic reticulum membrane ; Peripheral membrane protein ; Cytoplasmic side
  • Cytoplasm, cytosol
  • Enriched at endoplasmic reticulum exit sites (ERES), also known as transitional endoplasmic reticulum (tER)
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

6 GO annotations of cellular component

Name Definition
COPII vesicle coat One of two multimeric complexes that forms a membrane vesicle coat. COPII is best characterized in S. cerevisiae, where the subunits are called Sar1p, Sec13p, Sec31p, Sec23p, and Sec24p. Vesicles with COPII coats are found associated with endoplasmic reticulum (ER) 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.
endoplasmic reticulum exit site An endoplasmic reticulum part at which COPII-coated vesicles are produced.
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
extrinsic component of membrane The component of a membrane consisting of gene products and protein complexes that are loosely bound to one of its surfaces, but not integrated into the hydrophobic region.
perinuclear region of cytoplasm Cytoplasm situated near, or occurring around, the nucleus.

2 GO annotations of molecular function

Name Definition
GTPase activator activity Binds to and increases the activity of a GTPase, an enzyme that catalyzes the hydrolysis of GTP.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
COPII-coated vesicle cargo loading The formation of a macromolecular complex between the COPII coat proteins and proteins and/or lipoproteins that are going to be transported by the COPII vesicle to the Golgi.
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.

4 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
Q3SZN2 SEC23B Protein transport protein Sec23B Bos taurus (Bovine) PR
Q15436 SEC23A Protein transport protein Sec23A Homo sapiens (Human) PR
Q15437 SEC23B Protein transport protein Sec23B Homo sapiens (Human) PR
Q9D662 Sec23b Protein transport protein Sec23B Mus musculus (Mouse) PR
10 20 30 40 50 60
MATYLEFIQQ NEERDGVRFS WNVWPSSRLE ATRMVVPLAC LLTPLRERPD LPPVQYEPVL
70 80 90 100 110 120
CSRPTCKAVL NPLCQVDYRA KLWACNFCFQ RNQFPPAYAG ISEVNQPAEL MPQFSTIEYI
130 140 150 160 170 180
VQRGPQTPLI FLYVVDTCLE EEDLQALKES LQMSLSLLPA DALVGLITFG RMIQVHELSC
190 200 210 220 230 240
EGISKSYVFR GTKDLTAKQI QDMLGLSRPA VPIQQGRPLQ APEQPVISSR FLQPVHKIDM
250 260 270 280 290 300
NLTDLLGELQ RDPWPVTQGK RPLRSTGVAL SIAVGLLEGT FPNTGARIML FTGGPPTQGP
310 320 330 340 350 360
GMVVGDELKT PIRSWHDIEK DNARFMKKAT KHYETLANRT ATNGHCIDIY ACALDQTGLL
370 380 390 400 410 420
EMKCCANLTG GHMVMGDSFN TSLFKQTFQR VFNKGLNGEF RMAFGANLEV KTSRELKIAG
430 440 450 460 470 480
AIGPCVSLNV KGPCVSENEL GIGGTSQWKI CGLDPCTTLA IYFEVVNQHN APIPQGGRGA
490 500 510 520 530 540
VQFVTQYQHS STQKRIRVTT IARNWADAQS QLQHIEAAFD QEAAAVLMAR LGVYRAESEE
550 560 570 580 590 600
GPDVLRWLDR QLIRLCQKFG QYNKDDPNSF RLSESFSLYP QFMFHLRRSP FLQVFNNSPD
610 620 630 640 650 660
ESSYYRHHFA RQDLTQSLIM IQPILYAYSF HGPPEPVLLD SSSILPDRIL LMDTFFQIVI
670 680 690 700 710 720
YLGETIAQWQ KAGYQDMPEY ENFKHLLQAP LDDAQEILQT RFPMPRYVHT EHGGSQARFL
730 740 750 760
LSKVNPSQTH NNLYAWGQES GAPILTDDVS LQVFMDHLKK LAVSSAA