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 Q3ZC33

Entry ID Method Resolution Chain Position Source
AF-Q3ZC33-F1 Predicted AlphaFoldDB

58 variants for Q3ZC33

Variant ID(s) Position Change Description Diseaes Association Provenance
rs444247689 36 V>A No EVA
rs444247689 36 V>G No EVA
rs3423270410 64 G>S No EVA
rs474739878 73 N>T No EVA
rs440110540 74 R>P No EVA
rs442926088 97 H>P No EVA
rs459812486 99 Q>H No EVA
rs479875490 105 L>Q No EVA
rs442619002 112 A>D No EVA
rs459534233 116 V>G No EVA
rs438508531 133 H>R No EVA
rs458545681 134 G>A No EVA
rs468366601 140 V>A No EVA
rs468366601 140 V>G No EVA
rs718115122 149 N>S No EVA
rs464214657 158 S>A No EVA
rs432790009 164 F>Y No EVA
rs455964447 179 T>A No EVA
rs476744829 189 H>R No EVA
rs442256682 198 T>P No EVA
rs472793936 201 E>A No EVA
rs208467135 220 W>R No EVA
rs434670338 233 D>A No EVA
rs451463527 236 N>T No EVA
rs469102728 258 F>L No EVA
rs454497410 261 W>L No EVA
rs475136762 263 S>I No EVA
rs471459263 264 T>I No EVA
rs443242183 265 F>Y No EVA
rs463342293 266 L>M No EVA
rs449614218 270 V>L No EVA
rs460030551 273 I>M No EVA
rs1116688779 283 N>S No EVA
rs476246991 287 E>* No EVA
rs454301509 317 K>E No EVA
rs464766536 317 K>R No EVA
rs464766536 317 K>T No EVA
rs433369608 318 E>K No EVA
rs442069219 344 T>P No EVA
rs455752398 349 I>M No EVA
rs472551402 350 L>M No EVA
rs440300075 350 L>R No EVA
rs460356297 351 L>M No EVA
rs439379499 358 D>V No EVA
rs462520474 360 C>* No EVA
rs482506513 363 N>T No EVA
rs448056275 368 R>M No EVA
rs445284789 394 P>A No EVA
rs465323240 395 H>P No EVA
rs472939185 400 H>N No EVA
rs432675668 400 H>R No EVA
rs452642791 401 N>K No EVA
rs444590065 405 K>T No EVA
rs461315858 406 D>E No EVA
rs208119989 411 Y>* No EVA
rs458819154 428 G>A No EVA
rs467539229 433 A>V No EVA
rs481174816 438 V>E No EVA

No associated diseases with Q3ZC33

3 regional properties for Q3ZC33

Type Name Position InterPro Accession
domain GINS subunit, domain A 50 - 126 IPR021151
domain DNA replication complex GINS protein SLD5, C-terminal 165 - 223 IPR031633
domain GINS complex protein Sld5, alpha-helical domain 26 - 146 IPR038749

Functions

Description
EC Number 1.1.3.8 With oxygen as acceptor
Subcellular Localization
  • Microsome membrane ; Single-pass membrane protein
  • Endoplasmic reticulum membrane ; Single-pass membrane protein
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

2 GO annotations of cellular component

Name Definition
endoplasmic reticulum membrane The lipid bilayer surrounding the endoplasmic reticulum.
integral component of membrane The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane.

5 GO annotations of molecular function

Name Definition
D-arabinono-1,4-lactone oxidase activity Catalysis of the reaction: D-arabinono-1,4-lactone + O(2) = dehydro-D-arabinono-1,4-lactone + H(2)O(2) + H(+).
FAD binding Binding to the oxidized form, FAD, of flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes.
flavin adenine dinucleotide binding Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2.
L-gulonolactone oxidase activity Catalysis of the reaction: L-gulono-1,4-lactone + O2 = L-xylo-hex-3-ulonolactone + H2O2.
oxidoreductase activity Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced.

1 GO annotations of biological process

Name Definition
L-ascorbic acid biosynthetic process The chemical reactions and pathways resulting in the formation of L-ascorbic acid; L-ascorbic acid ionizes to give L-ascorbate, (2R)-2-[(1S)-1,2-dihydroxyethyl]-4-hydroxy-5-oxo-2,5-dihydrofuran-3-olate, which is required as a cofactor in the oxidation of prolyl residues to hydroxyprolyl, and other reactions.

5 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P58710 Gulo L-gulonolactone oxidase Mus musculus (Mouse) PR
Q8HXW0 GULO L-gulonolactone oxidase Sus scrofa (Pig) PR
P10867 Gulo L-gulonolactone oxidase Rattus norvegicus (Rat) PR
Q2QXY1 GLDH2 L-galactono-1,4-lactone dehydrogenase 2, mitochondrial Oryza sativa subsp japonica (Rice) PR
Q2RAP0 GLDH1 L-galactono-1,4-lactone dehydrogenase 1, mitochondrial Oryza sativa subsp japonica (Rice) PR
10 20 30 40 50 60
MVHGYKGVKF QNWARTYGCC PEMYFQPTSV EEVREVLALA RQQNKRVKVV GGGHSPSDIA
70 80 90 100 110 120
CTDGFMIHMG KMNRVLKVDT EKKQVTVEAG ILLADLHPQL DKHGLALSNL GAVSDVTAGG
130 140 150 160 170 180
VIGSGTHNTG IKHGILATQV VALTLLTANG TILECSESSN AEVFQAARVH LGCLGVILTV
190 200 210 220 230 240
TLQCVPQFHL QETTFPSTLK EVLDNLDSHL KKSEYFRFLW FPHSENVSVI YQDHTNKPPS
250 260 270 280 290 300
SSANWFWDYA IGFYLLEFLL WISTFLPGLV GWINRFFFWL LFNGKKENCN LSHKIFTYEC
310 320 330 340 350 360
RFKQHVQDWA IPREKTKEAL LELKAMLEAN PKVVAHYPVE VRFTRGDDIL LSPCFQRDSC
370 380 390 400 410 420
YMNIIMYRPY GKDVPRLDYW LAYETIMKKV GGRPHWAKAH NCTRKDFEKM YPAFQRFCAI
430
REKLDPTGMF LNAYLEKVFY