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 O42713

Entry ID Method Resolution Chain Position Source
AF-O42713-F1 Predicted AlphaFoldDB

No variants for O42713

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for O42713

No associated diseases with O42713

2 regional properties for O42713

Type Name Position InterPro Accession
domain Tyrosinase copper-binding domain 48 - 294 IPR002227
domain Tyosinase, C-terminal 411 - 513 IPR041640

Functions

Description
EC Number 1.14.18.1 With another compound as one donor, and incorporation of one atom of oxygen
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
metal ion binding Binding to a metal ion.
tyrosinase activity Catalysis of the reaction: L-tyrosine + O2 = L-DOPAquinone + H2O. This reaction can use both monophenols (such as tyrosine) and catechols (o-diphenols) as substrates.

1 GO annotations of biological process

Name Definition
melanin biosynthetic process The chemical reactions and pathways resulting in the formation of melanins, pigments largely of animal origin. High molecular weight polymers of indole quinone, they are irregular polymeric structures and are divided into three groups: allomelanins in the plant kingdom and eumelanins and phaeomelanins in the animal kingdom.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MSLIATVGPT GGVKNRLNIV DFVKNEKFFT LYVRSLELLQ AKEQHDYSSF FQLAGIHGLP
70 80 90 100 110 120
FTEWAKERPS MNLYKAGYCT HGQVLFPTWH RTYLSVLEQI LQGAAIEVAK KFTSNQTDWV
130 140 150 160 170 180
QAAQDLRQPY WDWGFELMPP DEVIKNEEVN ITNYDGKKIS VKNPILRYHF HPIDPSFKPY
190 200 210 220 230 240
GDFATWRTTV RNPDRNRRED IPGLIKKMRL EEGQIREKTY NMLKFNDAWE RFSNHGISDD
250 260 270 280 290 300
QHANSLESVH DDIHVMVGYG KIEGHMDHPF FAAFDPIFWL HHTNVDRLLS LWKAINPDVW
310 320 330 340 350 360
VTSGRNRDGT MGIAPNAQIN SETPLEPFYQ SGDKVWTSAS LADTARLGYS YPDFDKLVGG
370 380 390 400 410 420
TKELIRDAID DLIDERYGSK PSSGARNTAF DLLADFKGIT KEHKEDLKMY DWTIHVAFKK
430 440 450 460 470 480
FELKESFSLL FYFASDGGDY DQENCFVGSI NAFRGTAPET CANCQDNENL IQEGFIHLNH
490 500 510 520 530 540
YLARDLESFE PQDVHKFLKE KGLSYKLYSR GDKPLTSLSV KIEGRPLHLP PGEHRPKYDH
550
TQARVVFDDV AVHVIN