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

2 structures for P45377

Entry ID Method Resolution Chain Position Source
1FRB X-ray 170 A A 2-316 PDB
AF-P45377-F1 Predicted AlphaFoldDB

23 variants for P45377

Variant ID(s) Position Change Description Diseaes Association Provenance
rs3396678669 4 F>I No EVA
rs3388816505 17 G>C No EVA
rs3388814994 36 I>F No EVA
rs585048019 69 Q>K No EVA
rs3388805718 106 D>G No EVA
rs3388814542 146 E>G No EVA
rs37187587 159 V>I No EVA
rs3388822942 161 N>D No EVA
rs231075541 206 S>T No EVA
rs217666289 207 V>I No EVA
rs3388814541 213 L>Q No EVA
rs3388814986 217 D>H No EVA
rs583190156 229 L>V No EVA
rs36267008 233 K>R No EVA
rs225357632 242 E>K No EVA
rs3388821553 257 N>I No EVA
rs3388808296 259 V>A No EVA
rs3396465586 276 V>A No EVA
rs3396693602 276 V>L No EVA
rs585114148 284 E>K No EVA
rs3396678696 292 F>L No EVA
rs3388823992 307 M>K No EVA
rs580288184 307 M>L No EVA

No associated diseases with P45377

1 regional properties for P45377

Type Name Position InterPro Accession
domain Clathrin/coatomer adaptor, adaptin-like, N-terminal 40 - 621 IPR002553

Functions

Description
EC Number 1.1.1.21 With NAD(+) or NADP(+) as acceptor
Subcellular Localization
  • Cytoplasm
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

4 GO annotations of cellular component

Name Definition
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
extracellular region The space external to the outermost structure of a cell. For cells without external protective or external encapsulating structures this refers to space outside of the plasma membrane. This term covers the host cell environment outside an intracellular parasite.
lysosome A small lytic vacuole that has cell cycle-independent morphology found in most animal cells and that contains a variety of hydrolases, most of which have their maximal activities in the pH range 5-6. The contained enzymes display latency if properly isolated. About 40 different lysosomal hydrolases are known and lysosomes have a great variety of morphologies and functions.
mitochondrion A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration.

11 GO annotations of molecular function

Name Definition
alcohol dehydrogenase (NADP+) activity Catalysis of the reaction: an alcohol + NADP+ = an aldehyde + NADPH + H+.
alditol:NADP+ 1-oxidoreductase activity Catalysis of the reaction: an alditol + NADP+ = an aldose + NADPH + H+.
estradiol 17-beta-dehydrogenase activity Catalysis of the reaction: estradiol-17-beta + NADP+ = estrone + NADPH + H+.
geranylgeranyl reductase activity Catalysis of the formation of phytyl group from the stepwise reduction of a geranylgeranyl group.
indanol dehydrogenase activity Catalysis of the reaction: indan-1-ol + NAD(P)+ = indanone + NAD(P)H + H+.
NADP+ binding Binding to the oxidized form, NADP+, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
NADP-retinol dehydrogenase activity Catalysis of the reaction: all-trans-retinol + NADP+ = all-trans-retinal + NADPH + H+.
NADPH binding Binding to the reduced form, NADPH, of nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions.
oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor Catalysis of an oxidation-reduction (redox) reaction in which a CH-OH group acts as a hydrogen or electron donor and reduces NAD+ or NADP.
retinal binding Binding to retinal, one of the forms of vitamin A. Retinal plays an important role in the visual process in most vertebrates, combining with opsins to form visual pigments in the retina.
retinal dehydrogenase activity Catalysis of the reaction: retinal + NAD+ + H2O = retinoate + NADH. Acts on both 11-trans and 13-cis forms of retinal.

2 GO annotations of biological process

Name Definition
polyol metabolic process The chemical reactions and pathways involving a polyol, any alcohol containing three or more hydroxyl groups attached to saturated carbon atoms.
retinal metabolic process The chemical reactions and pathways involving retinal, a compound that plays an important role in the visual process in most vertebrates. In the retina, retinal combines with opsins to form visual pigments. Retinal is one of the forms of vitamin A.

10 homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
P16116 AKR1B1 Aldo-keto reductase family 1 member B1 Bos taurus (Bovine) PR
P15121 AKR1B1 Aldo-keto reductase family 1 member B1 Homo sapiens (Human) PR
O60218 AKR1B10 Aldo-keto reductase family 1 member B10 Homo sapiens (Human) PR
P45376 Akr1b1 Aldo-keto reductase family 1 member B1 Mus musculus (Mouse) PR
P80276 AKR1B1 Aldo-keto reductase family 1 member B1 Sus scrofa (Pig) PR
P07943 Akr1b1 Aldo-keto reductase family 1 member B1 Rattus norvegicus (Rat) PR
Q84TF0 AKR4C10 Aldo-keto reductase family 4 member C10 Arabidopsis thaliana (Mouse-ear cress) PR
Q9M338 AKR4C11 Aldo-keto reductase family 4 member C11 Arabidopsis thaliana (Mouse-ear cress) PR
Q0PGJ6 AKR4C9 NADPH-dependent aldo-keto reductase, chloroplastic Arabidopsis thaliana (Mouse-ear cress) PR
O80944 AKR4C8 Aldo-keto reductase family 4 member C8 Arabidopsis thaliana (Mouse-ear cress) PR
10 20 30 40 50 60
MATFVELSTK AKMPIVGLGT WKSPPNQVKE AVKAAIDAGY RHIDCAYAYC NENEVGEAIQ
70 80 90 100 110 120
EKIKEKAVQR EDLFIVSKLW PTCFEKKLLK EAFQKTLTDL KLDYLDLYLI HWPQGLQPGK
130 140 150 160 170 180
ELFPKDDQGR ILTSKTTFLE AWEGMEELVD QGLVKALGVS NFNHFQIERL LNKPGLKHKP
190 200 210 220 230 240
VTNQVECHPY LTQEKLIQYC HSKGISVTAY SPLGSPDRPS AKPEDPSLLE DPKIKEIAAK
250 260 270 280 290 300
HEKTSAQVLI RFHIQRNVVV IPKSVTPSRI QENIQVFDFQ LSDEEMATIL SFNRNWRACL
310
LPETVNMEEY PYDAEY