Protein detail

COPT1

High affinity copper uptake protein 1 (Copper transporter 1) (hCTR1) (Solute carrier family 31 member 1) [Cleaved into: Truncated CTR1 form]

Protein symbol COPT1	UniProt ID O15431	EVMP score 0.38
Frequency	Transmembrane count 3	Protein classification Metabolic proteinsPredicted membrane proteinsTransporters

Basic Information

Protein Names

High affinity copper uptake protein 1 (Copper transporter 1) (hCTR1) (Solute carrier family 31 member 1) [Cleaved into: Truncated CTR1 form]

Protein Class

Metabolic proteinsPredicted membrane proteinsTransporters

Protein Function

Transporters:Transporter channels and pores

Transmembrane

62..82; Helical; 133..153; Helical; 157..177; Helical

Transmembrane Count

Ensembl

ENSG00000136868

Entrez Gene Symbol

SLC31A1

Gene Synonym

COPT1CTR1hCTR1

Gene Description

Solute carrier family 31 member 1

Chromosome

Position

113221544-113264492

EVMP Score

0.38

Fluorescence & Localization

Function & Pathway

Protein Function

Transporters:Transporter channels and pores

Cellular Component

Molecular Function

Biological Process

KEGG

Reactome

Canonical Pathways

M3008 Naba ecm glycoproteins
M5884 Naba core matrisome
M5889 Naba matrisome

Mediation Categories

Clinical-translation mediationFusion and delivery mediation

Relations & Evidence

Enzyme-Mediated Modification

0 records.

Ligand-Receptor Signaling

24 records.

Category	Parent	Database	Transmitter	Receiver	Secreted	Plasma Membrane (Transmembrane)	Plasma Membrane (Peripheral)
receptor	receptor	OmniPath	No	Yes	No	No	No
intracellular	intracellular	GO_Intercell	No	No	No	No	No
intracellular	intracellular	UniProt_location	No	No	No	No	No
intracellular	intracellular	OmniPath	No	No	No	No	No
transporter	transporter	Surfaceome	No	Yes	No	No	No
solute_carrier	transporter	Almen2009	No	Yes	No	No	No
slc31	transporter	Surfaceome	No	Yes	No	No	No
slc	transporter	Surfaceome	No	Yes	No	No	No
transporter	transporter	OmniPath	No	Yes	No	No	No
transmembrane	transmembrane	UniProt_location	No	No	No	No	No

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Regulatory Interaction Network

0 records.

Protein Complex Composition

0 records.

Isolation & Detection Technology

1 record.

EV Isolation Method	Detection Method	Number of References	References
Differential UltracentrifugationUltrafiltration / Tangential Flow FiltrationSize Exclusion ChromatographyImmunoaffinity CaptureMicrofluidics-Based Methods	Mass spectrometry	55	31685984 34401050 34754007 36406491 37862381 38173217 38937789 39949490 39766158 31508500 34681663 38225453 38556629 39436214 39873726 10451508 40945317 40545963 40185859 32795414 38731868 26775013 22329422 25844599 27723984 28242843 29242380 30071318 30287549 33017416 34202855 36362114 39022990 39478498 40619995 40750896 24657793 30975894 31715689 38490958 39569406 41201090 34876625 33023655 28396511 30760538 35111156 31759091 39001700 40311616 40091455 38136601 38564289 32231660 24069378

Sequence, Structure & Domains

Sequences

Length

190

Mass

21,091

Sequence

MDHSHHMGMSYMDSNSTMQPSHHHPTTSASHSHGGGDSSMMMMPMTFYFGFKNVELLFSGLVINTAGEMAGAFVAVFLLAMFYEGLKIARESLLRKSQVSIRYNSMPVPGPNGTILMETHKTVGQQMLSFPHLLQTVLHIIQVVISYFLMLIFMTYNGYLCIAVAAGAGTGYFLFSWKKAVVVDITEHCH

3D Structural Models

Turn

83..85

Helix

67..82; 134..155; 163..168; 174..177

Beta Strand

160..162

3D Structure

NMR spectroscopy (3)

Domain & Motif Annotations

Compositional Bias

26..35; Low complexity

Motif

5..6; Bis-His motif; 7..12; Methionine segments (Mets) motif

Domain (CC)

The C-terminal domain mediates copper(1+) binding (PubMed:26745413) and is involved in the copper(1+)-dependent-ATOX1 interaction (PubMed:24837030, PubMed:26745413). The C-terminal domain appears to act to limit transport through the pore by regulating the rate of exit of copper ions at the intracellular side (PubMed:23658018). The N-terminal domain can collect copper(2+) from copper(2+) carriers in blood (PubMed:30489586). The N-terminal domain, in the trimeric arrangement, tunes its reactivity with copper, promoting copper(2+) reduction and copper(1+) stabilization thanks to the presence of histidine (His) and methionine (Met) motifs (PubMed:32914794, Ref.24). The bis-His motif directly coordinate to copper(2+), whereas the Mets motif is involved in copper(1+) binding (Ref.24). The ligand switching between the bis-His motif and the Mets motif is regulated by pH (PubMed:35601835).

Region

1..35; Disordered

Protein Families

Copper transporter (Ctr) (TC 1.A.56) family
SLC31A subfamily

Sequence Similarities

Belongs to the copper transporter (Ctr) (TC 1.A.56) family. SLC31A subfamily.

Clinical Relevance

Disease Involvement

EpilepsyNeurodegeneration

Drug Targets

Literature-reported target

Drugs

CARBOPLATIN

Antibody

HPA013810

Interaction Protein

ENSG00000100422ENSG00000134575ENSG00000149541ENSG00000170832ENSG00000204128

Interaction Count

Interaction Dataset

biogrid_bioplex