UniProt functional annotation for Q96JA1



	UniProt functional annotation for Q96JA1

UniProt code: Q96JA1.

Organism: Homo sapiens (Human).

Taxonomy: Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.

Function: Acts as a feedback negative regulator of signaling by receptor tyrosine kinases, through a mechanism that involves enhancement of receptor ubiquitination and accelerated intracellular degradation. {ECO:0000269|PubMed:15282549}.

Subunit: Interacts (via extracellular LRR and Ig-like domains) with EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 (via extracellular domain) (PubMed:15282549). The physiological relevance of the interaction is controversial; LRIG1 may have low affinity for EGFR, and interaction may occur only when high levels of both proteins are present (PubMed:25765764). {ECO:0000269|PubMed:15282549, ECO:0000269|PubMed:25765764}.

Subcellular location: Cell membrane {ECO:0000269|PubMed:15282549}; Single-pass type I membrane protein {ECO:0000305|PubMed:15282549}.

Tissue specificity: Widely expressed. {ECO:0000269|PubMed:11414704}.

Induction: By EGF. {ECO:0000269|PubMed:15282549}.

Domain: Contains LRR and Ig-domains that can mediate low-affinity interaction with EGFR (PubMed:25765764). The LRRs and the Ig-domains are each sufficient for EGFR/ERBB1 binding. This interaction is abolished only when both the LRRs and the Ig-domains are deleted (PubMed:15282549). {ECO:0000269|PubMed:15282549, ECO:0000269|PubMed:25765764}.

Annotations taken from UniProtKB at the EBI.


Organism:		Homo sapiens (Human).
Taxonomy:		Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.



Function:		Acts as a feedback negative regulator of signaling by receptor tyrosine kinases, through a mechanism that involves enhancement of receptor ubiquitination and accelerated intracellular degradation. {ECO:0000269\|PubMed:15282549}.


Subunit:		Interacts (via extracellular LRR and Ig-like domains) with EGFR/ERBB1, ERBB2, ERBB3 and ERBB4 (via extracellular domain) (PubMed:15282549). The physiological relevance of the interaction is controversial; LRIG1 may have low affinity for EGFR, and interaction may occur only when high levels of both proteins are present (PubMed:25765764). {ECO:0000269\|PubMed:15282549, ECO:0000269\|PubMed:25765764}.
Subcellular location:		Cell membrane {ECO:0000269\|PubMed:15282549}; Single-pass type I membrane protein {ECO:0000305\|PubMed:15282549}.
Tissue specificity:		Widely expressed. {ECO:0000269\|PubMed:11414704}.
Induction:		By EGF. {ECO:0000269\|PubMed:15282549}.
Domain:		Contains LRR and Ig-domains that can mediate low-affinity interaction with EGFR (PubMed:25765764). The LRRs and the Ig-domains are each sufficient for EGFR/ERBB1 binding. This interaction is abolished only when both the LRRs and the Ig-domains are deleted (PubMed:15282549). {ECO:0000269\|PubMed:15282549, ECO:0000269\|PubMed:25765764}.