Component

Rat sodium/imino-acid transporter 1 / Slc6a20

Context-specific entity; species, compartment and exposure are stated on each claim.

1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What it acts on

  1. Rat SIT1 expressed in Xenopus oocytes transported proline with apparent K0.5 about 0.2 mM; transport depended on sodium, was stimulated by chloride and depended on voltage.

    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Rat protein in Xenopus oocytes; alanine and lysine did not inhibit the reported proline transport.
    limitations
    This is not a human dietary sodium or chloride threshold.
    nutrient_topic
    L-Proline collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Proline
    plain_language
    The driving ions and membrane voltage affect how this transporter works.
    primary_references
    Identification of mammalian proline transporter SIT1 (SLC6A20) with characteristics of classical system imino. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15632147/ · DOI 10.1074/jbc.M413027200
    transport_effect
    raises Sodium-dependent, chloride-stimulated, voltage-dependent proline transport, which is inward.
    transport_pool
    the expressing cell Sodium-dependent, chloride-stimulated, voltage-dependent proline transport, which is inward.

    L-Proline: synthesis, collagen processing, redox metabolism and cross-nutrient mechanisms (2026-09-19) · lines 174–180

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Rat protein in Xenopus oocytes; alanine and lysine did not inhibit the reported proline transport. · source_derived_draft · unverified_draft

    ## l-proline-rat-sit1-ion-coupling The driving ions and membrane voltage affect how this transporter works. Rat SIT1 expressed in Xenopus oocytes transported proline with apparent K0.5 about 0.2 mM; transport depended on sodium, was stimulated by chloride and depended on voltage. Model: Rat protein in Xenopus oocytes; alanine and lysine did not inhibit the reported proline transport. Limitations: This is not a human dietary sodium or chloride threshold. Evidence access: Primary abstract Identification of mammalian proline transporter SIT1 (SLC6A20) with characteristics of classical system imino. · 2005 · https://pubmed.ncbi.nlm.nih.gov/15632147/ · DOI 10.1074/jbc.M413027200
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards