U.S. flag

An official website of the United States government

Format
Items per page
Sort by

Send to:

Choose Destination

Links from Protein

Items: 7

1.

VPS10 domain-containing protein

Sortilin, also known in mammals as neurotensin receptor-3, is the archetypical member of a Vps10-domain (Vps10-D) that binds neurotrophic factors and neuropeptides. This domain constitutes the entire luminal part of Sortilin and is activated in the trans-Golgi network by enzymatic propeptide cleavage [1,2]. The structure of the domain has been determined as a ten-bladed propeller, with up to 9 BNR or beta-hairpin turns in it. The mature receptor binds various ligands, including its own propeptide (Sort-pro), neurotensin, the pro-forms of nerve growth factor-beta (NGF)6 and brain-derived neurotrophic factor (BDNF)7, lipoprotein lipase (LpL), apo lipoprotein AV14 and the receptor-associated protein (RAP)1 [4,5]. [1]. 9013611. Molecular identification of a novel candidate sorting receptor purified from human brain by receptor-associated protein affinity chromatography. Petersen CM, Nielsen MS, Nykjaer A, Jacobsen L, Tommerup N, Rasmussen HH, Roigaard H, Gliemann J, Madsen P, Moestrup SK;. J Biol Chem. 1997;272:3599-3605. [2]. 9756851. The 100-kDa neurotensin receptor is gp95/sortilin, a non-G-protein-coupled receptor. Mazella J, Zsurger N, Navarro V, Chabry J, Kaghad M, Caput D, Ferrara P, Vita N, Gully D, Maffrand JP, Vincent JP;. J Biol Chem. 1998;273:26273-26276. [3]. 10085125. Sortilin/neurotensin receptor-3 binds and mediates degradation of lipoprotein lipase. Nielsen MS, Jacobsen C, Olivecrona G, Gliemann J, Petersen CM;. J Biol Chem. 1999;274:8832-8836. [4]. 19122660. Ligands bind to Sortilin in the tunnel of a ten-bladed beta-propeller domain. Quistgaard EM, Madsen P, Groftehauge MK, Nissen P, Petersen CM, Thirup SS;.. TRUNCATED at 1650 bytes (from Pfam)

Date:
2024-11-24
Family Accession:
NF027232.5
Method:
HMM
2.

BNR/Asp-box repeat protein

Members of this family contain multiple BNR (bacterial neuraminidase repeat) repeats or Asp-boxes. The repeats are short, however the repeats are never found closer than 40 residues together suggesting that the repeat is structurally longer. These repeats are found in many glycosyl hydrolases as well as other extracellular proteins of unknown function. [1]. 2562507. Conserved sequences in bacterial and viral sialidases. Roggentin P, Rothe B, Kaper JB, Galen J, Lawrisuk L, Vimr ER, Schauer R;. Glycoconj J 1989;6:349-353. [2]. 11266614. Sialidase-like Asp-boxes: sequence-similar structures within different protein folds. Copley RR, Russell RB, Ponting CP;. Protein Sci 2001;10:285-292. (from Pfam)

Date:
2024-10-16
Family Accession:
NF014110.5
Method:
HMM
3.
new record, indexing in progress
Family Accession:
4.
new record, indexing in progress
Family Accession:
5.
new record, indexing in progress
Family Accession:
6.
new record, indexing in progress
Family Accession:
7.

WD40/YVTN/BNR-like repeat-containing protein

WD40/YVTN/BNR-like repeat-containing protein similar to plant photosynthesis system II assembly factor Ycf48, and some glycosylhydrolases

Date:
2024-05-17
Family Accession:
11468233
Method:
Sparcle
Format
Items per page
Sort by

Send to:

Choose Destination

Supplemental Content

Find related data

Recent activity

Your browsing activity is empty.

Activity recording is turned off.

Turn recording back on

See more...
Support Center