About Dark Proteome Database  

DPD

Simplifying the generation of insight from protein structures

Nelson Perdigão1,2, Agostinho Rosa1,2, Seán I. O’Donoghue3

Updated: June 2016
This indicates when the Dark Proteome Database (DPD) was last calculated.
PDB structures released since then are not yet available in DPD.

1. University of Lisbon, Portugal
2. Instituto de Sistemas e Robótica, Lisboa, Portugal
3. Garvan Institute of Medical Research, Sydney, Australia

Q9H324 Overview

Primary Accession: Q9H324

Color: Grey

Darkness: 0.2765186

Darkness Potential: 0.2765186

Length 1103

Organism: 9606

Domain: Eukaryota

Kingdom: Metazoa

Q9H324 Sequence

MAPACQILRWALALGLGLMFEVTHAFRSQDEFLSSLESYEIAFPTRVDHNGALLAFSPPPPRRQRRGTGATAESRLFYKVASPSTHFLLNLTRSSRLLAGHVSVEYWTREGLAWQRAARPHCLYAGHLQGQASTSHVAISTCGGLHGLIVADEEEYLIEPLHGGPKGSRSPEESGPHVVYKRSSLRHPHLDTACGVRDEKPWKGRPWWLRTLKPPPARPLGNETERGQPGLKRSVSRERYVETLVVADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNILVTRLILLTEDQPTLEITHHAGKSLDSFCKWQKSIVNHSGHGNAIPENGVANHDTAVLITRYDICIYKNKPCGTLGLAPVGGMCERERSCSVNEDIGLATAFTIAHEIGHTFGMNHDGVGNSCGARGQDPAKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGLCLNNRPPRQDFVYPTVAPGQAYDADEQCRFQHGVKSRQCKYGEVCSELWCLSKSNRCITNSIPAAEGTLCQTHTIDKGWCYKRVCVPFGSRPEGVDGAWGPWTPWGDCSRTCGGGVSSSSRHCDSPRPTIGGKYCLGERRRHRSCNTDDCPPGSQDFREVQCSEFDSIPFRGKFYKWKTYRGGGVKACSLTCLAEGFNFYTERAAAVVDGTPCRPDTVDICVSGECKHVGCDRVLGSDLREDKCRVCGGDGSACETIEGVFSPASPGAGYEDVVWIPKGSVHIFIQDLNLSLSHLALKGDQESLLLEGLPGTPQPHRLPLAGTTFQLRQGPDQVQSLEALGPINASLIVMVLARTELPALRYRFNAPIARDSLPPYSWHYAPWTKCSAQCAGGSQVQAVECRNQLDSSAVAPHYCSAHSKLPKRQRACNTEPCPPDWVVGNWSLCSRSCDAGVRSRSVVCQRRVSAAEEKALDDSACPQPRPPVLEACHGPTCPPEWAALDWSECTPSCGPGLRHRVVLCKSADHRATLPPAHCSPAAKPPATMRCNLRRCPPARWVAGEWGECSAQCGVGQRQRSVRCTSHTGQASHECTEALRPPTTQQCEAKCDSPTPGDGPEECKDVNKVAYCPLVLKFQFCSRAYFRQMCCKTCHGH

Q9H324 Description

FUNCTION: Metalloprotease that participate in microfibrils assembly. Microfibrils are extracellular matrix components occurring independently or along with elastin in the formation of elastic tissues. {ECO:0000269|PubMed:21402694}.
COFACTOR: Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; Note=Binds 1 zinc ion per subunit. {ECO:0000250};
SUBUNIT: Interacts with FBN1; this interaction promotes microfibrils assembly. {ECO:0000269|PubMed:21402694}.
SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular matrix {ECO:0000269|PubMed:21402694}.
ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=2; Name=1; IsoId=Q9H324-1; Sequence=Displayed; Name=2; IsoId=Q9H324-2; Sequence=VSP_054707; Note=No experimental confirmation available. Gene prediction based on partial mRNA and EST data.;
TISSUE SPECIFICITY: Widely expressed in adult tissues. {ECO:0000269|PubMed:15355968}.
DOMAIN: The spacer domain and the TSP type-1 domains are important for a tight interaction with the extracellular matrix. {ECO:0000250}.
PTM: Glycosylated. Can be O-fucosylated by POFUT2 on a serine or a threonine residue found within the consensus sequence C1-X(2)-(S/T)-C2-G of the TSP type-1 repeat domains where C1 and C2 are the first and second cysteine residue of the repeat, respectively. Fucosylated repeats can then be further glycosylated by the addition of a beta-1,3-glucose residue by the glucosyltransferase, B3GALTL. Fucosylation mediates the efficient secretion of ADAMTS family members. Also can be C-glycosylated with one or two mannose molecules on tryptophan residues within the consensus sequence W-X-X-W of the TPRs, and N-glycosylated. These other glycosylations can also facilitate secretion (By similarity). {ECO:0000250}.
DISEASE: Weill-Marchesani syndrome 1 (WMS1) [MIM:277600]: A rare connective tissue disorder characterized by short stature, brachydactyly, joint stiffness, and eye abnormalities including microspherophakia, ectopia lentis, severe myopia and glaucoma. {ECO:0000269|PubMed:15368195, ECO:0000269|PubMed:18567016}. Note=The disease is caused by mutations affecting the gene represented in this entry.
SIMILARITY: Contains 1 disintegrin domain. {ECO:0000305}.
SIMILARITY: Contains 1 peptidase M12B domain. {ECO:0000255|PROSITE-ProRule:PRU00276}.
SIMILARITY: Contains 1 PLAC domain. {ECO:0000255|PROSITE-ProRule:PRU00233}.
SIMILARITY: Contains 5 TSP type-1 domains. {ECO:0000255|PROSITE-ProRule:PRU00210}.

Q9H324 Features

Number of Swiss-Prot Features: 44

Swiss-Prot Features:

var_seq,,off,,, {
var_seq_1,,MAPACQILRWALALGLGLMFEVTHAFRSQDEFLSSLESYEI AFPTRVDHNGALLAFSPPPPRRQRRGTGATAESRLFYKVAS PSTHFLLNLTRSSRLLAGHVSVEYWTREGLAWQRAARPHCL YAGHLQGQASTSHVAISTCGGLHGLIVADEEEYLIEPLHGG PKGSRSPEESGPHVVYKRSSLRHPHLDTACGVRDEKPWKGR PWWLRTLKPPPARPLGNETERGQPGLKRSVSRERYVETLVV ADKMMVAYHGRRDVEQYVLAIMNIVAKLFQDSSLGSTVNIL VTRLILLTEDQPTLEITHHAGKSLDSFCKWQKSIVNHSGHG NAIPENGVANHDTAVLITRYDICIYKNKPCGTLGLAPVGGM CERERSCSVNEDIGLATAFTIAHEIGHTFGMNHDGVGNSCG ARGQDPAKLMAAHITMKTNPFVWSSCSRDYITSFLDSGLGL CLNNRPPRQDFVYPTVAPGQAYDADEQCRFQHGVKSRQCKY GEVCSELWCLSKSNRCITNSIPAAEGTLCQTHTIDKGWCYK RVCVPFGSRPEGVDGAWGPWTPWGDCSRTCGGGVSSSSRHC DSPRPTIGGKYCLGERRRHRSCNTDDCPPGSQDFREVQCSE FDSIPFRGKFYKWKTYRGGGVK -> MGPTSVLRAGLTPSC LPPPSGATNGSVSPLGRAQRVWTEPGGRGLHGATAAGPVAA ACPLLAVTATAPGQPSGASTVWVREGGTAPATRMTVPLAPR TSEKCSVLNLTASLSVGNSTSGKRTGE (in isoform 2). {ECO:0000305}. /FTId=VSP_054707.,,1:637;
}
carbohyd,,off,,, {
carbohyd_1,,N-linked (GlcNAc...). {ECO:0000255},,90:90;
carbohyd_2,,N-linked (GlcNAc...). {ECO:0000255},,222:222;
carbohyd_3,,N-linked (GlcNAc...). {ECO:0000255},,323:323;
carbohyd_4,,N-linked (GlcNAc...). {ECO:0000255},,740:740;
carbohyd_5,,N-linked (GlcNAc...). {ECO:0000255},,795:795;
carbohyd_6,,N-linked (GlcNAc...). {ECO:0000255},,892:892;
}
variant,,off,,, {
variant_1,,R -> Q (in dbSNP:rs3814291) /FTId=VAR_054440.,,119:119;
variant_2,,T -> S (in dbSNP:rs7255721) {ECO:0000269|PubMed:15355968}. /FTId=VAR_054441.,,134:134;
}
propep,,off,,, {
propep_1,,{ECO:0000250} /FTId=PRO_0000029184.,,26:233;
}
disulfid,,off,,, {
disulfid_1,,{ECO:0000250},,315:376;
disulfid_2,,{ECO:0000250},,351:358;
disulfid_3,,{ECO:0000250},,370:452;
disulfid_4,,{ECO:0000250},,409:436;
disulfid_5,,{ECO:0000250},,479:501;
disulfid_6,,{ECO:0000250},,490:508;
disulfid_7,,{ECO:0000250},,496:531;
disulfid_8,,{ECO:0000250},,521:536;
disulfid_9,,{ECO:0000250},,559:596;
disulfid_10,,{ECO:0000250},,563:601;
disulfid_11,,{ECO:0000250},,574:586;
}
conflict,,off,,, {
conflict_1,,AT -> PQ (in Ref. 2; AAG35563) {ECO:0000305}.,,385:386;
conflict_2,,S -> N (in Ref. 2; AAG35563) {ECO:0000305}.,,437:437;
conflict_3,,C -> S (in Ref. 2; AAG35563) {ECO:0000305}.,,643:643;
conflict_4,,H -> Q (in Ref. 2; AAG35563) {ECO:0000305}.,,1101:1101;
}
region,,off,,, {
region_1,,Spacer,,706:828;
}
compbias,,off,,, {
compbias_1,,Poly-Pro,,58:61;
compbias_2,,Poly-Ser,,568:571;
compbias_3,,Cys-rich,,604:705;
}
chain,,off,,,color {
chain_1,,A disintegrin and metalloproteinase with thrombospondin motifs 10. /FTId=PRO_0000029185.,,234:1103;
}
act_site,,off,,, {
act_site_1,,{ECO:0000255|PROSITE-ProRule:PRU00276, ECO:0000255|PROSITE-ProRule:PRU10095}.,,393:393;
}
domain,,off,,,color {
domain_1,,Peptidase M12B. {ECO:0000255|PROSITE-ProRule:PRU00276}.,,239:457;
domain_2,,Disintegrin,,460:546;
domain_3,,TSP type-1 1. {ECO:0000255|PROSITE-ProRule:PRU00210}.,,547:602;
domain_4,,TSP type-1 2. {ECO:0000255|PROSITE-ProRule:PRU00210}.,,825:883;
domain_5,,TSP type-1 3. {ECO:0000255|PROSITE-ProRule:PRU00210}.,,884:945;
domain_6,,TSP type-1 4. {ECO:0000255|PROSITE-ProRule:PRU00210}.,,947:1001;
domain_7,,TSP type-1 5. {ECO:0000255|PROSITE-ProRule:PRU00210}.,,1003:1058;
domain_8,,PLAC. {ECO:0000255|PROSITE-ProRule:PRU00233}.,,1065:1103;
}
signal,,off,,, {
signal_1,,{ECO:0000255},,1:25;
}
variant in WMS1,,off,,, {
variant in WMS1_1,,A -> T (in WMS1; shows consistent and significantly diminished protein secretion). {ECO:0000269|PubMed:18567016}. /FTId=VAR_054439.,,25:25;
}
metal,,off,,, {
metal_1,,Zinc; catalytic. {ECO:0000250},,392:392;
metal_2,,Zinc; catalytic. {ECO:0000250},,396:396;
metal_3,,Zinc; catalytic. {ECO:0000250},,402:402;
}





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