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Protein

ADAMTS-like protein 3

Gene

ADAMTSL3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

GO - Molecular functioni

Complete GO annotation...

Enzyme and pathway databases

BioCyciZFISH:ENSG00000156218-MONOMER.
ReactomeiR-HSA-5083635. Defective B3GALTL causes Peters-plus syndrome (PpS).
R-HSA-5173214. O-glycosylation of TSR domain-containing proteins.

Names & Taxonomyi

Protein namesi
Recommended name:
ADAMTS-like protein 3
Short name:
ADAMTSL-3
Alternative name(s):
Punctin-2
Gene namesi
Name:ADAMTSL3
Synonyms:KIAA1233
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:14633. ADAMTSL3.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Organism-specific databases

DisGeNETi57188.
OpenTargetsiENSG00000156218.
PharmGKBiPA134934525.

Polymorphism and mutation databases

BioMutaiADAMTSL3.
DMDMi308153648.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 26Sequence analysisAdd BLAST26
ChainiPRO_000024968427 – 1691ADAMTS-like protein 3Add BLAST1665

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi87 ↔ 118By similarity
Disulfide bondi91 ↔ 123By similarity
Disulfide bondi102 ↔ 108By similarity
Glycosylationi293N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi576 ↔ 620By similarity
Disulfide bondi580 ↔ 625By similarity
Disulfide bondi591 ↔ 609By similarity
Glycosylationi681N-linked (GlcNAc...)Sequence analysis1
Glycosylationi797N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi831 ↔ 875By similarity
Disulfide bondi835 ↔ 880By similarity
Disulfide bondi846 ↔ 863By similarity
Glycosylationi915N-linked (GlcNAc...)Sequence analysis1
Glycosylationi927N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi934 ↔ 982By similarity
Glycosylationi1102N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1191N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1215 ↔ 1263By similarity
Glycosylationi1292N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1316N-linked (GlcNAc...)Sequence analysis1
Disulfide bondi1321 ↔ 1367By similarity
Glycosylationi1330N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1343N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1349N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1356N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1432N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1516N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1574N-linked (GlcNAc...)Sequence analysis1
Glycosylationi1591N-linked (GlcNAc...)Sequence analysis1

Post-translational modificationi

Glycosylated (By similarity). 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).By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiP82987.
PeptideAtlasiP82987.
PRIDEiP82987.

PTM databases

iPTMnetiP82987.
PhosphoSitePlusiP82987.

Expressioni

Tissue specificityi

Expressed in epithelial cells of the colon, fallopian tube, skin, breast, prostate, epididymis, liver, pancreatic islets and bile ducts, as well as by vascular endothelial cells, smooth muscle cells, fibroblasts, cortical and ganglionic neurons and cardiac myocytes. Also expressed by malignant epithelial cells in colon cancer, as well as breast, prostate, renal and skin tumors. Expression is significantly reduced in colon cancer compared to normal colon.2 Publications

Gene expression databases

BgeeiENSG00000156218.
CleanExiHS_ADAMTSL3.
GenevisibleiP82987. HS.

Organism-specific databases

HPAiHPA034773.
HPA034774.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
KRT40Q6A1623EBI-10221726,EBI-10171697
KRTAP10-8P604105EBI-10221726,EBI-10171774
KRTAP2-3P0C7H85EBI-10221726,EBI-10196781
MDFIQ997505EBI-10221726,EBI-724076
NOTCH2NLQ7Z3S93EBI-10221726,EBI-945833

Protein-protein interaction databases

BioGridi121437. 6 interactors.
IntActiP82987. 10 interactors.
MINTiMINT-3113527.
STRINGi9606.ENSP00000286744.

Structurei

3D structure databases

ProteinModelPortaliP82987.
SMRiP82987.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini75 – 124TSP type-1 1PROSITE-ProRule annotationAdd BLAST50
Domaini418 – 468TSP type-1 2PROSITE-ProRule annotationAdd BLAST51
Domaini478 – 535TSP type-1 3PROSITE-ProRule annotationAdd BLAST58
Domaini564 – 626TSP type-1 4PROSITE-ProRule annotationAdd BLAST63
Domaini703 – 760TSP type-1 5PROSITE-ProRule annotationAdd BLAST58
Domaini763 – 818TSP type-1 6PROSITE-ProRule annotationAdd BLAST56
Domaini819 – 881TSP type-1 7PROSITE-ProRule annotationAdd BLAST63
Domaini896 – 992Ig-like C2-type 1Add BLAST97
Domaini1185 – 1279Ig-like C2-type 2Add BLAST95
Domaini1296 – 1378Ig-like C2-type 3Add BLAST83
Domaini1424 – 1482TSP type-1 8PROSITE-ProRule annotationAdd BLAST59
Domaini1483 – 1545TSP type-1 9PROSITE-ProRule annotationAdd BLAST63
Domaini1597 – 1644TSP type-1 10PROSITE-ProRule annotationAdd BLAST48
Domaini1655 – 1691PLACPROSITE-ProRule annotationAdd BLAST37

Sequence similaritiesi

Contains 1 PLAC domain.PROSITE-ProRule annotation
Contains 10 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiENOG410INDC. Eukaryota.
ENOG410YY5R. LUCA.
GeneTreeiENSGT00760000118885.
HOGENOMiHOG000230906.
HOVERGENiHBG079989.
InParanoidiP82987.
OMAiMDTAQFD.
OrthoDBiEOG091G00BQ.
PhylomeDBiP82987.
TreeFamiTF351125.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR010909. PLAC.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF07679. I-set. 1 hit.
PF08686. PLAC. 1 hit.
PF00090. TSP_1. 9 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00209. TSP1. 12 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF82895. SSF82895. 12 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 10 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P82987-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MASWTSPWWV LIGMVFMHSP LPQTTAEKSP GAYFLPEFAL SPQGSFLEDT
60 70 80 90 100
TGEQFLTYRY DDQTSRNTRS DEDKDGNWDA WGDWSDCSRT CGGGASYSLR
110 120 130 140 150
RCLTGRNCEG QNIRYKTCSN HDCPPDAEDF RAQQCSAYND VQYQGHYYEW
160 170 180 190 200
LPRYNDPAAP CALKCHAQGQ NLVVELAPKV LDGTRCNTDS LDMCISGICQ
210 220 230 240 250
AVGCDRQLGS NAKEDNCGVC AGDGSTCRLV RGQSKSHVSP EKREENVIAV
260 270 280 290 300
PLGSRSVRIT VKGPAHLFIE SKTLQGSKGE HSFNSPGVFL VENTTVEFQR
310 320 330 340 350
GSERQTFKIP GPLMADFIFK TRYTAAKDSV VQFFFYQPIS HQWRQTDFFP
360 370 380 390 400
CTVTCGGGYQ LNSAECVDIR LKRVVPDHYC HYYPENVKPK PKLKECSMDP
410 420 430 440 450
CPSSDGFKEI MPYDHFQPLP RWEHNPWTAC SVSCGGGIQR RSFVCVEESM
460 470 480 490 500
HGEILQVEEW KCMYAPKPKV MQTCNLFDCP KWIAMEWSQC TVTCGRGLRY
510 520 530 540 550
RVVLCINHRG EHVGGCNPQL KLHIKEECVI PIPCYKPKEK SPVEAKLPWL
560 570 580 590 600
KQAQELEETR IATEEPTFIP EPWSACSTTC GPGVQVREVK CRVLLTFTQT
610 620 630 640 650
ETELPEEECE GPKLPTERPC LLEACDESPA SRELDIPLPE DSETTYDWEY
660 670 680 690 700
AGFTPCTATC VGGHQEAIAV CLHIQTQQTV NDSLCDMVHR PPAMSQACNT
710 720 730 740 750
EPCPPRWHVG SWGPCSATCG VGIQTRDVYC LHPGETPAPP EECRDEKPHA
760 770 780 790 800
LQACNQFDCP PGWHIEEWQQ CSRTCGGGTQ NRRVTCRQLL TDGSFLNLSD
810 820 830 840 850
ELCQGPKASS HKSCARTDCP PHLAVGDWSK CSVSCGVGIQ RRKQVCQRLA
860 870 880 890 900
AKGRRIPLSE MMCRDLPGLP LVRSCQMPEC SKIKSEMKTK LGEQGPQILS
910 920 930 940 950
VQRVYIQTRE EKRINLTIGS RAYLLPNTSV IIKCPVRRFQ KSLIQWEKDG
960 970 980 990 1000
RCLQNSKRLG ITKSGSLKIH GLAAPDIGVY RCIAGSAQET VVLKLIGTDN
1010 1020 1030 1040 1050
RLIARPALRE PMREYPGMDH SEANSLGVTW HKMRQMWNNK NDLYLDDDHI
1060 1070 1080 1090 1100
SNQPFLRALL GHCSNSAGST NSWELKNKQF EAAVKQGAYS MDTAQFDELI
1110 1120 1130 1140 1150
RNMSQLMETG EVSDDLASQL IYQLVAELAK AQPTHMQWRG IQEETPPAAQ
1160 1170 1180 1190 1200
LRGETGSVSQ SSHAKNSGKL TFKPKGPVLM RQSQPPSISF NKTINSRIGN
1210 1220 1230 1240 1250
TVYITKRTEV INILCDLITP SEATYTWTKD GTLLQPSVKI ILDGTGKIQI
1260 1270 1280 1290 1300
QNPTRKEQGI YECSVANHLG SDVESSSVLY AEAPVILSVE RNITKPEHNH
1310 1320 1330 1340 1350
LSVVVGGIVE AALGANVTIR CPVKGVPQPN ITWLKRGGSL SGNVSLLFNG
1360 1370 1380 1390 1400
SLLLQNVSLE NEGTYVCIAT NALGKAVATS VLHLLERRWP ESRIVFLQGH
1410 1420 1430 1440 1450
KKYILQATNT RTNSNDPTGE PPPQEPFWEP GNWSHCSATC GHLGARIQRP
1460 1470 1480 1490 1500
QCVMANGQEV SEALCDHLQK PLAGFEPCNI RDCPARWFTS VWSQCSVSCG
1510 1520 1530 1540 1550
EGYHSRQVTC KRTKANGTVQ VVSPRACAPK DRPLGRKPCF GHPCVQWEPG
1560 1570 1580 1590 1600
NRCPGRCMGR AVRMQQRHTA CQHNSSDSNC DDRKRPTLRR NCTSGACDVC
1610 1620 1630 1640 1650
WHTGPWKPCT AACGRGFQSR KVDCIHTRSC KPVAKRHCVQ KKKPISWRHC
1660 1670 1680 1690
LGPSCDRDCT DTTHYCMFVK HLNLCSLDRY KQRCCQSCQE G
Length:1,691
Mass (Da):188,692
Last modified:October 5, 2010 - v4
Checksum:i48C7281C737EA56E
GO
Isoform 2 (identifier: P82987-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1657-1691: RDCTDTTHYCMFVKHLNLCSLDRYKQRCCQSCQEG → STYTSQTATNKGAASHVKRDKPLEGS

Show »
Length:1,682
Mass (Da):187,240
Checksum:iEED57C7F66CA0CC6
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti265A → V in AAK15041 (PubMed:14667842).Curated1
Sequence conflicti986S → F in AAI28390 (PubMed:15489334).Curated1
Sequence conflicti1526A → S in AAI28390 (PubMed:15489334).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_027478146H → R.1 PublicationCorresponds to variant rs4483821dbSNPEnsembl.1
Natural variantiVAR_027479290L → V.1 PublicationCorresponds to variant rs4144691dbSNPEnsembl.1
Natural variantiVAR_035809330V → M in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_035810587R → H in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs142860011dbSNPEnsembl.1
Natural variantiVAR_027480661V → L.1 PublicationCorresponds to variant rs4842838dbSNPEnsembl.1
Natural variantiVAR_057365713G → R.Corresponds to variant rs34047645dbSNPEnsembl.1
Natural variantiVAR_035811855R → C in a colorectal cancer sample; somatic mutation. 1 PublicationCorresponds to variant rs146769560dbSNPEnsembl.1
Natural variantiVAR_027481855R → H.Corresponds to variant rs2277848dbSNPEnsembl.1
Natural variantiVAR_027482869L → F.1 PublicationCorresponds to variant rs2277849dbSNPEnsembl.1
Natural variantiVAR_0358121315A → E in a colorectal cancer sample; somatic mutation. 1 Publication1
Natural variantiVAR_0274831370T → A.Corresponds to variant rs17158450dbSNPEnsembl.1
Natural variantiVAR_0274841558M → T.Corresponds to variant rs7175910dbSNPEnsembl.1
Natural variantiVAR_0274851660T → I.Corresponds to variant rs950169dbSNPEnsembl.1
Natural variantiVAR_0274861679R → H.Corresponds to variant rs11857906dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0378101657 – 1691RDCTD…SCQEG → STYTSQTATNKGAASHVKRD KPLEGS in isoform 2. CuratedAdd BLAST35

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC087738 Genomic DNA. No translation available.
AC116157 Genomic DNA. No translation available.
AC027807 Genomic DNA. No translation available.
BC128389 mRNA. Translation: AAI28390.1.
BC128390 mRNA. Translation: AAI28391.1.
AF237652 mRNA. Translation: AAK15041.1.
AB033059 mRNA. Translation: BAA86547.1.
CCDSiCCDS10326.1. [P82987-1]
CCDS73773.1. [P82987-2]
RefSeqiNP_001288039.1. NM_001301110.1. [P82987-2]
NP_997400.2. NM_207517.2. [P82987-1]
UniGeneiHs.459162.

Genome annotation databases

EnsembliENST00000286744; ENSP00000286744; ENSG00000156218. [P82987-1]
ENST00000567476; ENSP00000456313; ENSG00000156218. [P82987-2]
GeneIDi57188.
KEGGihsa:57188.
UCSCiuc002bjz.5. human. [P82987-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC087738 Genomic DNA. No translation available.
AC116157 Genomic DNA. No translation available.
AC027807 Genomic DNA. No translation available.
BC128389 mRNA. Translation: AAI28390.1.
BC128390 mRNA. Translation: AAI28391.1.
AF237652 mRNA. Translation: AAK15041.1.
AB033059 mRNA. Translation: BAA86547.1.
CCDSiCCDS10326.1. [P82987-1]
CCDS73773.1. [P82987-2]
RefSeqiNP_001288039.1. NM_001301110.1. [P82987-2]
NP_997400.2. NM_207517.2. [P82987-1]
UniGeneiHs.459162.

3D structure databases

ProteinModelPortaliP82987.
SMRiP82987.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121437. 6 interactors.
IntActiP82987. 10 interactors.
MINTiMINT-3113527.
STRINGi9606.ENSP00000286744.

PTM databases

iPTMnetiP82987.
PhosphoSitePlusiP82987.

Polymorphism and mutation databases

BioMutaiADAMTSL3.
DMDMi308153648.

Proteomic databases

PaxDbiP82987.
PeptideAtlasiP82987.
PRIDEiP82987.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000286744; ENSP00000286744; ENSG00000156218. [P82987-1]
ENST00000567476; ENSP00000456313; ENSG00000156218. [P82987-2]
GeneIDi57188.
KEGGihsa:57188.
UCSCiuc002bjz.5. human. [P82987-1]

Organism-specific databases

CTDi57188.
DisGeNETi57188.
GeneCardsiADAMTSL3.
H-InvDBHIX0017599.
HGNCiHGNC:14633. ADAMTSL3.
HPAiHPA034773.
HPA034774.
MIMi609199. gene.
neXtProtiNX_P82987.
OpenTargetsiENSG00000156218.
PharmGKBiPA134934525.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410INDC. Eukaryota.
ENOG410YY5R. LUCA.
GeneTreeiENSGT00760000118885.
HOGENOMiHOG000230906.
HOVERGENiHBG079989.
InParanoidiP82987.
OMAiMDTAQFD.
OrthoDBiEOG091G00BQ.
PhylomeDBiP82987.
TreeFamiTF351125.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000156218-MONOMER.
ReactomeiR-HSA-5083635. Defective B3GALTL causes Peters-plus syndrome (PpS).
R-HSA-5173214. O-glycosylation of TSR domain-containing proteins.

Miscellaneous databases

GenomeRNAii57188.
PROiP82987.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000156218.
CleanExiHS_ADAMTSL3.
GenevisibleiP82987. HS.

Family and domain databases

Gene3Di2.60.40.10. 3 hits.
InterProiIPR007110. Ig-like_dom.
IPR013783. Ig-like_fold.
IPR013098. Ig_I-set.
IPR003599. Ig_sub.
IPR003598. Ig_sub2.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR010909. PLAC.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF07679. I-set. 1 hit.
PF08686. PLAC. 1 hit.
PF00090. TSP_1. 9 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00409. IG. 3 hits.
SM00408. IGc2. 3 hits.
SM00209. TSP1. 12 hits.
[Graphical view]
SUPFAMiSSF48726. SSF48726. 3 hits.
SSF82895. SSF82895. 12 hits.
PROSITEiPS50835. IG_LIKE. 3 hits.
PS50900. PLAC. 1 hit.
PS50092. TSP1. 10 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiATL3_HUMAN
AccessioniPrimary (citable) accession number: P82987
Secondary accession number(s): A1A566, A1A567, Q9ULI7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 19, 2006
Last sequence update: October 5, 2010
Last modified: November 30, 2016
This is version 107 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Caution

Although strongly similar to members of the ADAMTS family it lacks the metalloprotease and disintegrin-like domains which are typical of that family.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.