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Protein

A disintegrin and metalloproteinase with thrombospondin motifs gon-1

Gene

gon-1

Organism
Caenorhabditis elegans
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Secreted metalloprotease required for distal tip cell (DTC) migration along the body wall basement membranes, a key step that promotes gonad morphogenesis. Probably acts by remodeling the basement membrane during cell migration. Has a protease-independent function in promoting the transport from the endoplasmic reticulum to the Golgi apparatus of a variety of secretory cargos.4 Publications

Cofactori

Zn2+By similarityNote: Binds 1 zinc ion per subunit.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi424 – 4241Zinc; catalyticBy similarity
Active sitei425 – 4251
Metal bindingi428 – 4281Zinc; catalyticBy similarity
Metal bindingi434 – 4341Zinc; catalyticBy similarity

GO - Molecular functioni

  • metalloendopeptidase activity Source: InterPro
  • metallopeptidase activity Source: WormBase
  • zinc ion binding Source: InterPro

GO - Biological processi

  • cell migration Source: WormBase
  • ER to Golgi vesicle-mediated transport Source: WormBase
  • gonad development Source: WormBase
  • protein transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Metalloprotease, Protease

Keywords - Biological processi

ER-Golgi transport, Protein transport, Transport

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM12.135.

Names & Taxonomyi

Protein namesi
Recommended name:
A disintegrin and metalloproteinase with thrombospondin motifs gon-1 (EC:3.4.24.-)
Short name:
ADAMTS gon-1
Alternative name(s):
Abnormal gonad development protein 1
Gene namesi
Name:gon-1
ORF Names:F25H8.3
OrganismiCaenorhabditis elegans
Taxonomic identifieri6239 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
Proteomesi
  • UP000001940 Componenti: Chromosome IV

Organism-specific databases

WormBaseiF25H8.3a; CE42668; WBGene00001650; gon-1.

Subcellular locationi

GO - Cellular componenti

  • basement membrane Source: UniProtKB-SubCell
  • cell Source: WormBase
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • Golgi apparatus Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Basement membrane, Endoplasmic reticulum, Extracellular matrix, Golgi apparatus, Secreted

Pathology & Biotechi

Disruption phenotypei

down-regulation of gon-1 in distal tip cells results in deformation of ER structure and inhibition of protein secretion which are rescued upon GON-domain expression.1 Publication

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi425 – 4251E → A: Loss of function; abolishes DTCs migration or gonad arm extension. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2828Sequence analysisAdd
BLAST
Chaini29 – 21502122A disintegrin and metalloproteinase with thrombospondin motifs gon-1PRO_0000250561Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi134 – 1341N-linked (GlcNAc...)Sequence analysis
Glycosylationi213 – 2131N-linked (GlcNAc...)Sequence analysis
Glycosylationi243 – 2431N-linked (GlcNAc...)Sequence analysis
Glycosylationi248 – 2481N-linked (GlcNAc...)Sequence analysis
Disulfide bondi402 ↔ 488By similarity
Disulfide bondi440 ↔ 470By similarity
Disulfide bondi600 ↔ 637By similarity
Disulfide bondi604 ↔ 642By similarity
Disulfide bondi615 ↔ 627By similarity
Glycosylationi842 – 8421N-linked (GlcNAc...)Sequence analysis
Glycosylationi1139 – 11391N-linked (GlcNAc...)Sequence analysis
Glycosylationi1199 – 11991N-linked (GlcNAc...)Sequence analysis
Glycosylationi1370 – 13701N-linked (GlcNAc...)Sequence analysis
Glycosylationi1432 – 14321N-linked (GlcNAc...)2 Publications
Glycosylationi1528 – 15281N-linked (GlcNAc...)Sequence analysis
Glycosylationi1590 – 15901N-linked (GlcNAc...)Sequence analysis
Glycosylationi1606 – 16061N-linked (GlcNAc...)Sequence analysis
Glycosylationi1654 – 16541N-linked (GlcNAc...)Sequence analysis
Disulfide bondi1679 ↔ 1718By similarity
Disulfide bondi1690 ↔ 1730By similarity
Disulfide bondi1694 ↔ 1735By similarity
Glycosylationi1828 – 18281N-linked (GlcNAc...)Sequence analysis
Glycosylationi1855 – 18551N-linked (GlcNAc...)Sequence analysis
Glycosylationi1942 – 19421N-linked (GlcNAc...)Sequence analysis
Glycosylationi1960 – 19601N-linked (GlcNAc...)Sequence analysis
Glycosylationi1997 – 19971N-linked (GlcNAc...)Sequence analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

PaxDbiQ19791.

Expressioni

Tissue specificityi

Expressed by both the gonadal DTC and the nongonadal body wall muscles.1 Publication

Developmental stagei

In hermaphrodites, it is first expressed in gonads in L2 larvae and is limited to the DTCs. Continues to be expressed in DTCs through L4, but is faint or not present in the adult. Also expressed in muscle cells throughout development.1 Publication

Gene expression databases

ExpressionAtlasiQ19791. baseline.

Interactioni

Protein-protein interaction databases

STRINGi6239.F25H8.3b.

Structurei

3D structure databases

ProteinModelPortaliQ19791.
SMRiQ19791. Positions 281-760, 1483-1556.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini280 – 493214Peptidase M12BPROSITE-ProRule annotationAdd
BLAST
Domaini503 – 58785DisintegrinAdd
BLAST
Domaini588 – 64356TSP type-1 1PROSITE-ProRule annotationAdd
BLAST
Domaini943 – 100361TSP type-1 2PROSITE-ProRule annotationAdd
BLAST
Domaini1004 – 105754TSP type-1 3PROSITE-ProRule annotationAdd
BLAST
Domaini1060 – 111556TSP type-1 4PROSITE-ProRule annotationAdd
BLAST
Domaini1116 – 116550TSP type-1 5PROSITE-ProRule annotationAdd
BLAST
Domaini1168 – 122760TSP type-1 6PROSITE-ProRule annotationAdd
BLAST
Domaini1228 – 127750TSP type-1 7PROSITE-ProRule annotationAdd
BLAST
Domaini1280 – 133960TSP type-1 8PROSITE-ProRule annotationAdd
BLAST
Domaini1352 – 140958TSP type-1 9PROSITE-ProRule annotationAdd
BLAST
Domaini1410 – 146960TSP type-1 10PROSITE-ProRule annotationAdd
BLAST
Domaini1474 – 152451TSP type-1 11PROSITE-ProRule annotationAdd
BLAST
Domaini1527 – 158559TSP type-1 12PROSITE-ProRule annotationAdd
BLAST
Domaini1621 – 167555TSP type-1 13PROSITE-ProRule annotationAdd
BLAST
Domaini1678 – 173659TSP type-1 14PROSITE-ProRule annotationAdd
BLAST
Domaini1737 – 179357TSP type-1 15PROSITE-ProRule annotationAdd
BLAST
Domaini1794 – 186673TSP type-1 16PROSITE-ProRule annotationAdd
BLAST
Domaini1867 – 192458TSP type-1 17PROSITE-ProRule annotationAdd
BLAST
Domaini1924 – 2123200GONPROSITE-ProRule annotationAdd
BLAST

Domaini

The GON domain mediates protease-independent function in ER to Golgi transport.

Sequence similaritiesi

Contains 1 disintegrin domain.Curated
Contains 1 GON domain.PROSITE-ProRule annotation
Contains 1 peptidase M12B domain.PROSITE-ProRule annotation
Contains 17 TSP type-1 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Signal

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004798.
InParanoidiQ19791.
PhylomeDBiQ19791.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR012314. Pept_M12B_GON-ADAMTSs.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF08685. GON. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 14 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 18 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 16 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS51046. GON. 1 hit.
PS50092. TSP1. 15 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q19791-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MRSIGGSFHL LQPVVAALIL LVVCLVYALQ SGSGTISEFS SDVLFSRAKY
60 70 80 90 100
SGVPVHHSRW RQDAGIHVID SHHIVRRDSY GRRGKRDVTS TDRRRRLQGV
110 120 130 140 150
ARDCGHACHL RLRSDDAVYI VHLHRWNQIP DSHNKSVPHF SNSNFAPMVL
160 170 180 190 200
YLDSEEEVRG GMSRTDPDCI YRAHVKGVHQ HSIVNLCDSE DGLYGMLALP
210 220 230 240 250
SGIHTVEPII SGNGTEHDGA SRHRQHLVRK FDPMHFKSFD HLNSTSVNET
260 270 280 290 300
ETTVATWQDQ WEDVIERKAR SRRAANSWDH YVEVLVVADT KMYEYHGRSL
310 320 330 340 350
EDYVLTLFST VASIYRHQSL RASINVVVVK LIVLKTENAG PRITQNAQQT
360 370 380 390 400
LQDFCRWQQY YNDPDDSSVQ HHDVAILLTR KDICRSQGKC DTLGLAELGT
410 420 430 440 450
MCDMQKSCAI IEDNGLSAAF TIAHELGHVF SIPHDDERKC STYMPVNKNN
460 470 480 490 500
FHIMAPTLEY NTHPWSWSPC SAGMLERFLE NNRGQTQCLF DQPVERRYYE
510 520 530 540 550
DVFVRDEPGK KYDAHQQCKF VFGPASELCP YMPTCRRLWC ATFYGSQMGC
560 570 580 590 600
RTQHMPWADG TPCDESRSMF CHHGACVRLA PESLTKIDGQ WGDWRSWGEC
610 620 630 640 650
SRTCGGGVQK GLRDCDSPKP RNGGKYCVGQ RERYRSCNTQ ECPWDTQPYR
660 670 680 690 700
EVQCSEFNNK DIGIQGVAST NTHWVPKYAN VAPNERCKLY CRLSGSAAFY
710 720 730 740 750
LLRDKVVDGT PCDRNGDDIC VAGACMPAGC DHQLHSTLRR DKCGVCGGDD
760 770 780 790 800
SSCKVVKGTF NEQGTFGYNE VMKIPAGSAN IDIRQKGYNN MKEDDNYLSL
810 820 830 840 850
RAANGEFLLN GHFQVSLARQ QIAFQDTVLE YSGSDAIIER INGTGPIRSD
860 870 880 890 900
IYVHVLSVGS HPPDISYEYM TAAVPNAVIR PISSALYLWR VTDTWTECDR
910 920 930 940 950
ACRGQQSQKL MCLDMSTHRQ SHDRNCQNVL KPKQATRMCN IDCSTRWITE
960 970 980 990 1000
DVSSCSAKCG SGQKRQRVSC VKMEGDRQTP ASEHLCDRNS KPSDIASCYI
1010 1020 1030 1040 1050
DCSGRKWNYG EWTSCSETCG SNGKMHRKSY CVDDSNRRVD ESLCGREQKE
1060 1070 1080 1090 1100
ATERECNRIP CPRWVYGHWS ECSRSCDGGV KMRHAQCLDA ADRETHTSRC
1110 1120 1130 1140 1150
GPAQTQEHCN EHACTWWQFG VWSDCSAKCG DGVQYRDANC TDRHRSVLPE
1160 1170 1180 1190 1200
HRCLKMEKII TKPCHRESCP KYKLGEWSQC SVSCEDGWSS RRVSCVSGNG
1210 1220 1230 1240 1250
TEVDMSLCGT ASDRPASHQT CNLGTCPFWR NTDWSACSVS CGIGHRERTT
1260 1270 1280 1290 1300
ECIYREQSVD ASFCGDTKMP ETSQTCHLLP CTSWKPSHWS PCSVTCGSGI
1310 1320 1330 1340 1350
QTRSVSCTRG SEGTIVDEYF CDRNTRPRLK KTCEKDTCDG PRVLQKLQAD
1360 1370 1380 1390 1400
VPPIRWATGP WTACSATCGN GTQRRLLKCR DHVRDLPDEY CNHLDKEVST
1410 1420 1430 1440 1450
RNCRLRDCSY WKMAEWEECP ATCGTHVQQS RNVTCVSAED GGRTILKDVD
1460 1470 1480 1490 1500
CDVQKRPTSA RNCRLEPCPK GEEHIGSWII GDWSKCSASC GGGWRRRSVS
1510 1520 1530 1540 1550
CTSSSCDETR KPKMFDKCNE ELCPPLTNNS WQISPWTHCS VSCGGGVQRR
1560 1570 1580 1590 1600
KIWCEDVLSG RKQDDIECSE IKPREQRDCE MPPCRSHYHN KTSSASMTSL
1610 1620 1630 1640 1650
SSSNSNTTSS ASASSLPILP PVVSWQTSAW SACSAKCGRG TKRRVVECVN
1660 1670 1680 1690 1700
PSLNVTVAST ECDQTKKPVE EVRCRTKHCP RWKTTTWSSC SVTCGRGIRR
1710 1720 1730 1740 1750
REVQCYRGRK NLVSDSECNP KTKLNSVANC FPVACPAYRW NVTPWSKCKD
1760 1770 1780 1790 1800
ECARGQKQTR RVHCISTSGK RAAPRMCELA RAPTSIRECD TSNCPYEWVP
1810 1820 1830 1840 1850
GDWQTCSKSC GEGVQTREVR CRRKINFNST IPIIFMLEDE PAVPKEKCEL
1860 1870 1880 1890 1900
FPKPNESQTC ELNPCDSEFK WSFGPWGECS KNCGQGIRRR RVKCVANDGR
1910 1920 1930 1940 1950
RVERVKCTTK KPRRTQYCFE RNCLPSTCQE LKSQNVKAKD GNYTILLDGF
1960 1970 1980 1990 2000
TIEIYCHRMN STIPKAYLNV NPRTNFAEVY GKKLIYPHTC PFNGDRNDSC
2010 2020 2030 2040 2050
HCSEDGDASA GLTRFNKVRI DLLNRKFHLA DYTFAKREYG VHVPYGTAGD
2060 2070 2080 2090 2100
CYSMKDCPQG IFSIDLKSAG LKLVDDLNWE DQGHRTSSRI DRFYNNAKVI
2110 2120 2130 2140 2150
GHCGGFCGKC SPERYKGLIF EVNTKLLNHV KNGGHIDDEL DDDGFSGDMD
Length:2,150
Mass (Da):242,582
Last modified:January 20, 2009 - v3
Checksum:iB18051C284C29116
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69360, Z69361 Genomic DNA. Translation: CAA93287.2.
PIRiT21371.
RefSeqiNP_001255447.1. NM_001268518.1.
UniGeneiCel.8168.

Genome annotation databases

EnsemblMetazoaiF25H8.3a; F25H8.3a; WBGene00001650.
GeneIDi177850.
KEGGicel:CELE_F25H8.3.
UCSCiF25H8.3. c. elegans.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z69360, Z69361 Genomic DNA. Translation: CAA93287.2.
PIRiT21371.
RefSeqiNP_001255447.1. NM_001268518.1.
UniGeneiCel.8168.

3D structure databases

ProteinModelPortaliQ19791.
SMRiQ19791. Positions 281-760, 1483-1556.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi6239.F25H8.3b.

Protein family/group databases

MEROPSiM12.135.

Proteomic databases

PaxDbiQ19791.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblMetazoaiF25H8.3a; F25H8.3a; WBGene00001650.
GeneIDi177850.
KEGGicel:CELE_F25H8.3.
UCSCiF25H8.3. c. elegans.

Organism-specific databases

CTDi177850.
WormBaseiF25H8.3a; CE42668; WBGene00001650; gon-1.

Phylogenomic databases

eggNOGiKOG3538. Eukaryota.
ENOG410XPKZ. LUCA.
GeneTreeiENSGT00760000118880.
HOGENOMiHOG000004798.
InParanoidiQ19791.
PhylomeDBiQ19791.

Miscellaneous databases

NextBioi898652.
PROiQ19791.

Gene expression databases

ExpressionAtlasiQ19791. baseline.

Family and domain databases

Gene3Di3.40.390.10. 1 hit.
InterProiIPR010294. ADAM_spacer1.
IPR024079. MetalloPept_cat_dom.
IPR012314. Pept_M12B_GON-ADAMTSs.
IPR001590. Peptidase_M12B.
IPR013273. Peptidase_M12B_ADAM-TS.
IPR000884. TSP1_rpt.
[Graphical view]
PfamiPF05986. ADAM_spacer1. 1 hit.
PF08685. GON. 1 hit.
PF01421. Reprolysin. 1 hit.
PF00090. TSP_1. 14 hits.
[Graphical view]
PRINTSiPR01857. ADAMTSFAMILY.
SMARTiSM00209. TSP1. 18 hits.
[Graphical view]
SUPFAMiSSF82895. SSF82895. 16 hits.
PROSITEiPS50215. ADAM_MEPRO. 1 hit.
PS51046. GON. 1 hit.
PS50092. TSP1. 15 hits.
PS00142. ZINC_PROTEASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Genome sequence of the nematode C. elegans: a platform for investigating biology."
    The C. elegans sequencing consortium
    Science 282:2012-2018(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Bristol N2.
  2. "The gon-1 gene is required for gonadal morphogenesis in Caenorhabditis elegans."
    Blelloch R., Anna-Arriola S.S., Gao D., Li Y., Hodgkin J., Kimble J.
    Dev. Biol. 216:382-393(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  3. "Control of organ shape by a secreted metalloprotease in the nematode Caenorhabditis elegans."
    Blelloch R., Kimble J.
    Nature 399:586-590(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE, MUTAGENESIS OF GLU-425.
  4. "Lectin affinity capture, isotope-coded tagging and mass spectrometry to identify N-linked glycoproteins."
    Kaji H., Saito H., Yamauchi Y., Shinkawa T., Taoka M., Hirabayashi J., Kasai K., Takahashi N., Isobe T.
    Nat. Biotechnol. 21:667-672(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1432, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.
  5. "GON-1 and fibulin have antagonistic roles in control of organ shape."
    Hesselson D., Newman C., Kim K.W., Kimble J.
    Curr. Biol. 14:2005-2010(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  6. "Proteomics reveals N-linked glycoprotein diversity in Caenorhabditis elegans and suggests an atypical translocation mechanism for integral membrane proteins."
    Kaji H., Kamiie J., Kawakami H., Kido K., Yamauchi Y., Shinkawa T., Taoka M., Takahashi N., Isobe T.
    Mol. Cell. Proteomics 6:2100-2109(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1432, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Bristol N2.
  7. "Identification of a novel ADAMTS9/GON-1 function for protein transport from the ER to the Golgi."
    Yoshina S., Sakaki K., Yonezumi-Hayashi A., Gengyo-Ando K., Inoue H., Iino Y., Mitani S.
    Mol. Biol. Cell 23:1728-1741(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN TRANSPORT, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE.

Entry informationi

Entry nameiGON1_CAEEL
AccessioniPrimary (citable) accession number: Q19791
Secondary accession number(s): Q27524
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 3, 2006
Last sequence update: January 20, 2009
Last modified: March 16, 2016
This is version 127 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programCaenorhabditis annotation project

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. 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.