ID G1SIX7_RABIT Unreviewed; 1198 AA.
AC G1SIX7;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 74.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 3 {ECO:0000313|Ensembl:ENSOCUP00000002651.2};
GN Name=ADAMTS3 {ECO:0000313|Ensembl:ENSOCUP00000002651.2};
OS Oryctolagus cuniculus (Rabbit).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Lagomorpha; Leporidae; Oryctolagus.
OX NCBI_TaxID=9986 {ECO:0000313|Ensembl:ENSOCUP00000002651.2, ECO:0000313|Proteomes:UP000001811};
RN [1] {ECO:0000313|Ensembl:ENSOCUP00000002651.2, ECO:0000313|Proteomes:UP000001811}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Thorbecke inbred {ECO:0000313|Ensembl:ENSOCUP00000002651.2,
RC ECO:0000313|Proteomes:UP000001811};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSOCUP00000002651.2}
RP IDENTIFICATION.
RC STRAIN=Thorbecke {ECO:0000313|Ensembl:ENSOCUP00000002651.2};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000256|PIRSR:PIRSR613273-2};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000256|PIRSR:PIRSR613273-2};
CC -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC matrix {ECO:0000256|ARBA:ARBA00004498}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; AAGW02023044; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02023045; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02023046; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02023047; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02023048; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02023049; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02023050; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02023051; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02023052; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAGW02023053; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; G1SIX7; -.
DR SMR; G1SIX7; -.
DR STRING; 9986.ENSOCUP00000002651; -.
DR PaxDb; 9986-ENSOCUP00000002651; -.
DR Ensembl; ENSOCUT00000003048.4; ENSOCUP00000002651.2; ENSOCUG00000003040.4.
DR eggNOG; KOG3538; Eukaryota.
DR GeneTree; ENSGT00940000156085; -.
DR HOGENOM; CLU_000660_4_1_1; -.
DR InParanoid; G1SIX7; -.
DR OMA; GYCDANK; -.
DR TreeFam; TF313537; -.
DR Proteomes; UP000001811; Chromosome 15.
DR Bgee; ENSOCUG00000003040; Expressed in ovary and 12 other cell types or tissues.
DR GO; GO:0005615; C:extracellular space; IEA:Ensembl.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0032964; P:collagen biosynthetic process; IEA:Ensembl.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR GO; GO:1900748; P:positive regulation of vascular endothelial growth factor signaling pathway; IEA:Ensembl.
DR GO; GO:0016485; P:protein processing; IEA:Ensembl.
DR GO; GO:0010573; P:vascular endothelial growth factor production; IEA:Ensembl.
DR CDD; cd04273; ZnMc_ADAMTS_like; 1.
DR Gene3D; 2.60.120.830; -; 1.
DR Gene3D; 3.40.1620.60; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 4.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR002870; Peptidase_M12B_N.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF158; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 3; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01562; Pep_M12B_propep; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 3.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 4.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 4.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 4.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|PIRSR:PIRSR613273-2};
KW Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000001811};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Zinc {ECO:0000256|ARBA:ARBA00022833, ECO:0000256|PIRSR:PIRSR613273-2}.
FT SIGNAL 1..22
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 23..1198
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003421390"
FT DOMAIN 256..460
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1010..1053
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 1095..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1125..1175
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1176..1198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 399
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 259
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 351
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 398
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 402
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 408
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 455
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 458
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 333..382
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 376..455
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 415..441
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 482..507
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 493..516
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 502..535
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 529..540
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 563..600
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 567..605
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 578..590
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1198 AA; 135025 MW; C068D74F2FD0FEE1 CRC64;
MVLLSLWLIV AALVEVRTSA DGQAGNEEMV QIDLPIKRHR EYELVTPVST NLEGHYLSHI
LSANHKKRST RDVSSNPEQL FFNITAFGRD FHLRLKPNTQ LIAPGALVEW HETPLVPGNT
TDPINDHQPG SASERIWKTE PLHTNCAYVG DIMDVPGTSV AISNCDGLAG MIKSDNEEYF
IEPLERGKQM EEEKGRIHVV YKRSAVERAP IDRSTDFHYR ESDVEGLDDL GTIYSSIDQQ
LNETMRRRRH AGENDYNIEV LLGVDDSVVR FHGKEHVQNY LLTLMNIVNE IYHDESLGVH
INVVLVRMIM LGYAKSISLI ERGNPSRSLE NVCRWACQQQ KSDPNHSEHH DHAIFLTRQD
FGPAGMQGYA PVTGMCHPVR SCTLNHEDGF SSAFVVAHET GHVLGMEHDG QGNRCGDETA
MGSVMAPLVQ AAFHRYHWSR CSGQELKRYI HSYDCLLDDP FEHDWPKLPE LPGINYSMDE
QCRFDFGVGY KMCTAFRTFD PCKQLWCSHP DNPYFCKTKK GPPLDGTECS AGKWCYKGHC
MWKNANQQKQ DGNWGSWTKF GSCSRTCGTG VRFRTRQCNN PMPINGGQDC PGVNFEYQLC
NTEECQKHFE DFRAQQCQQR NSHFEYQNSR HHWLPYEHPD SKKRCHLYCQ SKETGDVAYM
KQLVHDGTRC SYKDPYSICV RGECVKVGCD KEIGSNKVED KCGVCGGDNS HCRTVKGTFT
RTPRKLGYLK MFDIPGARHV LIQEDEASPH ILAIKSQATG HYILNGKGEE AKSRTFIDLG
VEWDYNIEDD IETLHTDGPL RDPVIVLIIP QENDTRSSLT YKYIIHEDSV PTINSNNVIQ
EELDTFEWAL KSWSQCSKPC GGGFQYTKYG CRRKSDNKMV HRSFCEANKK PKPIRRMCNI
QECTHPLWVA EEWEHCTKTC GSTGYQLRTV RCLQPLQDGT NRSVHSKFCV GDRPESRRPC
NRVPCPAQWK TGPWNECSVT CGEGTEVRQV ICRAADHCDG AKPESVRACQ LPPCNDEPCL
GDKSIFCQME VLARYCSIPG YNKLCCESCS KRSSTLPPPY LLEAAETQED TILSPSGLPG
SLVVPTSLVP YYAETPAEKS SMGGPNTHTA FRPNRKRDGA KLHQKRAQQS GSETLRPVSV
PSSSPTQSGH LSSASQLAAA PFLAVSNSIG ASSQTRTSKK DEKMINKRHP VRSSNLER
//
