ID A0A2I2U861_FELCA Unreviewed; 1214 AA.
AC A0A2I2U861;
DT 28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2019, sequence version 3.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=ADAM metallopeptidase with thrombospondin type 1 motif 19 {ECO:0000313|Ensembl:ENSFCAP00000028645.3};
GN Name=ADAMTS19 {ECO:0000313|Ensembl:ENSFCAP00000028645.3,
GN ECO:0000313|VGNC:VGNC:102153};
OS Felis catus (Cat) (Felis silvestris catus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Feliformia; Felidae; Felinae; Felis.
OX NCBI_TaxID=9685 {ECO:0000313|Ensembl:ENSFCAP00000028645.3, ECO:0000313|Proteomes:UP000011712};
RN [1] {ECO:0000313|Ensembl:ENSFCAP00000028645.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000028645.3,
RC ECO:0000313|Proteomes:UP000011712};
RX PubMed=17975172; DOI=10.1101/gr.6380007;
RA Pontius J.U., Mullikin J.C., Smith D.R., Lindblad-Toh K., Gnerre S.,
RA Clamp M., Chang J., Stephens R., Neelam B., Volfovsky N., Schaffer A.A.,
RA Agarwala R., Narfstrom K., Murphy W.J., Giger U., Roca A.L., Antunes A.,
RA Menotti-Raymond M., Yuhki N., Pecon-Slattery J., Johnson W.E., Bourque G.,
RA Tesler G., O'Brien S.J.;
RT "Initial sequence and comparative analysis of the cat genome.";
RL Genome Res. 17:1675-1689(2007).
RN [2] {ECO:0000313|Ensembl:ENSFCAP00000028645.3, ECO:0000313|Proteomes:UP000011712}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000028645.3,
RC ECO:0000313|Proteomes:UP000011712};
RA Hillier L.W., Warren W., Obrien S., Wilson R.K.;
RT "Sequence assembly of the Felis catus genome version 6.2.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Ensembl:ENSFCAP00000028645.3}
RP IDENTIFICATION.
RC STRAIN=breed Abyssinian {ECO:0000313|Ensembl:ENSFCAP00000028645.3};
RG Ensembl;
RL Submitted (SEP-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; AANG04002524; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; A0A2I2U861; -.
DR STRING; 9685.ENSFCAP00000028645; -.
DR Ensembl; ENSFCAT00000038536.3; ENSFCAP00000028645.3; ENSFCAG00000032620.3.
DR VGNC; VGNC:102153; ADAMTS19.
DR GeneTree; ENSGT00940000161018; -.
DR InParanoid; A0A2I2U861; -.
DR OMA; QHAEPDG; -.
DR Proteomes; UP000011712; Chromosome A1.
DR Bgee; ENSFCAG00000032620; Expressed in embryonic head and 6 other cell types or tissues.
DR GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0030198; P:extracellular matrix organization; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 5.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR041645; ADAMTS_CR_2.
DR InterPro; IPR010294; ADAMTS_spacer1.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF197; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 19; 1.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR Pfam; PF17771; ADAMTS_CR_2; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 5.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 5.
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:ARBA00023049};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Metalloprotease {ECO:0000256|ARBA:ARBA00023049};
KW Protease {ECO:0000256|ARBA:ARBA00022670};
KW Reference proteome {ECO:0000313|Proteomes:UP000011712};
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|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..1214
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5023837673"
FT DOMAIN 332..552
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1167..1206
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 55..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 100..114
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..163
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 490
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 301
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /note="in inhibited form"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 335
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 420
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 437
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 489
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 493
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 499
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 547
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 408..473
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 448..455
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 467..547
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT DISULFID 506..531
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 576..600
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 587..608
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 595..627
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 621..632
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 652..687
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 656..692
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 667..677
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1214 AA; 134357 MW; 11C689DD80B39431 CRC64;
PGKSREMRLT HICCCCLLYQ LGVLSNGIVS GLQFTPDREE WEVVFPALWR REPVDAAGGS
GGSADPGWVR GAGGGGGART QAAGSSREVR SVAPAPPGEP AEGHSAPRPR PRPPSPPAGE
EDEEFESQEL PRGSGGAAAL SPGAPASWQP PPPQPPPSPP PAQEAESDGD EVLLRIPAFS
RDLYLLLRRD GRFLAPRFAV EQRPSPGPVP TLAAAARRPP APPDASCFYT GAVLQHPGSL
ASFSTCGGGL MGFIQLNEDF IFIEPLNDTM AITGHPHRVY RQKRSMEEKV TEKSAPHSHY
CGIISDKGRP RSKKITESGR GKRYSYKLPQ EYNIETVVVA DPAMVSYHGA DAARRFILTI
LNMVFNLFQH KSLGVQVNLR VIKLILLHET PADLYIGHHG EKMLESFCKW QHEEFGKKND
IHLEMSTSWG EDMTSVDAAI LITRKDFCVH KDEPCDTVGI AYLSGMCSEK RKCIIAEDNG
LNLAFTIAHE MGHNMGINHD NDHPSCADGL HIMSGEWIKG QNLGDVSWSR CSKEDLERFL
RSKASSCLLQ TNPQSVNSVM VPSKLPGMTY TADEQCQILF GPLASFCQEM QHLICTGLWC
KVEGEKECRT KLDPPMDGTD CDAGKWCKAG ECTTRTSAPG HVAGEWSMWS PCSRTCSSGI
SSRERKCPGL GSEARDCNGP RKQYRICENP PCPAGLPGFR DWQCQAYSVR TSYPKHGLQW
QAVMDEEKPC ALFCSPVGKE QPILLSEKVM DGTSCGYQGL DVCANGRCQK VGCDGFLGSL
AREDHCGVCN GNGKSCKIIK GDFNHTRGAG YVEVLVIPAG ARRIKVVEEK PAHSYLALRD
TGKQSINSDW KIEHSGAFNL AGTTVHYVRR GLWEKISAKG PTTSPLHLLV LLFQDQNYGL
HYEYTIPSDP LPENQSSKAP EPLFMWTHTG WEDCDATCGG GERKTTVSCT KIMNKNISIV
DNKKCKYLTK PEPQIRKCNE QPCQTRWMMT EWTPCSRTCG KGMQSRQVAC TQQLSNGTLI
RARERDCSGP KPASAQRCEG QDCMTVWEAG VWSECSVKCG KGVRHRTVRC TNPRKKCVLS
TRPREAEDCE DYSKCYVWRM GDWSKCSITC GKGMQSRVIQ CMHKITGRHG NECFSSEKPA
AYRPCHLQPC NEKINVNTIT SPRLAALTFK CLGDQWPVYC RVIREKNLCQ DMRWYQRCCE
TCRDFYAQKL QQKS
//
