ID A0A2U3VC44_ODORO Unreviewed; 1222 AA.
AC A0A2U3VC44;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 18 {ECO:0000313|RefSeq:XP_004392114.1};
GN Name=ADAMTS18 {ECO:0000313|RefSeq:XP_004392114.1};
OS Odobenus rosmarus divergens (Pacific walrus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Pinnipedia; Odobenidae;
OC Odobenus.
OX NCBI_TaxID=9708 {ECO:0000313|Proteomes:UP000245340, ECO:0000313|RefSeq:XP_004392114.1};
RN [1] {ECO:0000313|RefSeq:XP_004392114.1}
RP IDENTIFICATION.
RG RefSeq;
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 RefSeq; XP_004392114.1; XM_004392057.1.
DR AlphaFoldDB; A0A2U3VC44; -.
DR STRING; 9708.A0A2U3VC44; -.
DR GeneID; 101371925; -.
DR KEGG; oro:101371925; -.
DR CTD; 170692; -.
DR InParanoid; A0A2U3VC44; -.
DR OrthoDB; 2910701at2759; -.
DR Proteomes; UP000245340; Unplaced.
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; IEA:InterPro.
DR GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
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; 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:SF167; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 18; 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; PF08686; PLAC; 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; 6.
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: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:UP000245340};
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..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1222
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015650186"
FT DOMAIN 293..498
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1185..1222
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 212..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 437
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 296
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 384
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 436
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 440
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 446
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="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 496
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 369..420
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 395..402
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 414..493
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 453..477
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 521..546
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 532..553
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 541..572
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 566..577
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 601..638
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 605..643
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 616..628
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1222 AA; 134921 MW; C553E13B12A5E5E8 CRC64;
MECALLLACA LPAARSRPPC GPAGLGRVAK ALQLCCLCCA SVAAALASDS SGGGGGLNVD
YVFVTPVEVD SGGSYISHDI LHNGRKKRSA QSAHSSLHYQ FSAFGQELHL ELKPSAILSS
HFIVQVLGKD GASETREPAV QRCFYQGFIR NDSSSSIAVS TCAGLSGLIR TRKNEFLISP
LPQLLAQEHN YSAPAGHHPH VLYKRTAEEK VQHCHDYPGS SRHYPGHSPT HTPHASRSQE
REHHHPRLQK QHFCGRRKKY APKPPTEDTY LRFDEYGSAG RPRRSAGKSQ KGLNVETLVV
ADKKMVEKHG KANVTTYILT VMNMVSSLFK DGTIGSDINI VVVSLILLEQ EPGGLLINHH
ADQSLNSFCQ WQSALIGKNG KRHDHAILLT GFDICSWKNE PCDTLGFAPI SGMCSKYRSC
TINEDTGLGL AFTIAHESGH NFGMIHDGEG NPCRKAEGNI MSPTLTGNNG VFSWSSCSRQ
YLKKFLSTPQ AGCLVDEPKQ TGQYKYPDKL PGQIYDADTQ CKWQFGAKAK LCSLGFVKDI
CKSLWCHRVG HRCETKFMPA AEGTVCGLSM WCRQGQCVKF GEHGPRPVHG QWSAWSKWSE
CSRTCGGGVK YQERHCNNPK PQYGGKFCPG SSRIYQLCNI NPCNENSLDF RAQQCAEYNS
KPFRGWFYQW KPYTKVEDAD RCKLYCKAEN FEFFFAMSSK VKDGTPCSPD KHDVCIDGIC
EPVGCDHELG SKAVLDACGV CKGDNSTCKF YKGLYLNQHK ANEYYPVVTI PAGARSIEIQ
ELQLSSSYLA VRSLGQKYYL TGGWSIDWPG EFPFAGTVFE YQRSFNHPER LYAPGPTNET
LVFEVLMQGK NPGIAWKYAL PKVTNGTQPA SKRHSHAWTT VQSPCSISCG GGYISVKAIC
LRDQNTQVSS SFCNARTKPA TEPKICNAFS CPAYWKPGEW SVCSRSCAGG QQSRKIQCVQ
KKPFQKEEAV LHSLCPVSTP TQVQACNSHA CPPEWSLGPW SQCSKSCGRG VRKREVLCKS
SPTAENVPET LCSSIPRPES QEGCVLGRCP KNTRLQWVVS SWSECSMTCG LGVRKREMKC
SEKPFPGKLI TFPERRCRNI KKPNLELEET CQQGACPAHP GFSVAAGWYP SPWQQCTVTC
GGGVQTRSVH CVQQGRPSSG CLLHQKPPVL RACNTNFCPA PEKREDPSCV DFFSWCHLVP
QHGVCNHKFY GQQCCKSCTR KS
//
