ID K1RDR5_CRAGI Unreviewed; 1226 AA.
AC K1RDR5;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motifs 2 {ECO:0000313|EMBL:EKC39440.1};
GN ORFNames=CGI_10020043 {ECO:0000313|EMBL:EKC39440.1};
OS Crassostrea gigas (Pacific oyster) (Crassostrea angulata).
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Pteriomorphia; Ostreida; Ostreoidea; Ostreidae; Crassostrea.
OX NCBI_TaxID=29159 {ECO:0000313|EMBL:EKC39440.1};
RN [1] {ECO:0000313|EMBL:EKC39440.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05x7-T-G4-1.051#20 {ECO:0000313|EMBL:EKC39440.1};
RX PubMed=22992520; DOI=10.1038/nature11413;
RA Zhang G., Fang X., Guo X., Li L., Luo R., Xu F., Yang P., Zhang L.,
RA Wang X., Qi H., Xiong Z., Que H., Xie Y., Holland P.W., Paps J., Zhu Y.,
RA Wu F., Chen Y., Wang J., Peng C., Meng J., Yang L., Liu J., Wen B.,
RA Zhang N., Huang Z., Zhu Q., Feng Y., Mount A., Hedgecock D., Xu Z., Liu Y.,
RA Domazet-Loso T., Du Y., Sun X., Zhang S., Liu B., Cheng P., Jiang X.,
RA Li J., Fan D., Wang W., Fu W., Wang T., Wang B., Zhang J., Peng Z., Li Y.,
RA Li N., Wang J., Chen M., He Y., Tan F., Song X., Zheng Q., Huang R.,
RA Yang H., Du X., Chen L., Yang M., Gaffney P.M., Wang S., Luo L., She Z.,
RA Ming Y., Huang W., Zhang S., Huang B., Zhang Y., Qu T., Ni P., Miao G.,
RA Wang J., Wang Q., Steinberg C.E., Wang H., Li N., Qian L., Zhang G., Li Y.,
RA Yang H., Liu X., Wang J., Yin Y., Wang J.;
RT "The oyster genome reveals stress adaptation and complexity of shell
RT formation.";
RL Nature 490:49-54(2012).
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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; JH818808; EKC39440.1; -; Genomic_DNA.
DR AlphaFoldDB; K1RDR5; -.
DR HOGENOM; CLU_268156_0_0_1; -.
DR InParanoid; K1RDR5; -.
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:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
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; 1.
DR InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR InterPro; IPR045371; ADAMTS_CR_3.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR001590; Peptidase_M12B.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR PANTHER; PTHR13723:SF281; NO LONG NERVE CORD, ISOFORM C; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF01421; Reprolysin; 1.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 1.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50092; TSP1; 1.
PE 4: Predicted;
KW Calcium {ECO:0000256|PIRSR:PIRSR613273-2};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW ECO:0000256|PIRSR:PIRSR613273-3};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Integrin {ECO:0000313|EMBL:EKC39440.1};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT ACT_SITE 324
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 278
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 323
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 327
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 333
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 373
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 383
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 268..307
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 301..373
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 339..357
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 408..432
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 427..463
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 457..468
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 495..531
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 499..536
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 510..521
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1226 AA; 134936 MW; FAB8361E0F459F20 CRC64;
MAKVHDSKTK RSDDEALLSL LESRGIRFLE YSTLRHDSRA FRDRSKREAT SSNVLLSFKM
RFTYAKEHYE IEFNNPQQIL HPSAEVLTFT NGSVQQWLGA HPDCFLTGTV TSHSGVASLS
FCDKIVGLVK TRKHALYLES ISEIADNDNL QIIIGQQTQD EISNHVTKRL DGYNGARTRR
SLTSHNITIE MAVYIDAAYT QTMLVTDFSK RLQHILLKYY AVQMEWSRAD MLDYNVQIVL
KKVHFFEENP AWYNTSTSLL GSVLYQFCMA TTGDGPFDIR YMHVGLTNLD VLGRAYQNSV
CNPTYNCAVD TATGAASFAA TAHEIGHLLG MYHDADRGCT GNNIGLMGGF GTGWSSCSKE
DMAVLLNSGN KNCLWEENIP LEDVPESIAN VTLISAIPGQ IYSPDQVCEL KYGTGYQFRK
YPKLGVCVLY SCANHNSAQI NYGQMFKEWT SIFGMYCEKD KICFKMGCVD ASAAKLTNLM
KREGGWSQWG PWTGCTRTCG RGINYRKRKC DNPAPINLDG CAGEAYEAKI CNTQPCAKDS
SDELTLRNQR ASETCKRLRD NNVIDPDLYN ETGSRYSDTA HGQCEVTCDP APGHTIPTFT
RFGFIPDGVA CTGGSDPWDL YNWPRNSGSR YLCLDGLCQR FGCDNQLNGQ VLDECGVCGG
DNSTCIVIAN TDTEQQIQGE RRTLAVLPAG TFNIQFWFPY KEMADNYLEL YSKHGSVILA
SRIPSSWVWD ARSSPVVFAG TEWYYFFYGQ YLYAKGPLTE SCEIKLFQFG VNNNTGVSFT
YSEPLAEYFI HMSSLTTDKT ATISKQNIHG TSYDQYLSLS YHVTGIGSKI TVSLHGGINT
SVLWSSVDSS QLVINEWKSA TMNITTFEKY EIRITCETKV QHSGTISLDD LKLSYYEDSY
CNDEDSCVTP SLDLSTSTTF VSTTKSTFTT PSTTVKEDTT NPVASTTTNL HETTTKIKDI
TETTTSGSET TPVSPTITTE STSSITTLTS TKATSMPEST TTLSTGIPTT TETGTASSET
TAKTSGNTTT VSPVSTTETV ATSITTTMTT TTSVVTETST QKTTTKLTTL KEGTSTSTTV
SASTVTSSEE ITTAKSTQES TLSPTTFNST SSSLKSTTPV SLSSTTTISD ADSYGRYMFM
GLAIAGPFIL MLIAVGIFIC CRRCSKCSPK GKSQEKYRVS KQFDGNSSRT DGSSKPLSPQ
FWPDVDEIKI NITNDCDIDL GSKSEI
//
