ID L5L3P1_PTEAL Unreviewed; 1544 AA.
AC L5L3P1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motif 7 {ECO:0000313|EMBL:ELK18349.1};
DE Flags: Fragment;
GN ORFNames=PAL_GLEAN10009599 {ECO:0000313|EMBL:ELK18349.1};
OS Pteropus alecto (Black flying fox).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Chiroptera; Megachiroptera; Pteropodidae;
OC Pteropodinae; Pteropus.
OX NCBI_TaxID=9402 {ECO:0000313|EMBL:ELK18349.1, ECO:0000313|Proteomes:UP000010552};
RN [1] {ECO:0000313|Proteomes:UP000010552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23258410; DOI=10.1126/science.1230835;
RA Zhang G., Cowled C., Shi Z., Huang Z., Bishop-Lilly K.A., Fang X.,
RA Wynne J.W., Xiong Z., Baker M.L., Zhao W., Tachedjian M., Zhu Y., Zhou P.,
RA Jiang X., Ng J., Yang L., Wu L., Xiao J., Feng Y., Chen Y., Sun X.,
RA Zhang Y., Marsh G.A., Crameri G., Broder C.C., Frey K.G., Wang L.F.,
RA Wang J.;
RT "Comparative analysis of bat genomes provides insight into the evolution of
RT flight and immunity.";
RL Science 339:456-460(2013).
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; KB030332; ELK18349.1; -; Genomic_DNA.
DR STRING; 9402.L5L3P1; -.
DR MEROPS; M12.231; -.
DR eggNOG; KOG3538; Eukaryota.
DR InParanoid; L5L3P1; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
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: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; 6.
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; IPR010909; PLAC.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR PANTHER; PTHR13723:SF142; A DISINTEGRIN AND METALLOPROTEINASE WITH THROMBOSPONDIN MOTIFS 7; 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; PF01421; Reprolysin; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 6.
DR Pfam; PF00090; TSP_1; 1.
DR PRINTS; PR01857; ADAMTSFAMILY.
DR SMART; SM00209; TSP1; 7.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR SUPFAM; SSF82895; TSP-1 type 1 repeat; 6.
DR PROSITE; PS50215; ADAM_MEPRO; 1.
DR PROSITE; PS50900; PLAC; 1.
DR PROSITE; PS50092; TSP1; 7.
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 Integrin {ECO:0000313|EMBL:ELK18349.1};
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:UP000010552};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Zinc {ECO:0000256|PIRSR:PIRSR613273-2, ECO:0000256|PROSITE-
KW ProRule:PRU00276}.
FT DOMAIN 145..355
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 1490..1530
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 905..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 957..1195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1207..1279
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1525..1544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 971..995
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1009..1031
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1074
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1099..1131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1225..1259
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 292
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-1,
FT ECO:0000256|PROSITE-ProRule:PRU00276"
FT BINDING 107
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 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 148
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 232
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 239
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 291
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 295
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 301
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 350
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT BINDING 353
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-2"
FT DISULFID 221..275
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 250..257
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 269..350
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 308..334
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 377..400
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 388..406
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 395..425
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 419..430
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 453..490
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 457..495
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 468..480
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ELK18349.1"
SQ SEQUENCE 1544 AA; 167517 MW; 2C4BD88A303640FE CRC64;
NVHLLAPGFV SETRRRGGLG RAHIRTHAPA CHLLGEVQDP ELEGGLAAIS ACDGLKGVFQ
LSNEDYFIEP LEGVPARPGR AQPHVVYKRQ APKRRAEPGD TTAPGTCGVQ EPLEQEARRE
RWELRQQRRR PWPRRLHPRS VSREKWVETL VVADAKMVEY HGQPHVESYM LTIMNMVAGL
FHDPSIGNPI HITIVRLILL EDEEEDLKIT HHADNTLRSF CKWQKSINMK GDSHPLHHDT
AILLTRKDLC ASTNWPCETL GLSHVAGMCQ PHRSCNINED TGLPLAFTVA HELGHSFGIQ
HDGSGNDCEP VGKRPSVMSP QLLYDSVPLT WSRCSREYIT RFLDRGWGMC LDDTPAKEVI
DFPSVLPGVL YDVGHQCRLQ YGAYSVFCDG MDNVCHTLWC SVGTTCHSKL DAAVDGTACG
ESKWCLDGEC VAVGFRPEAV DGGWSGWSAW SICSRSCGVG VQSAERQCTQ PVPKYKGKYC
VGERRRLRLC NLHGCPAGRP SFRHVQCSHF DAMLYKGQLH TWVPVVNDEN PCELHCRPSD
EYFAEKLRDA VVDGTPCYQG QASHDLCING ICKNVGCDFE IDSGAVEDRW YVDVGLIPAG
AREILIEEVA EAANFLALRG EDPDRYFLNG GWTIQWNGDY QVAGTTFTYV RTGDWENLTS
PGPTSEPVWI QLLFQESNPG VRYEYTIHRE ADGPGLGPPP EFSWLHGPWS KCTVTCGTGM
QRRSVYCAER QLGPVDEGHC DPLSRPDDRQ RKCSEERCPA RWWAGEWQLC SSSCGPGGLS
RRAVLCVRSV GLDEQSALEP PACAHLPRPP AETPCNRNVT CPATWAVGNW SQCSVTCGPG
TQHRSVLCMN DTSVPCDEAQ RPAGEATCPR PPCPRALGEL DPEGSGSGSF SHELYNEVDF
VPRHLAPRPV RPSPPGPAGD GNAIEGAGPE PEPMFVDDFY YDYNFITFHE DLSYRPFEEP
SSDLGATGDW TPPPPSSPAE PPVGTPEPAP EPPGADGERA PRDRSPTSWP GQAGHSLPPP
SEQTLGNLLV TRSEDTPMGP PDLGLPGLPW TPASAGGTET TSAPEDQDES LTGVSGPSPP
LPPRWERTNE VSEDNEGAPH LPPSSTVSPL SSTSTVHSSP GPDSAQLWTR VTGTWEPALD
GGLGPGAREL WPTVGGSPPT PRPTASLPEA RDRDGPLEQG TPALPAPGPA LLEPQTPAVT
GSFLLMTPTG LRHTPGVTAL SPAPSGRAES PSPQAPLSSV LLSATAGDSP ANSSGAPDTQ
IPDPGLAEEG SPKDLPPASN ATWECSTTCG LGAVWRPVRC SSGREDDCAP AGQKRRGHLR
PCATWHAGNW SKCSRSCGGG SSVRDVQCVD RDLRPLRPFH CQAGPAPPPA RQPCGAQPCL
SWYTSSWREC SEACGGGQQQ RLVTCPQPGL CEEALRPSST RPCNTQPCTQ WAVGPWGQCS
APCGGGVQRR LVRCVNTHTG LPEEDGEQCG HEAWPENSRP CGTQDCELTE PPRCVRDRLP
FGFCETLRLL GRCQLPTVRT QCCRSCPPPG RTAPSRGHQR ASRR
//
