ID L5JVP1_PTEAL Unreviewed; 898 AA.
AC L5JVP1;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=A disintegrin and metalloproteinase with thrombospondin motif 19 {ECO:0000313|EMBL:ELK03127.1};
GN ORFNames=PAL_GLEAN10016916 {ECO:0000313|EMBL:ELK03127.1};
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:ELK03127.1, 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 -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00276}.
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DR EMBL; KB031114; ELK03127.1; -; Genomic_DNA.
DR AlphaFoldDB; L5JVP1; -.
DR STRING; 9402.L5JVP1; -.
DR MEROPS; M12.029; -.
DR eggNOG; KOG3538; Eukaryota.
DR InParanoid; L5JVP1; -.
DR Proteomes; UP000010552; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro.
DR GO; GO:0007229; P:integrin-mediated signaling pathway; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
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; 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; PF13688; Reprolysin_5; 1.
DR Pfam; PF19030; TSP1_ADAMTS; 4.
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 Extracellular matrix {ECO:0000256|ARBA:ARBA00022530};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023049};
KW Integrin {ECO:0000313|EMBL:ELK03127.1};
KW 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, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..898
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003968569"
FT DOMAIN 151..312
FT /note="Peptidase M12B"
FT /evidence="ECO:0000259|PROSITE:PS50215"
FT DOMAIN 851..890
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 106..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 309
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00276"
SQ SEQUENCE 898 AA; 101173 MW; A886C9978A8DDB0F CRC64;
MGKSREMRLA HLCCCCCLLY QLGVLSNGIV SGLQFAPDRE EWEVVFPALW RREPVDAAGG
SGGSSDQGWM GFIQLNEDFI FIEPLNDTMA ITGHPHRVYR QKRSMEEKVT EKSTPHSHYC
GIISDKGRPR SKKITESGRG KRYSYKLPQE YNIETIVVAD PAMVSYHGAD AARRFILTIL
NMVFNLFQHK SLGVQVNLRV IKLILLHETP ADLYIGHHGE KMLESFCKWQ HEEFGKKNDI
HLEMSTSWGE DMTPADAAIL ITRKDFCVHK DEPCDTVGIA YLSGMCSEKR KCIIAEDNGL
NLAFTIAHEM GHKSKASNCL LQTNPQSVNS VMVPSKLPGM TYTAHEQCQI LFGPLASFCQ
EMQHVICTGL WCKVEGEKEC RTKLDPPMDG TDCDAGKVLK QGIVMVPENN TEYVSIHLVL
QVCLDSETGN VRPIVLELRT QSMHFSGKLS WMKKVGCDGL LGSLAREDHC GVCNGNGKSC
KIIKGDFNHT RGAGYVEVLV IPTGARRIKV VEEKPAHSYL ALRDTGKQSI NSDWKIEHSG
AFNLAGTTVH YVRRGLWEKL SAKGPTTSPL HLLVLLFQDQ NYGLHYEYTI PSDPPPENQS
AKAPEPLFMW THAGWEDCDA TCGGGERKTT VSCTKIMNKN ISIVDNKKCK YLTKPEPQIR
KCNEQPCQTR WMMTEWTPCS RTCGKGMQSR QVACTQQLSN GTLVRARERD CAGPKPASAQ
RCEGQDCMTV WEAGVWSECS VKCGKGVRHR TVRCTNPRKK CVLSTRPREA EDCEDYSKCY
VWRMGDWSKC SITCGKGMQS RVIQCMHKIT GRHGNECFSS EKPAAYRPCH LQPCNEKINV
NTITSPRLAA LTFKCLGDQW PVYCRVIREK NLCQDMRWYQ RCCETCRDFY AQKLQQKS
//
