ID A0A2U9BLH1_SCOMX Unreviewed; 1793 AA.
AC A0A2U9BLH1;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Putative pappalysin-2 {ECO:0000313|EMBL:AWP04620.1};
GN ORFNames=SMAX5B_021737 {ECO:0000313|EMBL:AWP04620.1};
OS Scophthalmus maximus (Turbot) (Psetta maxima).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC Scophthalmus.
OX NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP04620.1, ECO:0000313|Proteomes:UP000246464};
RN [1] {ECO:0000313|EMBL:AWP04620.1, ECO:0000313|Proteomes:UP000246464}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Martinez P.;
RT "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT evaluation of genetic and physical mapping variation across individuals.";
RL Submitted (DEC-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the peptidase M43B family.
CC {ECO:0000256|ARBA:ARBA00008721}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00302}.
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DR EMBL; CP026249; AWP04620.1; -; Genomic_DNA.
DR Proteomes; UP000246464; Chromosome 7.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR CDD; cd00033; CCP; 3.
DR Gene3D; 2.60.120.200; -; 1.
DR Gene3D; 3.40.390.10; Collagenase (Catalytic Domain); 1.
DR Gene3D; 2.10.70.10; Complement Module, domain 1; 3.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR006558; LamG-like.
DR InterPro; IPR024079; MetalloPept_cat_dom_sf.
DR InterPro; IPR011936; Myxo_disulph_rpt.
DR InterPro; IPR000800; Notch_dom.
DR InterPro; IPR043543; PAPPA/PAPPA2.
DR InterPro; IPR008754; Peptidase_M43.
DR InterPro; IPR035976; Sushi/SCR/CCP_sf.
DR InterPro; IPR000436; Sushi_SCR_CCP_dom.
DR NCBIfam; TIGR02232; myxo_disulf_rpt; 1.
DR PANTHER; PTHR46130; LAMGL DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR46130:SF1; PAPPALYSIN-2; 1.
DR Pfam; PF13948; DUF4215; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF05572; Peptidase_M43; 1.
DR Pfam; PF00084; Sushi; 1.
DR SMART; SM00032; CCP; 4.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00004; NL; 2.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 3.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50923; SUSHI; 2.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000246464};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..1793
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5015966086"
FT DOMAIN 1467..1528
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1598..1653
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 59..78
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..190
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 227..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..186
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1793 AA; 196599 MW; EAEC14BE2D4A2A40 CRC64;
MLLIRLLAVF LALITNTWLL NPVRSDALDR HKRAMARRAD RELSRLAGEP CTVAGAWRSR
RQPRPLSPSQ HRPLAARART HASLRELYAV KSAPAVCAGG CGGDTGAHRV EGKAGWGDAE
GVTVGAGDGY VPWPGRLHAR PSTSDERDPS SVGADATQRP GIPARKDAGQ SASSRGHAQS
PRGSGSRLAR SLDGTLPFEE EGNSSWEKVF ADSSTDSRGP QVGLLHRLQR GDGGQRSSSG
TVEDYSGEVE EADPPAGSPP WGSPVPRVPP SWMTALYFSG RREQLKVKPA ARLELPRAKF
SLELWVKPEG GQSNPAVIAG VFDNCSHSLS EKGWSVGIRT VDPSGTRDAR FYFTLRTDRA
VKSTTVYSHQ RYRTSAWTHL MATYNGHNMT LYVDGAKVGE SNLQSGNLYS PFMRTCRTLF
LGSNQSEQGH SFRGHIGGVI LWGNARSHED LLKQPLQPDM SEPILAMWGD FTNVEQLWSP
HKAGLHPTVI TTPVPEQELV SSFLPPPCGL TSCDNTDIIL GYNNNWQLRT PKRVCYRIVN
LSNDDGGNPT VTQAQIQLQH LALTEAFRPY NITLDLSVHN VRNSSLKQRF ILSNCRIGKI
GNRRCDPECD HPKTGHDGGD CLRLGPCYNW KRQDGVCNME CNSIHYDYDD GDCCDPEVTD
VLKTCFDPES PDRAYMSVKE LKEELHLSGS DTLNVFFASN SVREELAGAA TWPWAKEALT
HQGGMVLNPS YFGTMGHHNT MIHEMGHIFG LYHVFKGVSE RDSCDDPCQE TTPSMETGDL
CADTAPTPKS KSCNDPGAIN DTCGVTTYQD TPYSNYMSYT DDNCTNHFTP NQVARMHCYL
DLVYQKWLMD RQPAPIPLAP LVTDQTKDSV SVYWLPPIRG PLYQSSPLLT SVINCGDCEK
DGIFHQYAYE ATSPRICDTS GYWTPEEAVG PPDVEQPCDP SLQAWSPELS LYDTNVTSPC
PDTEGCTLML RFLHPVVPHA LTLWVTYISS NNPAIANIEL ITDMGKSINL GPQHVFCDMP
LTLRINTHNA AIAAIKLCTF DEKMEIDAAM LSSGPGSPLC SNCRPLLYWI QRQPPFNSQS
PSPQTQHTFT DSSVRRGVKY QYSIQVEADG LLSDPSPPLL YTHGQSYCGD GRIQGTEECD
DSNLLDGDGC SKKCHKEMDF KCNGEPSQCY VFDGDGVCEE FERGSSVQDC GYFTPLGYTD
QWASTATASH QDSNHCPARA ATGEPSLNKL CRYQHLEMSD KLPSDAWFPC TAQSDTNNDL
EHSFWLKVGF LHPGVAASVM VYLGSDGSLS VEQCQRTATI LLSDTTGKNH SLGTHDLSCH
RNPLVVNVTH DLSRPFFLTS SVILLFSSPS VAVGGVALRT SCHFSTFALT GCASEGGLSH
SYLLNTHTCL HICLRQPCQM DSCGPPQLEH ASVRCTGGGE ASRCVVQCHR GFSISVLNGR
GAPPHQRKTE LECFHGSWDR VVSCQPVDCG LPDQSHVYHA IFSCPWGTAF GKQCSFTCGS
PAILQGDSDR LVCLEDGLWS FPEAYCKIEC PEVPNITDAK LLTADCLASG HDVGSVCRYK
CSPGFYVTGS LTKKTPRKYF KLACLEGGHW EETGCEPISC PALPDVFQGM YTCTNSLYYD
TVCTLQCSDA SENSEIRCTK DGEWTAAFAM CSRLQGSCSA PPNLNSVEYS CDQGMDVGAV
CYPTCIVALD MDLRDPVVLP NGTTADSVRH WMLPTGVESI VCTGMMKWYP DPQHIHCIQS
CEPFGGDGWC DTTNNRAYCQ YDGGDCCPST LSTRKVHKQT FPVLHLLSAT CMP
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