ID A0A3B4FWU6_9CICH Unreviewed; 1744 AA.
AC A0A3B4FWU6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Pappalysin 2 {ECO:0000313|Ensembl:ENSPNYP00000015090.1};
GN Name=PAPPA2 {ECO:0000313|Ensembl:ENSPNYP00000015090.1};
OS Pundamilia nyererei.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC Pseudocrenilabrinae; Haplochromini; Pundamilia.
OX NCBI_TaxID=303518 {ECO:0000313|Ensembl:ENSPNYP00000015090.1, ECO:0000313|Proteomes:UP000261460};
RN [1] {ECO:0000313|Ensembl:ENSPNYP00000015090.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2023) to UniProtKB.
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 Ensembl; ENSPNYT00000015472.1; ENSPNYP00000015090.1; ENSPNYG00000011062.1.
DR GeneTree; ENSGT00940000158543; -.
DR Proteomes; UP000261460; Unplaced.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro.
DR CDD; cd00033; CCP; 2.
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; 2.
DR InterPro; IPR013320; ConA-like_dom_sf.
DR InterPro; IPR036116; FN3_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; 2.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00004; NL; 2.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 2.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF49265; Fibronectin type III; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50923; SUSHI; 1.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
KW Sushi {ECO:0000256|PROSITE-ProRule:PRU00302}.
FT DOMAIN 1465..1533
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 53..82
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 127..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1724..1744
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 55..74
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..159
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..230
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1744 AA; 192130 MW; FE3B56EA802F5D3D CRC64;
MLLIRLLAVF LVFIANTWLL RSDALSLYKR SLARQADREL SRLAGEPCAV SGVWRSRRQP
SSHSPTQQRP PAARTRTHTS RRELYTVKSA RAVCAGGCGL EAGARGFAPA GEEEKGGRGD
AEMVAGREGG EYFGSPGSST DNQREQNEVG ASGGQSVKDA VSPSRAPRDP RSRFTRSLHG
TFRYEEEGNS SWEKVAPFSS TDSRGLQVLQ RLQQGDEDQS STATPESVTE DYSDEVQEGD
WLPAGTWGSP VPKVPPSWMT ALYFNGRREQ LKVKLPAGVE LPRATFSLEL WVKAEGGQSN
PAVIAGVFDN CSHSLSEKGW SVGIHTVETA GTRDARFYFT LRTDRAVKST TVHSHQRYQA
NVWTHLMAAY NGHNMTLYVD GAKVGESSHQ SGNLYSPFMK ACRTLFLGSN QSDQGQSFRG
HVGGVVLWGY ARSHADLLKR PLQIDMSEPV LVEQLWTPYK DHHPTIITSP VPEPELVSSF
SPPPCGLTPC DNIDIISGYN DNWQLRTPKR IRYRIVNLSN DDGGNPTVTE AQIQLQHQAL
TQAFRPYNIT LDLSVYTVKN SSLRERFILS NCRIAKIGNR QCDPECDHPR TGHDGGDCLR
LGPCYSWKRQ DGVCNMGCNS IHYDYDDGDC CDPDVTDVLK TCFDPDSPDR AYISVKELKE
ELKLSGTDTL NVFFASNSMR QELAGAATWP WAKEALTHQG GMVLNPSYFG TTGHSNTMIH
EMGHIFGLYH VFKGVSERDS CDDPCQETTP SMETGDLCAD TAPTPKSKAC HDPGAVNDTC
GVTTYLNTPY SNYMSYTDDN CTNHFTPNQV ARMHCYLDLV YQKWLMDPQP APIPLAPIVT
DQSTDSVSIY WLPPIRGSLY QRYDCMNCEK DGIFHQYAYE ASSTHICDTS GYWTPEEATG
PPDVEQPCDS SLQAWSPEFS LYDTNVTSPC PGTEGCTLTL RFLHPIVPHA LTLWVTYISA
NSPAIANIEL ISDTGKSINL GPQHVFCDLP LTMRLDTHNV AIAAIKFCTL EIMEIDAAML
SSGPGSPLCS SCQPLLYHIR RQPPFASKAP LPQTQQTFTD RSVTQGVKYK YTVQVEADGQ
LSDASPPLLY THGQPYCGDG LIQGTEECDD SNLLDGDGCS KRCGKEMGFK CNGEPSQCYV
FDGDGVCEEF ERSSSVQDCG YFTPLGYIDQ WASIATASHQ DRTRCPAHAA TGEPSLTKLC
TYHHLQGSEN LPPDAWFPCT AQSDINNDLE HSLWLKVGFA HPGVAASVMV YLASDGSWSR
EQCRRTVTIL LSDTADRNHT LGTHDLSCHR NPLVVNVTHD LSQPFFLTSS VILLLSSPTV
AVGGVALRTS CHFSTFALTG CASEGGLSHN YLLNTHTHTH PNVHTRYRQI AKIRPSKSYH
LGYKKAELEC FHGSWDRVVS CQPVDCGFPD QSHVYHAIFS CPWGTTFGKQ CSFTCGSPAI
LQGDSDRLVC LEDGLWSLPE AYCKIECPEV PSISDAKLLT ADCLASGHDV GSVCRYKCNP
GFYVLGSLKK KIRKHFKIEC QEGGQWEETG CEPISCPAPP DLFQGMYTCT NGLLSIVDFN
ACICFQVEMR CTKDGEWTAE FVMCPNLQGS CSAPPDLNSV EYSCDHGMAV GAECYPICIM
AVDLDLHDPV VLPNGTTVKS LKHWMVPKKV QSIVCTGMMK WYPDPQHIHC IQSCEPFGGD
GWCDTINNRA YCQYDGGDCC PSTLSTRKVI QFGADCTQDE CTCRDPDAEE NKSKAKHSEG
GGTQ
//
