ID G3QW20_GORGO Unreviewed; 1513 AA.
AC G3QW20;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Pappalysin 1 {ECO:0000313|Ensembl:ENSGGOP00000006962.2};
GN Name=PAPPA {ECO:0000313|Ensembl:ENSGGOP00000006962.2};
OS Gorilla gorilla gorilla (Western lowland gorilla).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Gorilla.
OX NCBI_TaxID=9595 {ECO:0000313|Ensembl:ENSGGOP00000006962.2, ECO:0000313|Proteomes:UP000001519};
RN [1] {ECO:0000313|Ensembl:ENSGGOP00000006962.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Scally A.;
RT "Insights into the evolution of the great apes provided by the gorilla
RT genome.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSGGOP00000006962.2, ECO:0000313|Proteomes:UP000001519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22398555; DOI=10.1038/nature10842;
RA Scally A., Dutheil J.Y., Hillier L.W., Jordan G.E., Goodhead I.,
RA Herrero J., Hobolth A., Lappalainen T., Mailund T., Marques-Bonet T.,
RA McCarthy S., Montgomery S.H., Schwalie P.C., Tang Y.A., Ward M.C., Xue Y.,
RA Yngvadottir B., Alkan C., Andersen L.N., Ayub Q., Ball E.V., Beal K.,
RA Bradley B.J., Chen Y., Clee C.M., Fitzgerald S., Graves T.A., Gu Y.,
RA Heath P., Heger A., Karakoc E., Kolb-Kokocinski A., Laird G.K., Lunter G.,
RA Meader S., Mort M., Mullikin J.C., Munch K., O'Connor T.D., Phillips A.D.,
RA Prado-Martinez J., Rogers A.S., Sajjadian S., Schmidt D., Shaw K.,
RA Simpson J.T., Stenson P.D., Turner D.J., Vigilant L., Vilella A.J.,
RA Whitener W., Zhu B., Cooper D.N., de Jong P., Dermitzakis E.T.,
RA Eichler E.E., Flicek P., Goldman N., Mundy N.I., Ning Z., Odom D.T.,
RA Ponting C.P., Quail M.A., Ryder O.A., Searle S.M., Warren W.C.,
RA Wilson R.K., Schierup M.H., Rogers J., Tyler-Smith C., Durbin R.;
RT "Insights into hominid evolution from the gorilla genome sequence.";
RL Nature 483:169-175(2012).
RN [3] {ECO:0000313|Ensembl:ENSGGOP00000006962.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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 EMBL; CABD030066032; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030066033; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030066034; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030066035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CABD030066036; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR STRING; 9593.ENSGGOP00000006962; -.
DR MEROPS; M43.004; -.
DR Ensembl; ENSGGOT00000007148.3; ENSGGOP00000006962.2; ENSGGOG00000007107.3.
DR eggNOG; ENOG502QQ7Z; Eukaryota.
DR GeneTree; ENSGT00940000156654; -.
DR InParanoid; G3QW20; -.
DR OMA; KQVVCEP; -.
DR TreeFam; TF331636; -.
DR Proteomes; UP000001519; Chromosome 9.
DR Bgee; ENSGGOG00000007107; Expressed in adult mammalian kidney and 1 other cell type or tissue.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0006508; P:proteolysis; IBA:GO_Central.
DR CDD; cd00033; CCP; 4.
DR CDD; cd04275; ZnMc_pappalysin_like; 1.
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; 4.
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:SF2; PAPPALYSIN-1; 1.
DR Pfam; PF13385; Laminin_G_3; 1.
DR Pfam; PF05572; Peptidase_M43; 1.
DR Pfam; PF00084; Sushi; 3.
DR SMART; SM00032; CCP; 4.
DR SMART; SM00560; LamGL; 1.
DR SMART; SM00004; NL; 3.
DR SUPFAM; SSF57535; Complement control module/SCR domain; 4.
DR SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR SUPFAM; SSF55486; Metalloproteases ('zincins'), catalytic domain; 1.
DR PROSITE; PS50923; SUSHI; 3.
PE 3: Inferred from homology;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00302}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000001519};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW Sushi {ECO:0000256|ARBA:ARBA00022659, ECO:0000256|PROSITE-
KW ProRule:PRU00302}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..1513
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003451643"
FT DOMAIN 1099..1168
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1169..1230
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT DOMAIN 1299..1359
FT /note="Sushi"
FT /evidence="ECO:0000259|PROSITE:PS50923"
FT REGION 619..640
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 1301..1344
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00302"
SQ SEQUENCE 1513 AA; 168433 MW; 264BF75B61063764 CRC64;
MRLWSWVLHL GLLSAAQRSP AVITGLYDKC SYTSRDRGWV VGIHTISDQD NKDPRYFFSL
KTDRARQVTT INAHRSYLPG QWVYLAATYD GQFMKLYVNG AQVATSGEQV GGIFSPLTQK
CKVLMLGGSA LNHNYRGYIE HFSLWKVART QREILSDMET HGAHTALPQL LLQENWDNVK
HAWSPMKDGS SPKVEFSNAH GFLLDTSLEP PLCGQTLCDN TEVIASYNQL PSFRQPKVVR
YRVVNLYEDD HKNPTVTREQ VDFQHLQLAE AFKHYNISWE LDVLEVSNSS LRRRLILANC
DISKIGDENC DPECNHTLTG HDGGDCRHLR HPAFVKKQQN GVCDMDCNYE RFNFDGGECC
DPEITNVTQT CFDPDSPHRA YLDVNELKNI LKLDGSTHLN IFFAKSSEEE LAGVATWPWD
KEALMHLGGI VLNPSFYGMP GHTHTMIHEI GHSLGLYHVF RGISEIQSCS DPCMETEPSF
ETGDLCNDTN PAPKHKSCGD PGPGNDTCGF HSFFNTPYNN FMSYADDDCT DSFTPNQVAR
MHCYLDLVYQ GWQPSRKPAP VALAPQVVGH TTDSVTLEWF PPIDGDFFER ELGSACHLCL
EGRILVQYAS NASSPMPCSP SGHWSPREAE GHPDVEQPCK SSVRTWSPNS AVNPHTVPPA
CPEPQGCYLE LEFLYPLVPE SLTIWVTFVS TDWDSSGAVN DIKLLTVSGK NISLGPQNVF
CDVPLTIRLW DVGEEVYGIQ IYTLDEHLEI DAAMLTSTAD TPLCLQCKPL KYKVVRDPPL
QVDVASILHL NRKFVDMDLN LGSVYQYWVI TISGTEESEP SPAVTYIHGS GYCGDGIIQK
DQGEQCDDMN KINGDGCSLF CRQEVSFNCI DEPSRCYFHD GDGVCEEFEQ KTSIKDCGVY
TPQGFLDQWA SNASVSHQDQ QCPGWVIIGQ PAASQVCRTK VIDLSEGISQ HAWYPCTISY
PYSQLAQTTF WLRAYFSQPM VAAAVIVHLV TDGTYYGDQK QETISVQLLD TKDQSHDLGL
HVLSCRNNPL IIPVVHDLSQ PFYHSQAVRV SFSSPLVAIS GVALRSFDNF DPVTLSSCQR
GETYSPAEQS CVHFACEKTD CPELAVENAS LNCSSSDRYH GAQCTVSCRT GYVLQIRRDD
ELIKSQTGPS VTVTCTEGKW NKQVACEPVD CSIPDHHQVY AASFSCPEGT TFGSQCSFQC
RHPAQLKGNN SLLTCMEDGL WSFPEALCEL LCLAPPPVPN ADLQTARCRE NKHKVGSFCK
YKCKPGYHVP GSSRKSKKRA FKTQCTQDGS WQEGACVPVT CDPPPPKFHG LYQCTNGFQF
NSECRIKCED SDASQGLGSN VIHCRKDGTW NGSFHVCQEM QGQCSVPNQL NSNLKLQCPD
GYAIGSECAT SCLDHNSESI ILPMNVTVRD IPHWLNPTRV ERVVCTAGLK WYPHPALIHC
VKGCEPFMGD NYCDAINNRA FCNYDGGDCC TSTVKTKKVT PFPMSCDLQG DCACRDPQAQ
EHSRKDLRGY SHG
//
