UniProt: A0A3P8N6G9

Database: UniProt
Entry: A0A3P8N6G9_ASTCA

LinkDB:  A0A3P8N6G9_ASTCA 
Original site:  A0A3P8N6G9_ASTCA

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Ontology (4)   
   GO (4)   
Gene (3)   
   ENSEMBL-UP (3)   
Protein domain (34)   
   InterPro (16)   
   Pfam (8)   
   PROSITE (5)   
   SMART (5)   
All databases (41)   

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ID   A0A3P8N6G9_ASTCA        Unreviewed;      1213 AA.
AC   A0A3P8N6G9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Papilin, proteoglycan like sulfated glycoprotein {ECO:0000313|Ensembl:ENSACLP00000000351.1};
GN   Name=PAPLN {ECO:0000313|Ensembl:ENSACLP00000000351.1};
OS   Astatotilapia calliptera (Eastern happy) (Chromis callipterus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Ovalentaria; Cichlomorphae; Cichliformes; Cichlidae; African cichlids;
OC   Pseudocrenilabrinae; Haplochromini; Astatotilapia.
OX   NCBI_TaxID=8154 {ECO:0000313|Ensembl:ENSACLP00000000351.1, ECO:0000313|Proteomes:UP000265100};
RN   [1] {ECO:0000313|Ensembl:ENSACLP00000000351.1, ECO:0000313|Proteomes:UP000265100}
RP   NUCLEOTIDE SEQUENCE.
RA   Datahose.;
RL   Submitted (MAY-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACLP00000000351.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
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DR   AlphaFoldDB; A0A3P8N6G9; -.
DR   STRING; 8154.ENSACLP00000000351; -.
DR   Ensembl; ENSACLT00000000364.1; ENSACLP00000000351.1; ENSACLG00000000279.1.
DR   GeneTree; ENSGT00940000156891; -.
DR   OMA; KLDSGWF; -.
DR   OrthoDB; 2910701at2759; -.
DR   Proteomes; UP000265100; Chromosome 19.
DR   Bgee; ENSACLG00000000279; Expressed in zone of skin and 5 other cell types or tissues.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004867; F:serine-type endopeptidase inhibitor activity; IEA:InterPro.
DR   GO; GO:0030198; P:extracellular matrix organization; IEA:InterPro.
DR   CDD; cd22635; Kunitz_papilin; 1.
DR   Gene3D; 2.60.120.830; -; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 4.10.410.10; Pancreatic trypsin inhibitor Kunitz domain; 1.
DR   Gene3D; 2.20.100.10; Thrombospondin type-1 (TSP1) repeat; 5.
DR   InterPro; IPR013273; ADAMTS/ADAMTS-like.
DR   InterPro; IPR045371; ADAMTS_CR_3.
DR   InterPro; IPR010294; ADAMTS_spacer1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR003598; Ig_sub2.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR002223; Kunitz_BPTI.
DR   InterPro; IPR036880; Kunitz_BPTI_sf.
DR   InterPro; IPR010909; PLAC.
DR   InterPro; IPR020901; Prtase_inh_Kunz-CS.
DR   InterPro; IPR000884; TSP1_rpt.
DR   InterPro; IPR036383; TSP1_rpt_sf.
DR   PANTHER; PTHR13723; ADAMTS A DISINTEGRIN AND METALLOPROTEASE WITH THROMBOSPONDIN MOTIFS PROTEASE; 1.
DR   PANTHER; PTHR13723:SF317; PAPILIN ISOFORM X1; 1.
DR   Pfam; PF19236; ADAMTS_CR_3; 1.
DR   Pfam; PF05986; ADAMTS_spacer1; 1.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF00014; Kunitz_BPTI; 1.
DR   Pfam; PF08686; PLAC; 1.
DR   Pfam; PF19030; TSP1_ADAMTS; 4.
DR   Pfam; PF00090; TSP_1; 1.
DR   PRINTS; PR01857; ADAMTSFAMILY.
DR   PRINTS; PR00759; BASICPTASE.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00406; IGv; 2.
DR   SMART; SM00131; KU; 1.
DR   SMART; SM00209; TSP1; 5.
DR   SUPFAM; SSF57362; BPTI-like; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   SUPFAM; SSF82895; TSP-1 type 1 repeat; 5.
DR   PROSITE; PS00280; BPTI_KUNITZ_1; 1.
DR   PROSITE; PS50279; BPTI_KUNITZ_2; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS50900; PLAC; 1.
DR   PROSITE; PS50092; TSP1; 5.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157,
KW   ECO:0000256|PIRSR:PIRSR613273-3}; Membrane {ECO:0000256|ARBA:ARBA00022989};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Secreted {ECO:0000256|ARBA:ARBA00022525};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022989};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..1213
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5018047604"
FT   DOMAIN          707..757
FT                   /note="BPTI/Kunitz inhibitor"
FT                   /evidence="ECO:0000259|PROSITE:PS50279"
FT   DOMAIN          854..952
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          955..1057
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1060..1147
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          1158..1197
FT                   /note="PLAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50900"
FT   REGION          758..833
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        769..830
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        33..69
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        37..74
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT   DISULFID        48..59
FT                   /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ   SEQUENCE   1213 AA;  132115 MW;  268CDCB1E375889E CRC64;
     MLLPLAILQL LLTPALMGPS VDYWDSWGPY GECSRTCGGG VTVRTRRCIT HREDGGHNCV
     GPDKSYRSCN IQDCPEGSRD FREEQCSQFD GTDFHGKRYK WLPYYGAENP CELNCMPRGE
     NFFYRHRRAV IDGTPCHPGR TDICVDGVCR RMGCDNMLES PQQEDPCLQC GGNGQSCYRV
     KNSFTARDLP TGYNQMFIIP VGATTISIRE THATRNYLAI KNLRGEYYLN GHWVIEFSRA
     TPIGGTMLYY QRGAEGDSVP ETIIGRGPTT EPLVVELISQ EPNQGVEYEY YLPNGRSREG
     YYWSYGSWSA CSKECGSGYQ SRLVFCSIDN EAYPDYLCAS LPRPQSNRTC NPQPCPQIRS
     WQTGEWNACS VTCGGGSQVR SVQCVSNDVS GPRVVEDAIC AAYADAPPPL QTCNMQKCAE
     YHVTGWSACS VTCGSGQQTR EVTCMGSDGT RLDETSCSAL LRPAAVQRCE MAPCPQQISW
     HVGDWGLCSK SCGSGSRERQ VICSDQERNL YPVDQCNTQP KPLTVERCNT QPCYSPQVVP
     SIQDPRGHDS TQIGFQPYVP DHATARRPET RDPTQTNTVY DPHSSAPALH CSQSYYGCCS
     DGHTSARGPQ GLGCPSAPAP SPVPTSCIQT SYGCCEDGVT AAQGPNKEGC AAYVNPAPTV
     TPSLPTENAV ECRTTTYGCC YDRTTPAGGP NGEGCPNPPN YIERSICSLP RAAGSCSSWV
     SRYHFDVISS KCVHFWYGGC HGNSNNFMTL AECKRTCPRP APSRQAPQPA APSGESTRTA
     AGEHSTTGAE TSAGRGSTTD GRSRNMGRIF IVQRGSTSST SRQATSAATN AHRGRVYLRV
     RRPSHGTAAQ HTGPAASLTL GGVTIDKTDP STVEALVGQT VVLPCRVSPP PSSTVVVEWR
     RDGIPLSTHR HHQQPNGSLL VGPVSKLDSG WFLCVATRER ERDHRYIYLA VSEGPSSTSL
     PRDGPFARFS IERSSSAQVE MRAGQTTRLP CTVVPSSARQ SVSIGWTKDG QLISDPRFTQ
     HSDGTLIIGP LKSDDSGVYT CTASNQQQLE QRQLQLRVQP DLKITTAPNN IQVSEGSTGM
     LPCVVSGDNV NIGWSRNGVP VRPDGRNILL SSDGSLILNN VKPSDQGTYT CNAYTGIYSV
     SATAEVKVIK ETQQGADLPP ECLDQPELAN CELIVYARLC SNSYYSSFCC ASCTRHSQKK
     RQVWSTRLKP QRV
//

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