ID G3SMX7_LOXAF Unreviewed; 1251 AA.
AC G3SMX7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 69.
DE SubName: Full=Papilin, proteoglycan like sulfated glycoprotein {ECO:0000313|Ensembl:ENSLAFP00000000907.3};
GN Name=PAPLN {ECO:0000313|Ensembl:ENSLAFP00000000907.3};
OS Loxodonta africana (African elephant).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Afrotheria; Proboscidea; Elephantidae; Loxodonta.
OX NCBI_TaxID=9785 {ECO:0000313|Ensembl:ENSLAFP00000000907.3, ECO:0000313|Proteomes:UP000007646};
RN [1] {ECO:0000313|Ensembl:ENSLAFP00000000907.3, ECO:0000313|Proteomes:UP000007646}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000907.3,
RC ECO:0000313|Proteomes:UP000007646};
RA Di Palma F., Heiman D., Young S., Johnson J., Lander E.S., Lindblad-Toh K.;
RT "The Genome Sequence of Loxodonta africana (African elephant).";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSLAFP00000000907.3}
RP IDENTIFICATION.
RC STRAIN=Isolate ISIS603380 {ECO:0000313|Ensembl:ENSLAFP00000000907.3};
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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DR AlphaFoldDB; G3SMX7; -.
DR STRING; 9785.ENSLAFP00000000907; -.
DR MEROPS; I02.972; -.
DR Ensembl; ENSLAFT00000001080.3; ENSLAFP00000000907.3; ENSLAFG00000001078.3.
DR eggNOG; KOG3510; Eukaryota.
DR eggNOG; KOG4597; Eukaryota.
DR GeneTree; ENSGT00940000156891; -.
DR HOGENOM; CLU_000660_7_0_1; -.
DR InParanoid; G3SMX7; -.
DR OMA; KLDSGWF; -.
DR TreeFam; TF316874; -.
DR Proteomes; UP000007646; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; 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; 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:SF179; PAPILIN; 1.
DR Pfam; PF19236; ADAMTS_CR_3; 1.
DR Pfam; PF05986; ADAMTS_spacer1; 1.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF00014; Kunitz_BPTI; 1.
DR Pfam; PF16626; Papilin_u7; 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; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000007646};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729}.
FT DOMAIN 742..792
FT /note="BPTI/Kunitz inhibitor"
FT /evidence="ECO:0000259|PROSITE:PS50279"
FT DOMAIN 879..973
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1012..1101
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1106..1191
FT /note="Ig-like"
FT /evidence="ECO:0000259|PROSITE:PS50835"
FT DOMAIN 1204..1243
FT /note="PLAC"
FT /evidence="ECO:0000259|PROSITE:PS50900"
FT REGION 537..618
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 671..705
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 786..881
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 990..1026
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1186..1206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 540..591
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 600..615
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 795..810
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 817..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 39..75
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 43..80
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
FT DISULFID 54..65
FT /evidence="ECO:0000256|PIRSR:PIRSR613273-3"
SQ SEQUENCE 1251 AA; 135745 MW; 0F40BA7E9FBDB284 CRC64;
LEYLPILLSL EGLALEALKV RRQRRQNDFW GPWGEWSPCS RTCGGGISFR ERPCYSQRRD
GAFSCVGPAR SHRSCRTESC PEGARDFRAE QCAEFDSVEF QGRHYKWLPY YGAPNKCELN
CIPKGENFYY KHKEAVVDGT PCEPGKRDVC VDGSCRVVGC DHKLDSPKQE DKCLQCGGDG
KTCYPVTGTF DANDLSRGYN QILIIPVGAT SIHIEEAAAS RNFLAVKNVR GEYYLNGHWT
IEAAGALPVA STVLQYERGT EGDLAPERLH ARGPTSEPLV IELISQEPNP GVHYEYYLPL
SIPDPGFHWN HGSWSDCSAE CGGGHQARLV FCTIDNEAYP DHLCQRQPRP VDRQPCNTHP
CPQTKRWKTG PWAPCSASCG GGSQSRSVYC VSANGAGIQE AADEAECAGL PRKPPTTQAC
NLQRCAAWSS EPWGECSVSC GSGVRRRTVT CQGDEGSVLH ATACSLEDRP PLTEPCVRDD
CPLLNDQTWH VGTWGLCSKS CNLGTRKRQV ICAIGPPNHC ESLQLSKPAD VEPCNTQPCH
LPQEVPSMQD VRTSSRDPRT SSGIRETAAS ESRGQWWAPQ GRSSAWSKTR GDQGPHLSAP
APSPSLQQSP RQQLPRDCRH SPHGCCPDGY TASLGPQWQG CPGVSCQQSR YGCCPDGVSV
AEGPHQAGCT RSYGSDNTGN RPRSRAVASV PPQAHRPQAQ QNQPSECRGS QFGCCYDNVA
SAAGPLGEGC VGQPSYAYPV QCLLPSAHGS CTDWAARWYF IASVGQCNRF WYGGCHGNAN
NFPSEEECVS SCRGPQPGAS AQSTHRDGGP RGQQEASKQR MGATVQRKPL PSSSLWRQDQ
EPELGEASHT QAIGEGPWGQ ERGPSIPRLG GDAGQPAQPS ISSSYRISLA GSEPTLVQAA
LGHLVRLFCP DDSSLDRHAG WQKDGRPISS DRHKLQADGS LVISPLRAED AGTYSCGSTR
PDLNSQKIQL RITGGDKAVL SEAEPRHFLQ SKDPAHGDAG GLGAVSSSHP RPTSRLRLDQ
NQPGVVDASP GQWIRLTCRA EGFPPPAIEW QKDGQSLSSP RHQLQPDGSL VISHVAVEDG
GFYACVAFNG QDRDQRWVQL RVLGELTITG LPTTVTVPEG DTARLLCVVA GENVNIRWSR
NGLPMRADGH RVHQAPDGTL LIYNLQARDE GSYTCSAYRG SQAASRSTEV KVVPPAPAPQ
PRDPGRECID QPELANCDLI LQAQLCGNEY YSSFCCASCS RVQPHTQPIW Q
//
