ID A0A1I8G6K2_9PLAT Unreviewed; 1220 AA.
AC A0A1I8G6K2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=SRCR domain-containing protein {ECO:0000313|WBParaSite:maker-uti_cns_0001023-snap-gene-0.9-mRNA-1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0001023-snap-gene-0.9-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0001023-snap-gene-0.9-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00196}.
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DR AlphaFoldDB; A0A1I8G6K2; -.
DR WBParaSite; maker-uti_cns_0001023-snap-gene-0.9-mRNA-1; maker-uti_cns_0001023-snap-gene-0.9-mRNA-1; maker-uti_cns_0001023-snap-gene-0.9.
DR Proteomes; UP000095280; Unplaced.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR CDD; cd00037; CLECT; 1.
DR CDD; cd00112; LDLa; 2.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 2.40.128.620; -; 1.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 2.
DR Gene3D; 3.10.100.10; Mannose-Binding Protein A, subunit A; 1.
DR Gene3D; 3.10.250.10; SRCR-like domain; 3.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR001304; C-type_lectin-like.
DR InterPro; IPR016186; C-type_lectin-like/link_sf.
DR InterPro; IPR016187; CTDL_fold.
DR InterPro; IPR000001; Kringle.
DR InterPro; IPR013806; Kringle-like.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR003609; Pan_app.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR001190; SRCR.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR018114; TRYPSIN_HIS.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF7; HYALIN; 1.
DR Pfam; PF00057; Ldl_recept_a; 2.
DR Pfam; PF00059; Lectin_C; 1.
DR Pfam; PF00530; SRCR; 3.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR PRINTS; PR00258; SPERACTRCPTR.
DR SMART; SM00034; CLECT; 1.
DR SMART; SM00130; KR; 1.
DR SMART; SM00192; LDLa; 3.
DR SMART; SM00202; SR; 3.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF56436; C-type lectin-like; 1.
DR SUPFAM; SSF57440; Kringle-like; 1.
DR SUPFAM; SSF57424; LDL receptor-like module; 2.
DR SUPFAM; SSF56487; SRCR-like; 3.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
DR PROSITE; PS50070; KRINGLE_2; 1.
DR PROSITE; PS01209; LDLRA_1; 2.
DR PROSITE; PS50068; LDLRA_2; 3.
DR PROSITE; PS50948; PAN; 1.
DR PROSITE; PS50287; SRCR_2; 3.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00134; TRYPSIN_HIS; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00196}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU363034};
KW Kringle {ECO:0000256|PROSITE-ProRule:PRU00121};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|RuleBase:RU363034};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825,
KW ECO:0000256|RuleBase:RU363034}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..1220
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5009319141"
FT DOMAIN 194..301
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 313..437
FT /note="C-type lectin"
FT /evidence="ECO:0000259|PROSITE:PS50041"
FT DOMAIN 444..517
FT /note="Kringle"
FT /evidence="ECO:0000259|PROSITE:PS50070"
FT DOMAIN 528..622
FT /note="Apple"
FT /evidence="ECO:0000259|PROSITE:PS50948"
FT DOMAIN 669..775
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 820..923
FT /note="SRCR"
FT /evidence="ECO:0000259|PROSITE:PS50287"
FT DOMAIN 978..1217
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 108..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 172..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..960
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..147
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 630..648
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 798..813
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 892..902
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00196"
SQ SEQUENCE 1220 AA; 133749 MW; 7023BE3089DA767E CRC64;
MKATLLPCLL ALCCCQLSQQ MQLSEEQTLT RPRSSDRSYR TTFRSYRTTY RTYRRVGTTG
GAGQQMQTGD ISWDSDDLSI NGDNDLWSDS DIDIDTGGDF DFDDGIDGTG DIGGEDGLDW
SIDMSGGSGS GSGSGTGTGS GSGGQLKPGF NVMQLYGATN DPAQPSYPLV PSARPVDSSS
KYIDGRVPQP PQRVRLRGNQ SDMNPNEGRV EVFYNGQWGL VCDDHFSEAE ANVACLSLGF
KSGSNRVYSG SFFGTGGYSA RDIRMERLRC SPSAEEVGLH QCSHSHLNRC SLDNTAGVEC
QYNEGCEFGW TGFDGLCYRV EAASPKTPED AARVCEAQDS TLAYVLSESE NNFISNMLYT
KFNNLSAVWT GGQYALIERQ RSFGYQLSSM RPQDEEKKSC LALSKIFYNS RTRNNTEVNY
FWWDNVSCKT RLPFVCQKLA ETSDCYNGTG VDYMGDAIRT EDGSLCQMWA PPASNLPNAS
FDSPMCNRPD KFFCPSMINY RPTCVRRIDV CDGYKDCIGG EDESPSFCRS CAFRLEESAM
VYLTANSETT SALRLVKLIG LIICKARCDR SGRAAVTRCA GFIFTQQGIF NASECSLLTE
RLTEVTIGEA TSLTYYEKEQ TCDPTTQYSC QNGNCVSNRL KCNGFDDCGD FSDEVEPTSC
ERPRPTFSVR LSGGKGPYEG RLEVKLFKEW GLVCDDGLDA SLGELVCRNL GYSQGFERLV
FNAKREFSQG SGQFLMNSVD CSGINDTDAS LYDCQHAGWK QGSCSINNIA GLVCRRQRAC
TSKEFRCVDR CVPLSAMCNG ISDCPDMSDE MTCGNMTLQL RGINNSLTES AGFLEVVRGN
ISGTICDDQF GERELQVACR HLGFARGRGR IVSQGTYEVP RDLVMWVHDI ACNGLESNLF
DCNIASWGNS HCDVSEAVAI QCGLPDTTTQ LPTTTAAPTT TQRTTTKPPP GATTTIGPTT
SSLPGCGKRF GRFPMGRIIN GYKAISGQFP WQVGIRLRLS STQHQQWCGG TIISDRWIVS
AAHCFEEHPK SSYMLRIGDV DNSMREKNER EMNVDLLIKH PGYTGNPEFD YDIALLRVKP
DRLGYIKFHD TVQPACLPDR DLVPLPGTAC HISGWGSIGA YDPPKNLMAA KVPLIDHARC
NQLYLNRITQ RMLCAGYEAG GIDSCQGDSG GPLVCSINGT YVLLGATSWG EGCAQPGAPG
VYANVKNLRE WIDQTIASNP
//
