ID S4RCE1_PETMA Unreviewed; 843 AA.
AC S4RCE1;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Corin, serine peptidase {ECO:0000313|Ensembl:ENSPMAP00000002873.1};
OS Petromyzon marinus (Sea lamprey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Cyclostomata;
OC Hyperoartia; Petromyzontiformes; Petromyzontidae; Petromyzon.
OX NCBI_TaxID=7757 {ECO:0000313|Ensembl:ENSPMAP00000002873.1, ECO:0000313|Proteomes:UP000245300};
RN [1] {ECO:0000313|Ensembl:ENSPMAP00000002873.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00124}.
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DR AlphaFoldDB; S4RCE1; -.
DR STRING; 7757.ENSPMAP00000002873; -.
DR Ensembl; ENSPMAT00000002887.1; ENSPMAP00000002873.1; ENSPMAG00000002612.1.
DR GeneTree; ENSGT00940000157103; -.
DR HOGENOM; CLU_010853_0_0_1; -.
DR OMA; HCSREQT; -.
DR Proteomes; UP000245300; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR CDD; cd00112; LDLa; 7.
DR CDD; cd00190; Tryp_SPc; 1.
DR Gene3D; 1.10.2000.10; Frizzled cysteine-rich domain; 2.
DR Gene3D; 4.10.400.10; Low-density Lipoprotein Receptor; 7.
DR Gene3D; 2.40.10.10; Trypsin-like serine proteases; 1.
DR InterPro; IPR020067; Frizzled_dom.
DR InterPro; IPR036790; Frizzled_dom_sf.
DR InterPro; IPR036055; LDL_receptor-like_sf.
DR InterPro; IPR023415; LDLR_class-A_CS.
DR InterPro; IPR002172; LDrepeatLR_classA_rpt.
DR InterPro; IPR009003; Peptidase_S1_PA.
DR InterPro; IPR043504; Peptidase_S1_PA_chymotrypsin.
DR InterPro; IPR017448; SRCR-like_dom.
DR InterPro; IPR036772; SRCR-like_dom_sf.
DR InterPro; IPR001254; Trypsin_dom.
DR InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF9; ATRIAL NATRIURETIC PEPTIDE-CONVERTING ENZYME ISOFORM X1; 1.
DR Pfam; PF01392; Fz; 1.
DR Pfam; PF00057; Ldl_recept_a; 6.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 1.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00020; Tryp_SPc; 1.
DR SUPFAM; SSF63501; Frizzled cysteine-rich domain; 2.
DR SUPFAM; SSF57424; LDL receptor-like module; 7.
DR SUPFAM; SSF56487; SRCR-like; 1.
DR SUPFAM; SSF50494; Trypsin-like serine proteases; 1.
DR PROSITE; PS50038; FZ; 2.
DR PROSITE; PS01209; LDLRA_1; 5.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Reference proteome {ECO:0000313|Proteomes:UP000245300}.
FT DOMAIN 1..53
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 241..363
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 604..838
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 201..221
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 8..32
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 68..86
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 80..95
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 97..109
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 104..122
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 116..131
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 141..159
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 153..168
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 178..196
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 190..205
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 293..331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 324..348
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 380..398
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 392..407
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 430..445
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 448..460
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 455..473
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 467..482
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 843 AA; 93213 MW; 41B92A2E2213C2C2 CRC64;
VLPCMSYCDA ARSSCERAFT QVGLGWPEFL SCYHFHNDRK KETMSITWVC FTPQMFNGRK
IACGGFWCSS RLCISKKLVC NGYNDCGDWS DEKLCSCGAG EFRCGTGRCV ALSQRCDGFN
DCGDLSDEAA CHCDNAVWFR CGDGVCVSRA WVCDGDADCS DRSDELNCTC KSHGMQECDG
GLCIPPSYLC DGERDCEDGR DEEGCGPANE SDSDSEPRCF PDPSLTSNGG GEICSAMNSF
KGLNLCEPIT LEWCLNQPYN ATGFPNALGH GTQASAAASW EAELLQALTH TACHPHMTFL
SCALLLPKCK PNSSHKILPC RSLCEEVRGS CERHLLNVGL SWPPEAECGR LSQWGPPDAC
LLPDASNADA RCSPLLHFRC ASGRCVSAAR RCDSRSDCDD ASDEQDCECA QRGMWECLSD
KSCINLDMHC DGFPDCRDEE DEKFCSQCEV EEMACLNHQC VPQRAWCDGE RHCADGSDEW
DCELFSLNVN HNELLVHRHA QSRLVCSDGW GAALSHLACA QMGFWGEADT RFLQRAVRKK
FLPPLHLTPG WHQTNTSTVQ AALAEGVPCD SESVVSVICH RNDVRADCGR RSSSPPPRRI
SKRILGGRVS REGRWPWQGS LRTALRPHSC GCTLIHRRWA LTGAHCFTRQ DDPEAWTAVF
GVNNLGHLSA FRQERKVRRI IRHERFSART LDYDVALVEL REEVWENPHV QPACLPHRGV
GVPDDTYCVI TGWGVTSAKV VPSKLQEGEV RIISPSTCQG FFPLRPLTPR MLCAGYEAGS
VDSCMGDSGG PLVCEETDRR WTLYGLTSWG SVCSSKSVGP GVYTNVTQLL GWIERHIFLH
TFF
//
