ID A0A2K5UDA6_MACFA Unreviewed; 1091 AA.
AC A0A2K5UDA6;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Corin, serine peptidase {ECO:0000313|Ensembl:ENSMFAP00000010354.2};
GN Name=CORIN {ECO:0000313|Ensembl:ENSMFAP00000010354.2};
OS Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9541 {ECO:0000313|Ensembl:ENSMFAP00000010354.2, ECO:0000313|Proteomes:UP000233100};
RN [1] {ECO:0000313|Ensembl:ENSMFAP00000010354.2, ECO:0000313|Proteomes:UP000233100}
RP NUCLEOTIDE SEQUENCE.
RA Warren W., Wilson R.K.;
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSMFAP00000010354.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-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; A0A2K5UDA6; -.
DR Ensembl; ENSMFAT00000040253.2; ENSMFAP00000010354.2; ENSMFAG00000036209.2.
DR VEuPathDB; HostDB:ENSMFAG00000036209; -.
DR GeneTree; ENSGT00940000157103; -.
DR Proteomes; UP000233100; Chromosome 5.
DR Bgee; ENSMFAG00000036209; Expressed in heart and 4 other cell types or tissues.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0016486; P:peptide hormone processing; IEA:InterPro.
DR GO; GO:0008217; P:regulation of blood pressure; IEA:InterPro.
DR CDD; cd07445; CRD_corin_1; 1.
DR CDD; cd07888; CRD_corin_2; 1.
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; IPR017052; Corin.
DR InterPro; IPR041762; Corin_CRD_1.
DR InterPro; IPR041763; Corin_CRD_2.
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 PANTHER; PTHR24252; ACROSIN-RELATED; 1.
DR PANTHER; PTHR24252:SF9; ATRIAL NATRIURETIC PEPTIDE-CONVERTING ENZYME ISOFORM X1; 1.
DR Pfam; PF01392; Fz; 2.
DR Pfam; PF00057; Ldl_recept_a; 6.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036376; Corin; 1.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 2.
DR SMART; SM00192; LDLa; 7.
DR SMART; SM00202; SR; 1.
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; 2.
DR PROSITE; PS50068; LDLRA_2; 7.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
PE 4: Predicted;
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00124}; Glycoprotein {ECO:0000256|ARBA:ARBA00023180};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000233100};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 134..259
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 450..573
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 802..1063
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 7..21
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 216..240
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 277..295
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 289..304
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 306..318
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 313..331
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 325..340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 350..368
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 362..377
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 387..405
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 399..414
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 502..540
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 529..570
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 533..557
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 580..592
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 587..605
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 599..614
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 637..652
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 655..667
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 662..680
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 674..689
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 1091 AA; 122050 MW; 2E16E06539108C7E CRC64;
MKQSTSLAPE ERYRRAGSSK PVLRADDNNM GNGCSQKLAT ANPLRFLLLV LIPCICALVL
LLVILLSYVG TLQKVYFKSN GSEPLVTDGE IQGSDVILTN TIYNQSTVIS TAHPDQHIPA
WTTDASLPGD QSHRNTSACM NITHSQCQML PYHSTPTPLL SVVRNMEMEK FLKFFTYLHR
LSCYQHIMLF GCSLAFPECI IDGDDSHGLL PCRSFCEAAK EGCESVLGMV NYSWPDFLKC
SQFRNHTESS DVSRICFSPQ QENGKQLLCG GGESFLCASG ICIPRKLQCN GYNDCDDWSD
EAHCNCSENL FHCHTGKCLN YSLVCDGYDD CGDLSDEQNC DCNPTTEHRC GDGRCIAMEW
VCDGDHDCVD KSDEVNCSCH SQGLVECRNG QCIPSTFQCD GDEDCKDGSD EENCSGSQTP
CQEGDRRCLY IACIDSCGGS SLCDPNNSLN NCSQCEPITL ELCMNLPYNS TSYPNYLGHR
TQKEASISWE SSLFPALVQT NCYKYLMFFA CTILVPKCDV NTGQSIPPCR ALCEHSKERC
ESVLGIVGLQ WPEDTDCSQF PEENSDNQTC LMPDEYVEEC SPSHFKCRSG RCVLASRRCD
GQADCDDDSD EENCGCKERD LWECPSNKQC LKHTVICDGF PDCPDYMDEK NCSFCQDDEL
ECANHACVSR NLWCDGEADC SDSSDEWDCV TLSINVNSSS FLMVHRAATE HHVCADGWQE
MFSQLACKQM GLGEPSVTEL IQEQEKELRW LTLHSNWESL NGTTLHELLV NGQSCQSRSK
ISLLCTKQDC GRRPAARMNK RILGGRTSRP GRWPWQCSLQ SEPSGHICGC VLIAKKWVLT
VAHCFEGREN AAVWKVVLGI NNLDHPSVFM QTRFVKTIIL HPRYSRAVVD YDISIIELNE
DISETGYVRP VCLPSPEQWL EPDTYCYITG WGHMGNKMPF KLQEGEVRII SLEQCQSYFD
MKTITTRMIC AGYESGTVDS CMQAELLEHW GLSHTWETSS STGEAGFIRL KRGSLLTKAF
GTPEDGSFPL LSDGELDLRT DNLWKRLLIS SKDLMGNPPS EGCLIYERQF RKVSIQSKAV
YNNFEGKLDI N
//
