ID A0A087X1D5_HUMAN Unreviewed; 938 AA.
AC A0A087X1D5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Corin, serine peptidase {ECO:0000313|Ensembl:ENSP00000484087.1};
GN Name=CORIN {ECO:0000313|Ensembl:ENSP00000484087.1};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000484087.1, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000484087.1, ECO:0000313|Proteomes:UP000005640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [2] {ECO:0000313|Ensembl:ENSP00000484087.1}
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 EMBL; AC092597; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC104646; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107068; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_001265514.1; NM_001278585.1.
DR AlphaFoldDB; A0A087X1D5; -.
DR SMR; A0A087X1D5; -.
DR MEROPS; S01.019; -.
DR MassIVE; A0A087X1D5; -.
DR PeptideAtlas; A0A087X1D5; -.
DR Antibodypedia; 23775; 382 antibodies from 27 providers.
DR DNASU; 10699; -.
DR Ensembl; ENST00000610355.4; ENSP00000484087.1; ENSG00000145244.12.
DR GeneID; 10699; -.
DR UCSC; uc032tif.2; human.
DR CTD; 10699; -.
DR HGNC; HGNC:19012; CORIN.
DR VEuPathDB; HostDB:ENSG00000145244; -.
DR GeneTree; ENSGT00940000157103; -.
DR OrthoDB; 4252799at2759; -.
DR BioGRID-ORCS; 10699; 7 hits in 1149 CRISPR screens.
DR ChiTaRS; CORIN; human.
DR GenomeRNAi; 10699; -.
DR Proteomes; UP000005640; Chromosome 4.
DR Bgee; ENSG00000145244; Expressed in cardiac muscle of right atrium and 118 other cell types or tissues.
DR ExpressionAtlas; A0A087X1D5; baseline and differential.
DR GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
DR GO; GO:0016604; C:nuclear body; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
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; 6.
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; 6.
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 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; 2.
DR Pfam; PF00057; Ldl_recept_a; 5.
DR Pfam; PF15494; SRCR_2; 1.
DR Pfam; PF00089; Trypsin; 1.
DR PIRSF; PIRSF036376; Corin; 3.
DR PRINTS; PR00261; LDLRECEPTOR.
DR SMART; SM00063; FRI; 2.
DR SMART; SM00192; LDLa; 6.
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; 6.
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; 6.
DR PROSITE; PS50240; TRYPSIN_DOM; 1.
DR PROSITE; PS00135; TRYPSIN_SER; 1.
PE 1: Evidence at protein level;
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 Proteomics identification {ECO:0007829|MaxQB:A0A087X1D5,
KW ECO:0007829|PeptideAtlas:A0A087X1D5};
KW Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 46..71
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 67..192
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 346..469
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 698..931
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT REGION 1..24
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 ACT_SITE 739
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT ACT_SITE 788
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT ACT_SITE 881
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT DISULFID 149..173
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 210..228
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 222..237
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 239..251
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 246..264
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 258..273
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 283..301
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 295..310
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 398..436
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 425..466
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 429..453
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 476..488
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 483..501
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 495..510
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 533..548
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 551..563
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 558..576
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 570..585
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 938 AA; 105121 MW; 943C7FC5E7D21C10 CRC64;
MKQSPALAPE ERCRRAGSPK PVLRADDNNM GNGCSQKLAT ANLLRFLLLV LIPCICALVL
LLVILLSYVG ACMNITHSQC QMLPYHATLT PLLSVVRNME MEKFLKFFTY LHRLSCYQHI
MLFGCTLAFP ECIIDGDDSH GLLPCRSFCE AAKEGCESVL GMVNYSWPDF LRCSQFRNQT
ESSNVSRICF SPQQENGKQL LCGRGENFLC ASGICIPGKL QCNGYNDCDD WSDEAHCNCS
ENLFHCHTGK CLNYSLVCDG YDDCGDLSDE QNCACHSQGL VECRNGQCIP STFQCDGDED
CKDGSDEENC SVIQTSCQEG DQRCLYNPCL DSCGGSSLCD PNNSLNNCSQ CEPITLELCM
NLPYNSTSYP NYFGHRTQKE ASISWESSLF PALVQTNCYK YLMFFSCTIL VPKCDVNTGE
HIPPCRALCE HSKERCESVL GIVGLQWPED TDCSQFPEEN SDNQTCLMPD EYVEECSPSH
FKCRSGQCVL ASRRCDGQAD CDDDSDEENC GCKERDLWEC PSNKQCLKHT VICDGFPDCP
DYMDEKNCSF CQDDELECAN HACVSRDLWC DGEADCSDSS DEWDCVTLSI NVNSSSFLMV
HRAATEHHVC ADGWQEILSQ LACKQMGLGE PSVTKLIQEQ EKEPRWLTLH SNWESLNGTT
LHELLVNGQS CESRSKISLL CTKQDCGRRP AARMNKRILG GRTSRPGRWP WQCSLQSEPS
GHICGCVLIA KKWVLTVAHC FEGRENAAVW KVVLGINNLD HPSVFMQTRF VKTIILHPRY
SRAVVDYDIS IVELSEDISE TGYVRPVCLP NPEQWLEPDT YCYITGWGHM GNKMPFKLQE
GEVRIISLEH CQSYFDMKTI TTRMICAGYE SGTVDSCMGD SGGPLVCEKP GGRWTLFGLT
SWGSVCFSKV LGPGVYSNVS YFVEWIKRQI YIQTFLLN
//
