ID H0V903_CAVPO Unreviewed; 980 AA.
AC H0V903;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 2.
DT 24-JAN-2024, entry version 88.
DE SubName: Full=Corin, serine peptidase {ECO:0000313|Ensembl:ENSCPOP00000006276.3};
GN Name=CORIN {ECO:0000313|Ensembl:ENSCPOP00000006276.3};
OS Cavia porcellus (Guinea pig).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC Cavia.
OX NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000006276.3, ECO:0000313|Proteomes:UP000005447};
RN [1] {ECO:0000313|Proteomes:UP000005447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX PubMed=21993624; DOI=10.1038/nature10530;
RA Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL Nature 478:476-482(2011).
RN [2] {ECO:0000313|Ensembl:ENSCPOP00000006276.3}
RP IDENTIFICATION.
RC STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000006276.3};
RG Ensembl;
RL Submitted (JUL-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; AAKN02028214; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02028215; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02028216; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02028217; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02028218; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAKN02028219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; H0V903; -.
DR STRING; 10141.ENSCPOP00000006276; -.
DR Ensembl; ENSCPOT00000007026.3; ENSCPOP00000006276.3; ENSCPOG00000006957.4.
DR VEuPathDB; HostDB:ENSCPOG00000006957; -.
DR eggNOG; KOG3577; Eukaryota.
DR eggNOG; KOG3627; Eukaryota.
DR GeneTree; ENSGT00940000157103; -.
DR HOGENOM; CLU_010853_0_0_1; -.
DR InParanoid; H0V903; -.
DR OMA; HCSREQT; -.
DR TreeFam; TF351678; -.
DR Proteomes; UP000005447; Unassembled WGS sequence.
DR Bgee; ENSCPOG00000006957; Expressed in heart and 8 other cell types or tissues.
DR GO; GO:0015629; C:actin cytoskeleton; IEA:Ensembl.
DR GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR GO; GO:0016604; C:nuclear body; IEA:Ensembl.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:Ensembl.
DR GO; GO:0007565; P:female pregnancy; IEA:Ensembl.
DR GO; GO:0016486; P:peptide hormone processing; IEA:Ensembl.
DR GO; GO:0035813; P:regulation of renal sodium excretion; IEA:Ensembl.
DR GO; GO:0003050; P:regulation of systemic arterial blood pressure by atrial natriuretic peptide; IEA:Ensembl.
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 InterPro; IPR033116; TRYPSIN_SER.
DR PANTHER; PTHR24252:SF8; ACROSIN; 1.
DR PANTHER; PTHR24252; ACROSIN-RELATED; 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; 2.
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.
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 Hydrolase {ECO:0000256|ARBA:ARBA00022825};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Protease {ECO:0000256|ARBA:ARBA00022825};
KW Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW Serine protease {ECO:0000256|ARBA:ARBA00022825};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145}.
FT TRANSMEM 48..73
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 72..194
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 385..508
FT /note="FZ"
FT /evidence="ECO:0000259|PROSITE:PS50038"
FT DOMAIN 737..970
FT /note="Peptidase S1"
FT /evidence="ECO:0000259|PROSITE:PS50240"
FT ACT_SITE 778
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT ACT_SITE 827
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT ACT_SITE 920
FT /note="Charge relay system"
FT /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT DISULFID 151..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 212..230
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 224..239
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 241..253
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 248..266
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 260..275
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 285..303
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 297..312
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 322..340
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 334..349
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 437..475
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 464..505
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 468..492
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT DISULFID 515..527
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 522..540
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 534..549
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 572..587
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 590..602
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 597..615
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT DISULFID 609..624
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ SEQUENCE 980 AA; 109228 MW; 40082C8EC2153710 CRC64;
MFTKQCPGLA PEERYRPSGA PKRVLGVDDN NVGDGCSQKL AAVNLLRFLL LVLIPCICAL
VVLLVILLCL VGACVTVTHS QCQMLPYHTT LTSPVSTIVN VETEKFLKFF TYLHRLSCYK
YIMLFGCSLA FPECIIDGDD RHGLQPCRSF CEAAKEGCEP VLEMVNASWP NFLKCSQFRN
QTESSNISRI CFSPQQGNGK QLLCGGGDHF LCTSGICIPR TLQCNGYNDC DDWSDETHCN
CTVDLFRCHT GKCLNYSFVC DGYDDCGDLS DEQNCDCDPT KEHRCGDGRC ISVEWVCDGD
HDCVDKSDEV NCSCHSQGLV ECGNGQCIPS AFQCDGDEDC RDASDERNCS APQTPCQEGD
QRCLFSSCLD SCGGSSLCDP DNGLNNCSQC EPITLELCMN LPYNHTKYPN YLGHRTQKEA
SISWESSLFP ALVPTNCYKY LMFFACTILV PKCDVTTSQR IPPCRALCEH SKERCESVLG
IVGLQWPEDT DCSQFPEENS DNQTCLMPDE DVEECSPSHF KCHSGGCVLA FRRCDGQADC
DDDSDEENCG CKERDLWECP SNKQCLKHSV ICDGFPDCPD NMDEKNCSFC QDDEVECANH
KCVSRELWCD GEADCSDSSD EWNCVTLSKT MNSSALLYVH RSATEHHVCA DGWQETLSQL
ACRQMGLGEP SLTESIPEEE ENQQWLRLRS DWKNVSGTAL HRLLVPGQAC PSRNKISLLC
TKEDCGRRPA ARMNKRILGG RTSRPGRWPW QCSLQSEPSG HICGCVLIAK KWVLTVAHCF
EGRENSAMWK VVLGINNLDH PSTYTQTRLV KTIILHPRYS RAVVDYDISI VELNEDINET
SYVRPICLPS PGQALEPDTY CYITGWGHMG NKMPFKLQEG EVRIISLEQC QSYFDMKTIT
TRMICAGYES GTVDSCMGDS GGPLVCEQPG GQWTLFGLTS WGSICFSKVL GPGVYSNVSY
FVGWIEKQIY IQTFLPRKKG
//