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Database: UniProt
Entry: A0A2K6KT78_RHIBE
LinkDB: A0A2K6KT78_RHIBE
Original site: A0A2K6KT78_RHIBE 
ID   A0A2K6KT78_RHIBE        Unreviewed;       984 AA.
AC   A0A2K6KT78;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Corin, serine peptidase {ECO:0000313|Ensembl:ENSRBIP00000014474.1};
GN   Name=CORIN {ECO:0000313|Ensembl:ENSRBIP00000014474.1};
OS   Rhinopithecus bieti (Black snub-nosed monkey) (Pygathrix bieti).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Colobinae; Rhinopithecus.
OX   NCBI_TaxID=61621 {ECO:0000313|Ensembl:ENSRBIP00000014474.1, ECO:0000313|Proteomes:UP000233180};
RN   [1] {ECO:0000313|Ensembl:ENSRBIP00000014474.1, ECO:0000313|Proteomes:UP000233180}
RP   NUCLEOTIDE SEQUENCE.
RA   Wu, C.-I. and Zhang, Y.;
RT   "Genome of Rhinopithecus bieti.";
RL   Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSRBIP00000014474.1}
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; A0A2K6KT78; -.
DR   Ensembl; ENSRBIT00000038308.1; ENSRBIP00000014474.1; ENSRBIG00000031285.1.
DR   GeneTree; ENSGT00940000157103; -.
DR   Proteomes; UP000233180; 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: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; 2.
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   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:UP000233180};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        25..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          113..238
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          392..515
FT                   /note="FZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50038"
FT   DOMAIN          744..977
FT                   /note="Peptidase S1"
FT                   /evidence="ECO:0000259|PROSITE:PS50240"
FT   ACT_SITE        785
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT   ACT_SITE        834
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT   ACT_SITE        927
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR036376-50"
FT   DISULFID        195..219
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        256..274
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        268..283
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        285..297
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        292..310
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        304..319
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        329..347
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        341..356
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        444..482
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        471..512
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        475..499
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00090"
FT   DISULFID        522..534
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        529..547
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        541..556
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        579..594
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        597..609
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        604..622
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
FT   DISULFID        616..631
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00124"
SQ   SEQUENCE   984 AA;  110135 MW;  D9BA89304E166194 CRC64;
     VLRADDNNMG NGCSQKLVTA NLLRFLLLVL IPCICALILL LVILLSYVGT LQKVYFKSNG
     SEPLVTDGEI QGSDVILTNT IYNQSTVIST AHPDQHIPAW TTDASLPGDQ SHRNTSACMN
     ITHSQCQMLP YHSTLTPLLS VVRNMEMEKF LKFFTYLHRL SCYQHIMLFG CSLAFPECII
     DGDDSHGLLP CRSFCEAAKE GCESVLGMVN YSWPDFLKCS QFRNHTESSN VSRICFSPQQ
     ENGKQLLCGG GESFLCASGI CIPRKLQCNG YNDCDDWSDE AHCNCSENLF HCHTGKCLNY
     SLVCDGYDDC GDLSDEQNCA CHSQGLVECR NGQCIPSTFQ CDGDEDCKDG SDEENCSGSQ
     TLCQEGDRRC LYIPCIDLCG GSSLCDPNNS LNNCSQCEPI TLELCMNLPY NSTSYPNYLG
     HRTQKEASIS WESSLFPALV QTNCYKYLMF FACTILVPKC DVNTGQSIPP CRALCEHSKE
     RCESVLGIVG LQWPEHTDCS QFPEENSDNQ TCLMPDEYVE ECSPSHFKCR SGRCVLASRR
     CDGQADCDDD SDEENCGCKE RDLWECPSNK QCLKHTVICD GFPDCPDYMD EKNCSFCQDD
     ELECANHACV SRNLWCDGEA DCSDSSDEWD CVTLSINVNS SSFLMVHRAA TEHHVCADGW
     REMFSQLACK QMGLGEPSVT KLIQEQEKEL RWLTLHSNWE SLNGTTLHEL LVNGQSCQSR
     SKISLLCTKQ DCGRRPAARM NKRILGGRTS RPGRWPWQCS LQSEPSGHIC GCVLIAKKWV
     LTVAHCFEGR ENAAVWKVVL GINNLDHPSV FMQTRFVKTI ILHPRYSRAV VDYDISIIEL
     NEDISETGYV RPVCLPSPEQ WLEPDTYCYI TGWGHMGNKM PFKLQEGEVR IIPLEQCQSY
     FDMKTITTRM ICAGYESGTV DSCMGDSGGP LVCEKPGGQW TLFGLTSWGS VCFSKVLGPG
     VYSNVSYFVE WIKRQIYIQT FLLN
//
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