RISC_HUMAN
ID RISC_HUMAN Reviewed; 452 AA.
AC Q9HB40; Q96A94; Q9H3F0;
DT 28-FEB-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 175.
DE RecName: Full=Retinoid-inducible serine carboxypeptidase;
DE EC=3.4.16.-;
DE AltName: Full=Serine carboxypeptidase 1;
DE Flags: Precursor;
GN Name=SCPEP1; Synonyms=RISC, SCP1; ORFNames=MSTP034, UNQ265/PRO302;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Cho J.-J., Baik H.-H.;
RT "Cloning of novel serine carboxypeptidase precursor.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Mammary gland;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Eye, and Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 9-452 (ISOFORM 1).
RC TISSUE=Aorta;
RA Liu B., Liu Y.Q., Wang X.Y., Zhao B., Sheng H., Zhao X.W., Liu S., Xu Y.Y.,
RA Ye J., Song L., Gao Y., Zhang C.L., Zhang J., Wei Y.J., Cao H.Q., Zhao Y.,
RA Liu L.S., Ding J.F., Gao R.L., Wu Q.Y., Qiang B.Q., Yuan J.G., Liew C.C.,
RA Zhao M.S., Hui R.T.;
RL Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP PROTEIN SEQUENCE OF 27-41.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [7]
RP GLYCOSYLATION AT ASN-126.
RX PubMed=12754519; DOI=10.1038/nbt827;
RA Zhang H., Li X.-J., Martin D.B., Aebersold R.;
RT "Identification and quantification of N-linked glycoproteins using
RT hydrazide chemistry, stable isotope labeling and mass spectrometry.";
RL Nat. Biotechnol. 21:660-666(2003).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
CC -!- FUNCTION: May be involved in vascular wall and kidney homeostasis.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9HB40-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9HB40-2; Sequence=VSP_008555, VSP_008556;
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the peptidase S10 family. {ECO:0000305}.
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DR EMBL; AF282618; AAG16692.1; -; mRNA.
DR EMBL; AY358559; AAQ88923.1; -; mRNA.
DR EMBL; AK027373; BAB55069.1; -; mRNA.
DR EMBL; BC010078; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC072405; AAH72405.1; -; mRNA.
DR EMBL; AF113214; AAG39285.1; -; mRNA.
DR CCDS; CCDS11593.1; -. [Q9HB40-1]
DR RefSeq; NP_067639.1; NM_021626.2. [Q9HB40-1]
DR AlphaFoldDB; Q9HB40; -.
DR SMR; Q9HB40; -.
DR BioGRID; 121884; 83.
DR IntAct; Q9HB40; 4.
DR STRING; 9606.ENSP00000262288; -.
DR ChEMBL; CHEMBL2189131; -.
DR DrugBank; DB07506; L-BENZYLSUCCINIC ACID.
DR ESTHER; human-SCPEP1; Carboxypeptidase_S10.
DR MEROPS; S10.013; -.
DR GlyConnect; 1715; 2 N-Linked glycans (1 site).
DR GlyGen; Q9HB40; 5 sites, 2 N-linked glycans (1 site), 1 O-linked glycan (2 sites).
DR iPTMnet; Q9HB40; -.
DR PhosphoSitePlus; Q9HB40; -.
DR SwissPalm; Q9HB40; -.
DR BioMuta; SCPEP1; -.
DR DMDM; 41690765; -.
DR EPD; Q9HB40; -.
DR jPOST; Q9HB40; -.
DR MassIVE; Q9HB40; -.
DR MaxQB; Q9HB40; -.
DR PaxDb; Q9HB40; -.
DR PeptideAtlas; Q9HB40; -.
DR PRIDE; Q9HB40; -.
DR ProteomicsDB; 81478; -. [Q9HB40-1]
DR ProteomicsDB; 81479; -. [Q9HB40-2]
DR TopDownProteomics; Q9HB40-1; -. [Q9HB40-1]
DR Antibodypedia; 30882; 121 antibodies from 20 providers.
DR DNASU; 59342; -.
DR Ensembl; ENST00000262288.8; ENSP00000262288.3; ENSG00000121064.13. [Q9HB40-1]
DR Ensembl; ENST00000576154.5; ENSP00000458587.1; ENSG00000121064.13. [Q9HB40-2]
DR GeneID; 59342; -.
DR KEGG; hsa:59342; -.
DR MANE-Select; ENST00000262288.8; ENSP00000262288.3; NM_021626.3; NP_067639.1.
DR UCSC; uc002iuv.5; human. [Q9HB40-1]
DR CTD; 59342; -.
DR DisGeNET; 59342; -.
DR GeneCards; SCPEP1; -.
DR HGNC; HGNC:29507; SCPEP1.
DR HPA; ENSG00000121064; Tissue enhanced (parathyroid).
DR MIM; 619723; gene.
DR neXtProt; NX_Q9HB40; -.
DR OpenTargets; ENSG00000121064; -.
DR PharmGKB; PA134960711; -.
DR VEuPathDB; HostDB:ENSG00000121064; -.
DR eggNOG; KOG1283; Eukaryota.
DR GeneTree; ENSGT00940000156193; -.
DR HOGENOM; CLU_008523_1_0_1; -.
DR InParanoid; Q9HB40; -.
DR OMA; FMNMEGD; -.
DR PhylomeDB; Q9HB40; -.
DR TreeFam; TF313740; -.
DR PathwayCommons; Q9HB40; -.
DR SignaLink; Q9HB40; -.
DR BioGRID-ORCS; 59342; 16 hits in 1078 CRISPR screens.
DR ChiTaRS; SCPEP1; human.
DR GeneWiki; SCPEP1; -.
DR GenomeRNAi; 59342; -.
DR Pharos; Q9HB40; Tbio.
DR PRO; PR:Q9HB40; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q9HB40; protein.
DR Bgee; ENSG00000121064; Expressed in right adrenal gland cortex and 197 other tissues.
DR ExpressionAtlas; Q9HB40; baseline and differential.
DR Genevisible; Q9HB40; HS.
DR GO; GO:0005829; C:cytosol; ISS:UniProtKB.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0004185; F:serine-type carboxypeptidase activity; ISS:CAFA.
DR GO; GO:0097746; P:blood vessel diameter maintenance; ISS:CAFA.
DR GO; GO:0045776; P:negative regulation of blood pressure; ISS:CAFA.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR GO; GO:0042573; P:retinoic acid metabolic process; ISS:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001563; Peptidase_S10.
DR InterPro; IPR018202; Ser_caboxypep_ser_AS.
DR PANTHER; PTHR11802; PTHR11802; 1.
DR Pfam; PF00450; Peptidase_S10; 1.
DR PRINTS; PR00724; CRBOXYPTASEC.
DR SUPFAM; SSF53474; SSF53474; 1.
DR PROSITE; PS00131; CARBOXYPEPT_SER_SER; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Carboxypeptidase; Direct protein sequencing;
KW Glycoprotein; Hydrolase; Protease; Reference proteome; Secreted; Signal.
FT SIGNAL 1..26
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 27..452
FT /note="Retinoid-inducible serine carboxypeptidase"
FT /id="PRO_0000004284"
FT ACT_SITE 167
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 371
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT ACT_SITE 431
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10074"
FT CARBOHYD 64
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 126
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:12754519"
FT CARBOHYD 362
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 295..296
FT /note="CL -> WF (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008555"
FT VAR_SEQ 297..452
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_008556"
FT VARIANT 3
FT /note="L -> V (in dbSNP:rs34108204)"
FT /id="VAR_048684"
FT VARIANT 241
FT /note="V -> I (in dbSNP:rs16957938)"
FT /id="VAR_048685"
SQ SEQUENCE 452 AA; 50831 MW; 40D8FB3CBC09E3DE CRC64;
MELALRRSPV PRWLLLLPLL LGLNAGAVID WPTEEGKEVW DYVTVRKDAY MFWWLYYATN
SCKNFSELPL VMWLQGGPGG SSTGFGNFEE IGPLDSDLKP RKTTWLQAAS LLFVDNPVGT
GFSYVNGSGA YAKDLAMVAS DMMVLLKTFF SCHKEFQTVP FYIFSESYGG KMAAGIGLEL
YKAIQRGTIK CNFAGVALGD SWISPVDSVL SWGPYLYSMS LLEDKGLAEV SKVAEQVLNA
VNKGLYREAT ELWGKAEMII EQNTDGVNFY NILTKSTPTS TMESSLEFTQ SHLVCLCQRH
VRHLQRDALS QLMNGPIRKK LKIIPEDQSW GGQATNVFVN MEEDFMKPVI SIVDELLEAG
INVTVYNGQL DLIVDTMGQE AWVRKLKWPE LPKFSQLKWK ALYSDPKSLE TSAFVKSYKN
LAFYWILKAG HMVPSDQGDM ALKMMRLVTQ QE
