SCRN1_HUMAN
ID SCRN1_HUMAN Reviewed; 414 AA.
AC Q12765; A8K0E9; B4DHM0; B4DIP5; C9JPG0; Q25QX7; Q8IWD1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-MAY-2003, sequence version 2.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Secernin-1;
GN Name=SCRN1; Synonyms=KIAA0193;
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).
RC TISSUE=Brain;
RX PubMed=16630140; DOI=10.1111/j.1349-7006.2006.00194.x;
RA Suda T., Tsunoda T., Uchida N., Watanabe T., Hasegawa S., Satoh S.,
RA Ohgi S., Furukawa Y., Nakamura Y., Tahara H.;
RT "Identification of secernin 1 as a novel immunotherapy target for gastric
RT cancer using the expression profiles of cDNA microarray.";
RL Cancer Sci. 97:411-419(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [3]
RP SEQUENCE REVISION TO N-TERMINUS.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 3).
RC TISSUE=Brain, Cerebellum, and Hippocampus;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Hypothalamus;
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 [8]
RP PROTEIN SEQUENCE OF 52-64; 99-114; 163-173 AND 186-196, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Platelet;
RX PubMed=11921445;
RX DOI=10.1002/1615-9861(200203)2:3<288::aid-prot288>3.0.co;2-0;
RA O'Neill E.E., Brock C.J., von Kriegsheim A.F., Pearce A.C., Dwek R.A.,
RA Watson S.P., Hebestreit H.F.;
RT "Towards complete analysis of the platelet proteome.";
RL Proteomics 2:288-305(2002).
RN [10]
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 [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
CC -!- FUNCTION: Regulates exocytosis in mast cells. Increases both the extent
CC of secretion and the sensitivity of mast cells to stimulation with
CC calcium (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q12765; Q9BQQ3: GORASP1; NbExp=3; IntAct=EBI-2690712, EBI-2561458;
CC Q12765-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-12027936, EBI-742054;
CC Q12765-2; Q9BQQ3: GORASP1; NbExp=3; IntAct=EBI-12027936, EBI-2561458;
CC Q12765-2; P42858: HTT; NbExp=3; IntAct=EBI-12027936, EBI-466029;
CC Q12765-2; P17030: ZNF25; NbExp=3; IntAct=EBI-12027936, EBI-7934204;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q12765-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12765-2; Sequence=VSP_044454;
CC Name=3;
CC IsoId=Q12765-3; Sequence=VSP_044453;
CC -!- MISCELLANEOUS: 'Secern' is an archaic English term meaning 'secrete'.
CC -!- SIMILARITY: Belongs to the peptidase C69 family. Secernin subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA12106.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB071705; BAE91926.1; -; mRNA.
DR EMBL; D83777; BAA12106.2; ALT_INIT; mRNA.
DR EMBL; AK289514; BAF82203.1; -; mRNA.
DR EMBL; AK295172; BAG58182.1; -; mRNA.
DR EMBL; AK295713; BAG58557.1; -; mRNA.
DR EMBL; AC004912; AAQ96874.1; -; Genomic_DNA.
DR EMBL; AC007285; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471073; EAW93926.1; -; Genomic_DNA.
DR EMBL; CH471073; EAW93928.1; -; Genomic_DNA.
DR EMBL; BC040492; AAH40492.1; -; mRNA.
DR CCDS; CCDS47567.1; -. [Q12765-2]
DR CCDS; CCDS47568.1; -. [Q12765-3]
DR CCDS; CCDS5422.1; -. [Q12765-1]
DR RefSeq; NP_001138985.1; NM_001145513.1. [Q12765-1]
DR RefSeq; NP_001138986.1; NM_001145514.1. [Q12765-2]
DR RefSeq; NP_001138987.1; NM_001145515.1. [Q12765-3]
DR RefSeq; NP_055581.3; NM_014766.4. [Q12765-1]
DR AlphaFoldDB; Q12765; -.
DR SMR; Q12765; -.
DR BioGRID; 115145; 40.
DR IntAct; Q12765; 16.
DR STRING; 9606.ENSP00000388942; -.
DR MEROPS; C69.003; -.
DR GlyGen; Q12765; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q12765; -.
DR MetOSite; Q12765; -.
DR PhosphoSitePlus; Q12765; -.
DR SwissPalm; Q12765; -.
DR BioMuta; SCRN1; -.
DR DMDM; 30923294; -.
DR OGP; Q12765; -.
DR EPD; Q12765; -.
DR jPOST; Q12765; -.
DR MassIVE; Q12765; -.
DR MaxQB; Q12765; -.
DR PaxDb; Q12765; -.
DR PeptideAtlas; Q12765; -.
DR PRIDE; Q12765; -.
DR ProteomicsDB; 11103; -.
DR ProteomicsDB; 4315; -.
DR ProteomicsDB; 58907; -. [Q12765-1]
DR Antibodypedia; 12563; 189 antibodies from 28 providers.
DR DNASU; 9805; -.
DR Ensembl; ENST00000242059.10; ENSP00000242059.5; ENSG00000136193.17. [Q12765-1]
DR Ensembl; ENST00000409497.5; ENSP00000386872.1; ENSG00000136193.17. [Q12765-1]
DR Ensembl; ENST00000425819.6; ENSP00000414245.2; ENSG00000136193.17. [Q12765-3]
DR Ensembl; ENST00000426154.5; ENSP00000409068.1; ENSG00000136193.17. [Q12765-1]
DR Ensembl; ENST00000434476.6; ENSP00000388942.1; ENSG00000136193.17. [Q12765-2]
DR GeneID; 9805; -.
DR KEGG; hsa:9805; -.
DR MANE-Select; ENST00000242059.10; ENSP00000242059.5; NM_014766.5; NP_055581.3.
DR UCSC; uc003tak.4; human. [Q12765-1]
DR CTD; 9805; -.
DR DisGeNET; 9805; -.
DR GeneCards; SCRN1; -.
DR HGNC; HGNC:22192; SCRN1.
DR HPA; ENSG00000136193; Tissue enhanced (brain).
DR MIM; 614965; gene.
DR neXtProt; NX_Q12765; -.
DR OpenTargets; ENSG00000136193; -.
DR PharmGKB; PA134874373; -.
DR VEuPathDB; HostDB:ENSG00000136193; -.
DR eggNOG; ENOG502QTSN; Eukaryota.
DR GeneTree; ENSGT00390000013474; -.
DR HOGENOM; CLU_046840_0_0_1; -.
DR InParanoid; Q12765; -.
DR OrthoDB; 322959at2759; -.
DR PhylomeDB; Q12765; -.
DR TreeFam; TF323890; -.
DR PathwayCommons; Q12765; -.
DR SignaLink; Q12765; -.
DR BioGRID-ORCS; 9805; 11 hits in 1076 CRISPR screens.
DR ChiTaRS; SCRN1; human.
DR GeneWiki; SCRN1; -.
DR GenomeRNAi; 9805; -.
DR Pharos; Q12765; Tbio.
DR PRO; PR:Q12765; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; Q12765; protein.
DR Bgee; ENSG00000136193; Expressed in trigeminal ganglion and 199 other tissues.
DR ExpressionAtlas; Q12765; baseline and differential.
DR Genevisible; Q12765; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070004; F:cysteine-type exopeptidase activity; IEA:InterPro.
DR GO; GO:0016805; F:dipeptidase activity; IEA:InterPro.
DR GO; GO:0006887; P:exocytosis; ISS:UniProtKB.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR InterPro; IPR005322; Peptidase_C69.
DR PANTHER; PTHR12994; PTHR12994; 1.
DR Pfam; PF03577; Peptidase_C69; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Direct protein sequencing;
KW Exocytosis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..414
FT /note="Secernin-1"
FT /id="PRO_0000221436"
FT ACT_SITE 9
FT /evidence="ECO:0000255"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT VAR_SEQ 1..68
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044453"
FT VAR_SEQ 1
FT /note="M -> MVQDGTFKTRDSTWTCESTRM (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044454"
FT VARIANT 189
FT /note="S -> N (in dbSNP:rs35960711)"
FT /id="VAR_057709"
FT VARIANT 338
FT /note="Q -> R (in dbSNP:rs17324153)"
FT /id="VAR_029512"
FT CONFLICT 120
FT /note="G -> W (in Ref. 4; BAG58182)"
FT /evidence="ECO:0000305"
FT CONFLICT 298
FT /note="P -> H (in Ref. 7; AAH40492)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 414 AA; 46382 MW; 1B14D1007AE6BEBE CRC64;
MAAAPPSYCF VAFPPRAKDG LVVFGKNSAR PRDEVQEVVY FSAADHEPES KVECTYISID
QVPRTYAIMI SRPAWLWGAE MGANEHGVCI ANEAINTREP AAEIEALLGM DLVRLGLERG
ETAKEALDVI VSLLEEHGQG GNYFEDANSC HSFQSAYLIV DRDEAWVLET IGKYWAAEKV
TEGVRCICSQ LSLTTKMDAE HPELRSYAQS QGWWTGEGEF NFSEVFSPVE DHLDCGAGKD
SLEKQEESIT VQTMMNTLRD KASGVCIDSE FFLTTASGVS VLPQNRSSPC IHYFTGTPDP
SRSIFKPFIF VDDVKLVPKT QSPCFGDDDP AKKEPRFQEK PDRRHELYKA HEWARAIIES
DQEQGRKLRS TMLELEKQGL EAMEEILTSS EPLDPAEVGD LFYDCVDTEI KFFK
