Full text data of SCRN1
SCRN1
(KIAA0193)
[Confidence: low (only semi-automatic identification from reviews)]
Secernin-1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Secernin-1
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q12765
ID SCRN1_HUMAN Reviewed; 414 AA.
AC Q12765; A8K0E9; B4DHM0; B4DIP5; C9JPG0; Q25QX7; Q8IWD1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-MAY-2003, sequence version 2.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Secernin-1;
GN Name=SCRN1; Synonyms=KIAA0193;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT gastric 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.
RT The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS
RP 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Regulates exocytosis in mast cells. Increases both the
CC extent of secretion and the sensitivity of mast cells to
CC stimulation with calcium (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q12765-3; Sequence=VSP_044453;
CC Note=No experimental confirmation available;
CC -!- MISCELLANEOUS: 'Secern' is an archaic English term meaning
CC 'secrete'.
CC -!- SIMILARITY: Belongs to the peptidase C69 family. Secernin
CC subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA12106.2; Type=Erroneous initiation;
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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 RefSeq; NP_001138985.1; NM_001145513.1.
DR RefSeq; NP_001138986.1; NM_001145514.1.
DR RefSeq; NP_001138987.1; NM_001145515.1.
DR RefSeq; NP_055581.3; NM_014766.4.
DR RefSeq; XP_005249975.1; XM_005249918.1.
DR UniGene; Hs.520740; -.
DR ProteinModelPortal; Q12765; -.
DR IntAct; Q12765; 1.
DR MEROPS; C69.003; -.
DR PhosphoSite; Q12765; -.
DR DMDM; 30923294; -.
DR OGP; Q12765; -.
DR PaxDb; Q12765; -.
DR PeptideAtlas; Q12765; -.
DR PRIDE; Q12765; -.
DR DNASU; 9805; -.
DR Ensembl; ENST00000242059; ENSP00000242059; ENSG00000136193.
DR Ensembl; ENST00000409497; ENSP00000386872; ENSG00000136193.
DR Ensembl; ENST00000425819; ENSP00000414245; ENSG00000136193.
DR Ensembl; ENST00000426154; ENSP00000409068; ENSG00000136193.
DR Ensembl; ENST00000434476; ENSP00000388942; ENSG00000136193.
DR GeneID; 9805; -.
DR KEGG; hsa:9805; -.
DR UCSC; uc003tak.3; human.
DR CTD; 9805; -.
DR GeneCards; GC07M029926; -.
DR HGNC; HGNC:22192; SCRN1.
DR HPA; HPA024517; -.
DR MIM; 614965; gene.
DR neXtProt; NX_Q12765; -.
DR PharmGKB; PA134874373; -.
DR eggNOG; COG4690; -.
DR HOVERGEN; HBG056050; -.
DR InParanoid; Q12765; -.
DR KO; K14358; -.
DR OMA; AFPPRTK; -.
DR OrthoDB; EOG7W1545; -.
DR PhylomeDB; Q12765; -.
DR ChiTaRS; SCRN1; human.
DR GeneWiki; SCRN1; -.
DR GenomeRNAi; 9805; -.
DR NextBio; 36916; -.
DR PRO; PR:Q12765; -.
DR ArrayExpress; Q12765; -.
DR Bgee; Q12765; -.
DR CleanEx; HS_SCRN1; -.
DR Genevestigator; Q12765; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
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 Pfam; PF03577; Peptidase_C69; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Exocytosis; Polymorphism;
KW Reference proteome.
FT CHAIN 1 414 Secernin-1.
FT /FTId=PRO_0000221436.
FT ACT_SITE 9 9 Potential.
FT VAR_SEQ 1 68 Missing (in isoform 3).
FT /FTId=VSP_044453.
FT VAR_SEQ 1 1 M -> MVQDGTFKTRDSTWTCESTRM (in isoform
FT 2).
FT /FTId=VSP_044454.
FT VARIANT 189 189 S -> N (in dbSNP:rs35960711).
FT /FTId=VAR_057709.
FT VARIANT 338 338 Q -> R (in dbSNP:rs17324153).
FT /FTId=VAR_029512.
FT CONFLICT 120 120 G -> W (in Ref. 4; BAG58182).
FT CONFLICT 298 298 P -> H (in Ref. 7; AAH40492).
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
//
ID SCRN1_HUMAN Reviewed; 414 AA.
AC Q12765; A8K0E9; B4DHM0; B4DIP5; C9JPG0; Q25QX7; Q8IWD1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 16-MAY-2003, sequence version 2.
DT 22-JAN-2014, entry version 112.
DE RecName: Full=Secernin-1;
GN Name=SCRN1; Synonyms=KIAA0193;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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
RT gastric 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.
RT The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA 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
RT project: 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 MASS
RP 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Regulates exocytosis in mast cells. Increases both the
CC extent of secretion and the sensitivity of mast cells to
CC stimulation with calcium (By similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
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 Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q12765-3; Sequence=VSP_044453;
CC Note=No experimental confirmation available;
CC -!- MISCELLANEOUS: 'Secern' is an archaic English term meaning
CC 'secrete'.
CC -!- SIMILARITY: Belongs to the peptidase C69 family. Secernin
CC subfamily.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA12106.2; Type=Erroneous initiation;
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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 RefSeq; NP_001138985.1; NM_001145513.1.
DR RefSeq; NP_001138986.1; NM_001145514.1.
DR RefSeq; NP_001138987.1; NM_001145515.1.
DR RefSeq; NP_055581.3; NM_014766.4.
DR RefSeq; XP_005249975.1; XM_005249918.1.
DR UniGene; Hs.520740; -.
DR ProteinModelPortal; Q12765; -.
DR IntAct; Q12765; 1.
DR MEROPS; C69.003; -.
DR PhosphoSite; Q12765; -.
DR DMDM; 30923294; -.
DR OGP; Q12765; -.
DR PaxDb; Q12765; -.
DR PeptideAtlas; Q12765; -.
DR PRIDE; Q12765; -.
DR DNASU; 9805; -.
DR Ensembl; ENST00000242059; ENSP00000242059; ENSG00000136193.
DR Ensembl; ENST00000409497; ENSP00000386872; ENSG00000136193.
DR Ensembl; ENST00000425819; ENSP00000414245; ENSG00000136193.
DR Ensembl; ENST00000426154; ENSP00000409068; ENSG00000136193.
DR Ensembl; ENST00000434476; ENSP00000388942; ENSG00000136193.
DR GeneID; 9805; -.
DR KEGG; hsa:9805; -.
DR UCSC; uc003tak.3; human.
DR CTD; 9805; -.
DR GeneCards; GC07M029926; -.
DR HGNC; HGNC:22192; SCRN1.
DR HPA; HPA024517; -.
DR MIM; 614965; gene.
DR neXtProt; NX_Q12765; -.
DR PharmGKB; PA134874373; -.
DR eggNOG; COG4690; -.
DR HOVERGEN; HBG056050; -.
DR InParanoid; Q12765; -.
DR KO; K14358; -.
DR OMA; AFPPRTK; -.
DR OrthoDB; EOG7W1545; -.
DR PhylomeDB; Q12765; -.
DR ChiTaRS; SCRN1; human.
DR GeneWiki; SCRN1; -.
DR GenomeRNAi; 9805; -.
DR NextBio; 36916; -.
DR PRO; PR:Q12765; -.
DR ArrayExpress; Q12765; -.
DR Bgee; Q12765; -.
DR CleanEx; HS_SCRN1; -.
DR Genevestigator; Q12765; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0031965; C:nuclear membrane; IDA:UniProtKB.
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 Pfam; PF03577; Peptidase_C69; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Cytoplasm;
KW Direct protein sequencing; Exocytosis; Polymorphism;
KW Reference proteome.
FT CHAIN 1 414 Secernin-1.
FT /FTId=PRO_0000221436.
FT ACT_SITE 9 9 Potential.
FT VAR_SEQ 1 68 Missing (in isoform 3).
FT /FTId=VSP_044453.
FT VAR_SEQ 1 1 M -> MVQDGTFKTRDSTWTCESTRM (in isoform
FT 2).
FT /FTId=VSP_044454.
FT VARIANT 189 189 S -> N (in dbSNP:rs35960711).
FT /FTId=VAR_057709.
FT VARIANT 338 338 Q -> R (in dbSNP:rs17324153).
FT /FTId=VAR_029512.
FT CONFLICT 120 120 G -> W (in Ref. 4; BAG58182).
FT CONFLICT 298 298 P -> H (in Ref. 7; AAH40492).
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
//
MIM
614965
*RECORD*
*FIELD* NO
614965
*FIELD* TI
*614965 SECERNIN 1; SCRN1
;;SES1;;
KIAA0193
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated KG-1 myeloid cell
read moreline cDNA library, Nagase et al. (1996) obtained a partial SCRN1 clone,
which they designated KIAA0193. Northern blot analysis detected SCRN1
expression in all human tissues and cell lines examined, with highest
expression in brain.
By database analysis to identify orthologs of mouse secernin-1 (named
after secern, an archaic English term for secrete), Way et al. (2002)
identified human SCRN1, SCRN2 (614966), and SCRN3 (614967). The deduced
SCRN1 protein contains 346 amino acids and is N-terminally truncated
compared with mouse Scrn1.
GENE FUNCTION
Way et al. (2002) found that purified bovine brain secernin-1 stimulated
secretion of hexosaminidase from permeabilized rat mast cells.
MAPPING
By radiation hybrid analysis, Nagase et al. (1996) mapped the SCRN1 gene
to chromosome 7.
Way et al. (2002) mapped the SCRN1 gene to chromosome 7p14.3-p14.1 by
genomic sequence analysis.
*FIELD* RF
1. Nagase, T.; Seki, N.; Ishikawa, K.; Tanaka, A.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. V. The coding
sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 3: 17-24, 1996.
2. Way, G.; Morrice, N.; Smythe, C.; O'Sullivan, A. J.: Purification
and identification of secernin, a novel cytosolic protein that regulates
exocytosis in mast cells. Molec. Biol. Cell 13: 3344-3354, 2002.
*FIELD* CD
Patricia A. Hartz: 12/3/2012
*FIELD* ED
mgross: 12/03/2012
*RECORD*
*FIELD* NO
614965
*FIELD* TI
*614965 SECERNIN 1; SCRN1
;;SES1;;
KIAA0193
*FIELD* TX
CLONING
By sequencing clones obtained from a size-fractionated KG-1 myeloid cell
read moreline cDNA library, Nagase et al. (1996) obtained a partial SCRN1 clone,
which they designated KIAA0193. Northern blot analysis detected SCRN1
expression in all human tissues and cell lines examined, with highest
expression in brain.
By database analysis to identify orthologs of mouse secernin-1 (named
after secern, an archaic English term for secrete), Way et al. (2002)
identified human SCRN1, SCRN2 (614966), and SCRN3 (614967). The deduced
SCRN1 protein contains 346 amino acids and is N-terminally truncated
compared with mouse Scrn1.
GENE FUNCTION
Way et al. (2002) found that purified bovine brain secernin-1 stimulated
secretion of hexosaminidase from permeabilized rat mast cells.
MAPPING
By radiation hybrid analysis, Nagase et al. (1996) mapped the SCRN1 gene
to chromosome 7.
Way et al. (2002) mapped the SCRN1 gene to chromosome 7p14.3-p14.1 by
genomic sequence analysis.
*FIELD* RF
1. Nagase, T.; Seki, N.; Ishikawa, K.; Tanaka, A.; Nomura, N.: Prediction
of the coding sequences of unidentified human genes. V. The coding
sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis
of cDNA clones from human cell line KG-1. DNA Res. 3: 17-24, 1996.
2. Way, G.; Morrice, N.; Smythe, C.; O'Sullivan, A. J.: Purification
and identification of secernin, a novel cytosolic protein that regulates
exocytosis in mast cells. Molec. Biol. Cell 13: 3344-3354, 2002.
*FIELD* CD
Patricia A. Hartz: 12/3/2012
*FIELD* ED
mgross: 12/03/2012