SCG2_HUMAN
ID SCG2_HUMAN Reviewed; 617 AA.
AC P13521; B2R662; Q53T11; Q8TBH3;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 2.
DT 03-AUG-2022, entry version 181.
DE RecName: Full=Secretogranin-2;
DE AltName: Full=Chromogranin-C;
DE AltName: Full=Secretogranin II;
DE Short=SgII;
DE Contains:
DE RecName: Full=Secretoneurin;
DE Short=SN;
DE Contains:
DE RecName: Full=Manserin;
DE Flags: Precursor;
GN Name=SCG2; Synonyms=CHGC;
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], AND SULFATION AT TYR-151.
RC TISSUE=Pituitary;
RX PubMed=2745426; DOI=10.1016/s0021-9258(18)80167-3;
RA Gerdes H.-H., Rosa P., Phillips E., Baeuerle P.A., Frank R., Argos P.,
RA Huttner W.B.;
RT "The primary structure of human secretogranin II, a widespread tyrosine-
RT sulfated secretory granule protein that exhibits low pH- and calcium-
RT induced aggregation.";
RL J. Biol. Chem. 264:12009-12015(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Caudate nucleus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS GLY-294; GLY-421 AND
RP GLY-535.
RC TISSUE=Brain;
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 [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 182-214.
RX PubMed=9654353; DOI=10.1016/s0304-3940(98)00345-0;
RA Leitner B., Schneitler C., Klocker H., Volknandt W., Zimmermann H.,
RA Winkler H., Fischer-Colbrie R.;
RT "Formation and sequence analysis of secretoneurin, a neuropeptide derived
RT from secretogranin II, in mammalian, bird, reptile, amphibian and fish
RT brains.";
RL Neurosci. Lett. 248:105-108(1998).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pituitary;
RX PubMed=16807684; DOI=10.1007/s11102-006-8916-x;
RA Beranova-Giorgianni S., Zhao Y., Desiderio D.M., Giorgianni F.;
RT "Phosphoproteomic analysis of the human pituitary.";
RL Pituitary 9:109-120(2006).
RN [8]
RP INTERACTION WITH SCG3, AND FUNCTION.
RX PubMed=19357184; DOI=10.1677/joe-08-0531;
RA Hotta K., Hosaka M., Tanabe A., Takeuchi T.;
RT "Secretogranin II binds to secretogranin III and forms secretory granules
RT with orexin, neuropeptide Y, and POMC.";
RL J. Endocrinol. 202:111-121(2009).
RN [9]
RP GLYCOSYLATION, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=23234360; DOI=10.1021/pr300963h;
RA Halim A., Ruetschi U., Larson G., Nilsson J.;
RT "LC-MS/MS characterization of O-glycosylation sites and glycan structures
RT of human cerebrospinal fluid glycoproteins.";
RL J. Proteome Res. 12:573-584(2013).
CC -!- FUNCTION: Neuroendocrine protein of the granin family that regulates
CC the biogenesis of secretory granules. {ECO:0000269|PubMed:19357184}.
CC -!- SUBUNIT: Interacts with Secretogranin III/SCG3.
CC {ECO:0000269|PubMed:19357184}.
CC -!- INTERACTION:
CC P13521; Q8WXE1: ATRIP; NbExp=3; IntAct=EBI-947132, EBI-747353;
CC P13521; Q9UMX0: UBQLN1; NbExp=4; IntAct=EBI-947132, EBI-741480;
CC -!- SUBCELLULAR LOCATION: Secreted. Note=Neuroendocrine and endocrine
CC secretory granules.
CC -!- PTM: O-glycosylated. {ECO:0000269|PubMed:23234360}.
CC -!- MISCELLANEOUS: Binds calcium with a low-affinity.
CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family.
CC {ECO:0000305}.
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DR EMBL; M25756; AAA36607.1; -; mRNA.
DR EMBL; AK312452; BAG35359.1; -; mRNA.
DR EMBL; AC012512; AAY24243.1; -; Genomic_DNA.
DR EMBL; CH471063; EAW70811.1; -; Genomic_DNA.
DR EMBL; BC022509; AAH22509.1; -; mRNA.
DR CCDS; CCDS2457.1; -.
DR PIR; A34174; A34174.
DR RefSeq; NP_003460.2; NM_003469.4.
DR AlphaFoldDB; P13521; -.
DR SMR; P13521; -.
DR BioGRID; 113611; 12.
DR CORUM; P13521; -.
DR IntAct; P13521; 9.
DR MINT; P13521; -.
DR STRING; 9606.ENSP00000304133; -.
DR iPTMnet; P13521; -.
DR PhosphoSitePlus; P13521; -.
DR BioMuta; SCG2; -.
DR DMDM; 143811457; -.
DR jPOST; P13521; -.
DR MassIVE; P13521; -.
DR MaxQB; P13521; -.
DR PaxDb; P13521; -.
DR PeptideAtlas; P13521; -.
DR PRIDE; P13521; -.
DR ProteomicsDB; 52923; -.
DR Antibodypedia; 2205; 338 antibodies from 34 providers.
DR DNASU; 7857; -.
DR Ensembl; ENST00000305409.3; ENSP00000304133.2; ENSG00000171951.5.
DR GeneID; 7857; -.
DR KEGG; hsa:7857; -.
DR MANE-Select; ENST00000305409.3; ENSP00000304133.2; NM_003469.5; NP_003460.2.
DR UCSC; uc002vnm.4; human.
DR CTD; 7857; -.
DR DisGeNET; 7857; -.
DR GeneCards; SCG2; -.
DR HGNC; HGNC:10575; SCG2.
DR HPA; ENSG00000171951; Group enriched (adrenal gland, brain, pituitary gland).
DR MIM; 118930; gene.
DR neXtProt; NX_P13521; -.
DR OpenTargets; ENSG00000171951; -.
DR PharmGKB; PA34987; -.
DR VEuPathDB; HostDB:ENSG00000171951; -.
DR eggNOG; ENOG502QV5W; Eukaryota.
DR GeneTree; ENSGT00390000010895; -.
DR HOGENOM; CLU_031294_0_0_1; -.
DR InParanoid; P13521; -.
DR OMA; KYPEIIN; -.
DR OrthoDB; 587478at2759; -.
DR PhylomeDB; P13521; -.
DR TreeFam; TF334018; -.
DR PathwayCommons; P13521; -.
DR Reactome; R-HSA-381426; Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs).
DR Reactome; R-HSA-8957275; Post-translational protein phosphorylation.
DR SignaLink; P13521; -.
DR BioGRID-ORCS; 7857; 11 hits in 1068 CRISPR screens.
DR ChiTaRS; SCG2; human.
DR GeneWiki; SCG2; -.
DR GenomeRNAi; 7857; -.
DR Pharos; P13521; Tbio.
DR PRO; PR:P13521; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P13521; protein.
DR Bgee; ENSG00000171951; Expressed in type B pancreatic cell and 145 other tissues.
DR ExpressionAtlas; P13521; baseline and differential.
DR Genevisible; P13521; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; IDA:HGNC-UCL.
DR GO; GO:0098992; C:neuronal dense core vesicle; IEA:Ensembl.
DR GO; GO:0030141; C:secretory granule; IBA:GO_Central.
DR GO; GO:0042056; F:chemoattractant activity; IDA:HGNC-UCL.
DR GO; GO:0005125; F:cytokine activity; IDA:HGNC-UCL.
DR GO; GO:0001525; P:angiogenesis; IDA:HGNC-UCL.
DR GO; GO:0043542; P:endothelial cell migration; TAS:HGNC-UCL.
DR GO; GO:0048245; P:eosinophil chemotaxis; IDA:HGNC-UCL.
DR GO; GO:0050930; P:induction of positive chemotaxis; IDA:HGNC-UCL.
DR GO; GO:0006954; P:inflammatory response; TAS:HGNC-UCL.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:HGNC-UCL.
DR GO; GO:0000165; P:MAPK cascade; IDA:HGNC-UCL.
DR GO; GO:2000352; P:negative regulation of endothelial cell apoptotic process; IDA:BHF-UCL.
DR GO; GO:0001937; P:negative regulation of endothelial cell proliferation; TAS:HGNC-UCL.
DR GO; GO:2001237; P:negative regulation of extrinsic apoptotic signaling pathway; IDA:BHF-UCL.
DR GO; GO:0050918; P:positive chemotaxis; IDA:BHF-UCL.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; IDA:HGNC-UCL.
DR GO; GO:0009306; P:protein secretion; TAS:ProtInc.
DR InterPro; IPR018054; Chromogranin_CS.
DR InterPro; IPR001990; Granin.
DR InterPro; IPR038858; ScgII.
DR PANTHER; PTHR15119; PTHR15119; 1.
DR Pfam; PF01271; Granin; 1.
DR PROSITE; PS00422; GRANINS_1; 1.
PE 1: Evidence at protein level;
KW Calcium; Cleavage on pair of basic residues; Glycoprotein; Phosphoprotein;
KW Reference proteome; Secreted; Signal; Sulfation.
FT SIGNAL 1..27
FT /evidence="ECO:0000255"
FT PROPEP 28..30
FT /evidence="ECO:0000255"
FT /id="PRO_0000005452"
FT CHAIN 31..617
FT /note="Secretogranin-2"
FT /id="PRO_0000005453"
FT PEPTIDE 182..214
FT /note="Secretoneurin"
FT /id="PRO_0000005454"
FT PEPTIDE 527..566
FT /note="Manserin"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT /id="PRO_0000432735"
FT REGION 120..143
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 182..200
FT /note="O-glycosylated at one site"
FT REGION 257..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 552..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 151
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000269|PubMed:2745426"
FT MOD_RES 174
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT MOD_RES 432
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P10362"
FT MOD_RES 532
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03517"
FT MOD_RES 555
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03517"
FT MOD_RES 556
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q03517"
FT VARIANT 61
FT /note="Y -> H (in dbSNP:rs16864976)"
FT /id="VAR_031555"
FT VARIANT 196
FT /note="A -> V (in dbSNP:rs1438157)"
FT /id="VAR_048755"
FT VARIANT 294
FT /note="D -> G (in dbSNP:rs17852053)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031556"
FT VARIANT 421
FT /note="R -> G (in dbSNP:rs17856669)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031557"
FT VARIANT 535
FT /note="D -> G (in dbSNP:rs17852054)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031558"
FT VARIANT 564
FT /note="P -> L (in dbSNP:rs36043001)"
FT /id="VAR_031559"
FT CONFLICT 273
FT /note="E -> G (in Ref. 1; AAA36607)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 617 AA; 70941 MW; A81C9C091DE9DF6B CRC64;
MAEAKTHWLG AALSLIPLIF LISGAEAASF QRNQLLQKEP DLRLENVQKF PSPEMIRALE
YIENLRQQAH KEESSPDYNP YQGVSVPLQQ KENGDESHLP ERDSLSEEDW MRIILEALRQ
AENEPQSAPK ENKPYALNSE KNFPMDMSDD YETQQWPERK LKHMQFPPMY EENSRDNPFK
RTNEIVEEQY TPQSLATLES VFQELGKLTG PNNQKRERMD EEQKLYTDDE DDIYKANNIA
YEDVVGGEDW NPVEEKIESQ TQEEVRDSKE NIEKNEQIND EMKRSGQLGI QEEDLRKESK
DQLSDDVSKV IAYLKRLVNA AGSGRLQNGQ NGERATRLFE KPLDSQSIYQ LIEISRNLQI
PPEDLIEMLK TGEKPNGSVE PERELDLPVD LDDISEADLD HPDLFQNRML SKSGYPKTPG
RAGTEALPDG LSVEDILNLL GMESAANQKT SYFPNPYNQE KVLPRLPYGA GRSRSNQLPK
AAWIPHVENR QMAYENLNDK DQELGEYLAR MLVKYPEIIN SNQVKRVPGQ GSSEDDLQEE
EQIEQAIKEH LNQGSSQETD KLAPVSKRFP VGPPKNDDTP NRQYWDEDLL MKVLEYLNQE
KAEKGREHIA KRAMENM
