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   24-JAN-2024, entry version 189.
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; 14.
DR   CORUM; P13521; -.
DR   IntAct; P13521; 10.
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; 9606-ENSP00000304133; -.
DR   PeptideAtlas; P13521; -.
DR   ProteomicsDB; 52923; -.
DR   Antibodypedia; 2205; 377 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   AGR; HGNC:10575; -.
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; CVDAASF; -.
DR   OrthoDB; 5351720at2759; -.
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; 13 hits in 1146 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 146 other cell types or tissues.
DR   ExpressionAtlas; P13521; baseline and differential.
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; SECRETOGRANIN II; 1.
DR   PANTHER; PTHR15119:SF0; SECRETOGRANIN-2; 1.
DR   Pfam; PF01271; Granin; 1.
DR   PROSITE; PS00422; GRANINS_1; 1.
DR   Genevisible; P13521; HS.
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                   /evidence="ECO:0000250|UniProtKB:P30945"
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
//