ID Q86T07_HUMAN Unreviewed; 367 AA. AC Q86T07; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 98. DE RecName: Full=Chromogranin-A {ECO:0000256|ARBA:ARBA00040787}; DE Flags: Fragment; 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 {ECO:0000313|EMBL:CAD62591.1}; RN [1] {ECO:0000313|EMBL:CAD62591.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Adult brain {ECO:0000313|EMBL:CAD62591.1}; RA Li W.B., Gruber C., Jessee J., Polayes D.; RT "Full-length cDNA libraries and normalization."; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAD62591.1} RP NUCLEOTIDE SEQUENCE. RC TISSUE=Adult brain {ECO:0000313|EMBL:CAD62591.1}; RA Genoscope; RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Strongly inhibits glucose induced insulin release from the CC pancreas. {ECO:0000256|ARBA:ARBA00037544}. CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle CC {ECO:0000256|ARBA:ARBA00004398}. Secreted CC {ECO:0000256|ARBA:ARBA00004613}. Vesicle CC {ECO:0000256|ARBA:ARBA00004373}. CC -!- SIMILARITY: Belongs to the chromogranin/secretogranin protein family. CC {ECO:0000256|ARBA:ARBA00005723}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX248263; CAD62591.1; -; mRNA. DR RefSeq; NP_001266.1; NM_001275.3. DR RefSeq; NP_001288619.1; NM_001301690.1. DR AlphaFoldDB; Q86T07; -. DR DNASU; 1113; -. DR GeneID; 1113; -. DR KEGG; hsa:1113; -. DR CTD; 1113; -. DR PharmGKB; PA26461; -. DR OrthoDB; 4262934at2759; -. DR BioGRID-ORCS; 1113; 178 hits in 1147 CRISPR screens. DR GenomeRNAi; 1113; -. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0030141; C:secretory granule; IEA:InterPro. DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell. DR InterPro; IPR001819; Chromogranin_AB. DR InterPro; IPR018054; Chromogranin_CS. DR InterPro; IPR001990; Granin. DR PANTHER; PTHR10583; CHROMOGRANIN; 1. DR PANTHER; PTHR10583:SF1; CHROMOGRANIN-A; 1. DR Pfam; PF01271; Granin; 2. DR PRINTS; PR00659; CHROMOGRANIN. DR PROSITE; PS00422; GRANINS_1; 1. DR PROSITE; PS00423; GRANINS_2; 1. DR Genevisible; Q86T07; HS. PE 2: Evidence at transcript level; KW Cytoplasmic vesicle {ECO:0000256|ARBA:ARBA00023329}; KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}; KW Sulfation {ECO:0000256|ARBA:ARBA00022641}. FT REGION 1..42 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 149..349 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 149..165 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 195..221 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 232..283 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 323..349 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT NON_TER 1 FT /evidence="ECO:0000313|EMBL:CAD62591.1" SQ SEQUENCE 367 AA; 40456 MW; 86024ED83D2EF724 CRC64; EPRAGELAGG STDRRTHAEA LRPQPRAGAT AARPRPPVQP PLARCLGARP HTASCSAPGS AMRSAAVLAL LLCAGQVTAL PVNSPMNKGD TEVMKCIVEV ISDTLSKPSP MPVSQECFET LRGDERILSI LRHQNLLKEL QDLALQGAKE RAHQQKKHSG FEDELSEVLE NQSSQAELKG RSEALAVDGA GKPGAEEAQD PEGKGEQEHS QQKEEEEEMA VVPQGLFRGG KSGELEQEEE RLSKEWEDSK RWSKMDQLAK ELTAEKRLEG QEEEEDNRDS SMKLSFRARA YGFRGPGPQL RRGWRPSSRE DSLEAGLPLQ VRGYPEEKKE EEGSANRRPE DQELESLSAI EAELEKVAHQ LQALRRG //