General information | DisProt: | DP00124 | Name: | Secretogranin-1 | Synonym(s): | SCG1_BOVIN
Secretogranin I
SgI
Chromogranin-B
CgB
Secretogranin-1(476-566) [cleavage product 1]
Peptide BAM-1745 [cleavage product 2]
Secretolytin [cleavage product 3]
| First appeared in release: | Release 1.0 (08/01/2003) | UniProt: | P23389 | UniGene: | Bt.5448 | SwissProt: | SCG1_BOVIN | TrEMBL: | | NCBI (GI): | 12644006 | Source organism: | Bos taurus (Bovine) | Sequence length: | 646 | Percent disordered: | 100% | Homologues: | |
Native sequence |
10 20 30 40 50 60 | | | | | | MQPAALLGLL GATVVAAVSS MPVDIRNHNE EVVTHCIIEV LSNALLKSSA PPITPECRQV - 60 LKKNGKELKD EEKSENENTR FEVRLLRDPA DTSEAPGLSS REDSGEGDAQ VPTVADTESG - 120 GHSRERAGEP PGSQVAKEAK TRYSKSEGQN REEEMVKYQK RERGEVGSEE RLSEGPGKAQ - 180 MAFLNQRNQT PAKKEELVSR YDTQSARGLE KSHSRERSSQ ESGEETKSQE NWPQELQRHP - 240 EGQEAPGESE EDASPEVDKR RSRPRHHHGR SRPDRSSQEG NPPLEEESHV GTGNSDEEKA - 300 RHPAHFRALE EGAEYGEEVR RHSAAQAPGD LQGARFGGRG RGEHQALRRP SEESLEQENK - 360 RHGLSPDLNM AQGYSEESEE ERGPARGPSY RARGGEAAAY STLGQTDEKR FLGETHHRVQ - 420 ESQRDKARRR LPGELRNYLD YGEEKGEEAA RGKWQPQGDP RDADENREEA RLRGKQYAPH - 480 HITEKRLGEL LNPFYDPSQW KSSRFERKDP MDDSFLEGEE ENGLTLNEKN FFPEYNYDWW - 540 EKKPFEEDVN WGYEKRNPVP KLDLKRQYDR VAELDQLLHY RKKSAEFPDF YDSEEQVSPQ - 600 HTAENEEEKA GQGVLTEEEE KELENLAAMD LELQKIAEKF SGTRRG
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Functional narrative |
Secretogranin-1 is a neuroendocrine secretory granule protein, which may be the precursor for other biologically active peptides. The 16 pairs of basic AA distributed throughout its sequence may be used as proteolytic cleavage sites. Secretolytin has antibacterial activity.
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Map of ordered and disordered regions |
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
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Region 1 | Type: | Disordered | Name: | | Location: | 1 - 646 | Length: | 646 | Region sequence: |
MQPAALLGLLGATVVAAVSSMPVDIRNHNEEVVTHCIIEVLSNALLKSSAPPITPECRQV LKKNGKELKDEEKSENENTRFEVRLLRDPADTSEAPGLSSREDSGEGDAQVPTVADTESG GHSRERAGEPPGSQVAKEAKTRYSKSEGQNREEEMVKYQKRERGEVGSEERLSEGPGKAQ MAFLNQRNQTPAKKEELVSRYDTQSARGLEKSHSRERSSQESGEETKSQENWPQELQRHP EGQEAPGESEEDASPEVDKRRSRPRHHHGRSRPDRSSQEGNPPLEEESHVGTGNSDEEKA RHPAHFRALEEGAEYGEEVRRHSAAQAPGDLQGARFGGRGRGEHQALRRPSEESLEQENK RHGLSPDLNMAQGYSEESEEERGPARGPSYRARGGEAAAYSTLGQTDEKRFLGETHHRVQ ESQRDKARRRLPGELRNYLDYGEEKGEEAARGKWQPQGDPRDADENREEARLRGKQYAPH HITEKRLGELLNPFYDPSQWKSSRFERKDPMDDSFLEGEEENGLTLNEKNFFPEYNYDWW EKKPFEEDVNWGYEKRNPVPKLDLKRQYDRVAELDQLLHYRKKSAEFPDFYDSEEQVSPQ HTAENEEEKAGQGVLTEEEEKELENLAAMDLELQKIAEKFSGTRRG | Modification type: | | PDB: | | Structural/functional type: | | Functional classes: | | Functional subclasses: | | Detection methods: | References:
- Yoo SH, Kang YK. "Identification of the secretory vesicle membrane binding region of chromogranin B." FEBS Lett. 1997; 406(3): 259-62. PubMed: 9136897
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Comments |
There are a number sequence conflicts according to the UniProt entry. So the sequence associated with the disorder-related paper does not match the sequence provided by UniProt.
Disordered residues lie within the residues corresponding to each of the cleavage products, however, the cleavage products are not discussed in the given reference.
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