ID   CRAS_ACHAC              Reviewed;         184 AA.
AC   W1I921; C0HJG1;
DT   09-JUL-2014, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 1.
DT   25-MAY-2022, entry version 16.
DE   RecName: Full=Cysteine-rich atrial secretory protein {ECO:0000303|PubMed:26444993};
DE   Flags: Precursor;
GN   Name=crasp {ECO:0000312|EMBL:CDL67813.1};
OS   Achatina achatina (Giant Ghana snail).
OC   Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Gastropoda;
OC   Heterobranchia; Euthyneura; Panpulmonata; Eupulmonata; Stylommatophora;
OC   Helicina; Achatinoidea; Achatinidae; Achatina.
OX   NCBI_TaxID=1442373 {ECO:0000303|PubMed:26444993};
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 27-46 AND 48-64,
RP   SUBCELLULAR LOCATION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE,
RP   GLYCOSYLATION AT ASN-74, DISULFIDE BONDS, AND MASS SPECTROMETRY.
RC   TISSUE=Heart atrium {ECO:0000303|PubMed:26444993};
RX   PubMed=26444993; DOI=10.1371/journal.pone.0138787;
RA   Shabelnikov S., Kiselev A.;
RT   "Cysteine-Rich Atrial Secretory Protein from the Snail Achatina achatina:
RT   Purification and Structural Characterization.";
RL   PLoS ONE 10:E0138787-E0138787(2015).
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:26444993}.
CC       Note=Stored in secretory granules of atrial granular cells and released
CC       into hemolymph after electrostimulation of the heart nerve.
CC       {ECO:0000269|PubMed:26444993}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in atrium. Moderately expressed in
CC       the pericardium, pulmonary vein, nephridium, arteria anterior,
CC       ovotestis and connective tissue. Low expression found in intestine,
CC       lung plexus, diaphragm, subesophageal ganglion, ventricle and digestive
CC       gland. Very low expression found in columellar retractor, pedal nerves
CC       and cerebral ganglion. Not expressed in hemocytes.
CC       {ECO:0000269|PubMed:26444993}.
CC   -!- DEVELOPMENTAL STAGE: Expressed in newborn snails as well as adults.
CC       {ECO:0000269|PubMed:26444993}.
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:26444993}.
CC   -!- MASS SPECTROMETRY: Mass=18110.8; Method=Electrospray; Note=Non-
CC       glycosylated.; Evidence={ECO:0000269|PubMed:26444993};
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DR   EMBL; HG798329; CDL67813.1; -; mRNA.
DR   AlphaFoldDB; W1I921; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Secreted; Signal.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000269|PubMed:26444993"
FT   CHAIN           27..184
FT                   /note="Cysteine-rich atrial secretory protein"
FT                   /evidence="ECO:0000269|PubMed:26444993"
FT                   /id="PRO_0000429763"
FT   CARBOHYD        74
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   DISULFID        29..34
FT                   /evidence="ECO:0000269|PubMed:26444993"
FT   DISULFID        65..111
FT                   /evidence="ECO:0000269|PubMed:26444993"
FT   DISULFID        75..82
FT                   /evidence="ECO:0000269|PubMed:26444993"
FT   DISULFID        123..155
FT                   /evidence="ECO:0000269|PubMed:26444993"
FT   DISULFID        135..144
FT                   /evidence="ECO:0000269|PubMed:26444993"
SQ   SEQUENCE   184 AA;  20776 MW;  4A29D46F2B8437D5 CRC64;
     MATFQAHFFA AVMCVGVLGL SKLCGADSCE YPDCVFTGLP RSSGVERYIL LLNIIEVPDD
     IQQQCDILIQ RAHNCTSQRT GCSRRVEESY DRRFYDGAYV MYLLDLGVYV CGHLSQLLDL
     KNCFTPKLQE SVQSCINAAY NIQCLLDQYD QKNNCPPNTD DYFHTLVNNW LANNPYLGTG
     ADRD