ID   GRN1_CYPCA              Reviewed;          57 AA.
AC   P81013;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=Granulin-1;
OS   Cyprinus carpio (Common carp).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC   Cyprinidae; Cyprininae; Cyprinus.
OX   NCBI_TaxID=7962;
RN   [1]
RP   PROTEIN SEQUENCE.
RC   TISSUE=Kidney, and Spleen;
RX   PubMed=8486624; DOI=10.1016/s0021-9258(18)98340-7;
RA   Belcourt D.R., Lazure C., Bennett H.P.;
RT   "Isolation and primary structure of the three major forms of granulin-like
RT   peptides from hematopoietic tissues of a teleost fish (Cyprinus carpio).";
RL   J. Biol. Chem. 268:9230-9237(1993).
RN   [2]
RP   STRUCTURE BY NMR OF 1-30.
RX   PubMed=10424355; DOI=10.1034/j.1399-3011.1999.00048.x;
RA   Vranken W.F., Chen Z.G., Xu P., James S., Bennett H.P., Ni F.;
RT   "A 30-residue fragment of the carp granulin-1 protein folds into a stack of
RT   two beta-hairpins similar to that found in the native protein.";
RL   J. Pept. Res. 53:590-597(1999).
RN   [3]
RP   STRUCTURE BY NMR OF 3-30.
RX   PubMed=11870861; DOI=10.1002/prot.10077.abs;
RA   Vranken W.F., James S., Bennett H.P., Ni F.;
RT   "Solution structures of a 30-residue amino-terminal domain of the carp
RT   granulin-1 protein and its amino-terminally truncated 3-30 subfragment:
RT   implications for the conformational stability of the stack of two beta-
RT   hairpins.";
RL   Proteins 47:14-24(2002).
CC   -!- FUNCTION: Granulins have possible cytokine-like activity. They may play
CC       a role in inflammation, wound repair, and tissue remodeling.
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- TISSUE SPECIFICITY: Ubiquitous.
CC   -!- PTM: Granulins are disulfide bridged.
CC   -!- SIMILARITY: Belongs to the granulin family. {ECO:0000305}.
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DR   PIR; A46654; A46654.
DR   PDB; 1I8X; NMR; -; A=1-30.
DR   PDB; 1I8Y; NMR; -; A=3-30.
DR   PDB; 1QGM; NMR; -; A=1-30.
DR   PDBsum; 1I8X; -.
DR   PDBsum; 1I8Y; -.
DR   PDBsum; 1QGM; -.
DR   AlphaFoldDB; P81013; -.
DR   SMR; P81013; -.
DR   EvolutionaryTrace; P81013; -.
DR   Proteomes; UP000694384; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   Gene3D; 2.10.25.160; -; 1.
DR   InterPro; IPR000118; Granulin.
DR   InterPro; IPR039036; Granulin_fam.
DR   InterPro; IPR037277; Granulin_sf.
DR   PANTHER; PTHR12274; PTHR12274; 1.
DR   Pfam; PF00396; Granulin; 1.
DR   SMART; SM00277; GRAN; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytokine; Direct protein sequencing; Disulfide bond;
KW   Reference proteome; Secreted.
FT   CHAIN           1..57
FT                   /note="Granulin-1"
FT                   /id="PRO_0000150130"
FT   DISULFID        4..16
FT   DISULFID        10..26
FT   TURN            4..7
FT                   /evidence="ECO:0007829|PDB:1I8X"
FT   STRAND          14..18
FT                   /evidence="ECO:0007829|PDB:1I8X"
FT   STRAND          24..28
FT                   /evidence="ECO:0007829|PDB:1I8X"
SQ   SEQUENCE   57 AA;  6289 MW;  E4A131B1288FE55A CRC64;
     VIHCDAATIC PDGTTCCLSP YGVWYCCPFS MGQCCRDGIH CCRHGYHCDS TSTHCLR