ID   CCL2_PONAB              Reviewed;          99 AA.
AC   Q5RA36;
DT   16-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-DEC-2004, sequence version 1.
DT   25-MAY-2022, entry version 67.
DE   RecName: Full=C-C motif chemokine 2;
DE   AltName: Full=Small-inducible cytokine A2;
DE   Flags: Precursor;
GN   Name=CCL2;
OS   Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Pongo.
OX   NCBI_TaxID=9601;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Kidney;
RG   The German cDNA consortium;
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Acts as a ligand for C-C chemokine receptor CCR2 (By
CC       similarity). Signals through binding and activation of CCR2 and induces
CC       a strong chemotactic response and mobilization of intracellular calcium
CC       ions (By similarity). Exhibits a chemotactic activity for monocytes and
CC       basophils but not neutrophils or eosinophils (By similarity). Plays an
CC       important role in mediating peripheral nerve injury-induced neuropathic
CC       pain (By similarity). Increases NMDA-mediated synaptic transmission in
CC       both dopamine D1 and D2 receptor-containing neurons, which may be
CC       caused by MAPK/ERK-dependent phosphorylation of GRIN2B/NMDAR2B (By
CC       similarity). {ECO:0000250|UniProtKB:P10148,
CC       ECO:0000250|UniProtKB:P13500}.
CC   -!- SUBUNIT: Monomer or homodimer; in equilibrium. Is tethered on
CC       endothelial cells by glycosaminoglycan (GAG) side chains of
CC       proteoglycans. Interacts with TNFAIP6 (via Link domain).
CC       {ECO:0000250|UniProtKB:P13500}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:P13500}.
CC   -!- PTM: Processing at the N-terminus can regulate receptor and target cell
CC       selectivity (By similarity). Deletion of the N-terminal residue
CC       converts it from an activator of basophil to an eosinophil
CC       chemoattractant (By similarity). {ECO:0000250|UniProtKB:P13500}.
CC   -!- PTM: N-Glycosylated. {ECO:0000250|UniProtKB:P13500}.
CC   -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC       {ECO:0000305}.
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DR   EMBL; CR859186; CAH91374.1; -; mRNA.
DR   RefSeq; NP_001125812.1; NM_001132340.2.
DR   AlphaFoldDB; Q5RA36; -.
DR   SMR; Q5RA36; -.
DR   STRING; 9601.ENSPPYP00000009183; -.
DR   GeneID; 100172740; -.
DR   KEGG; pon:100172740; -.
DR   CTD; 6347; -.
DR   eggNOG; ENOG502S6ZP; Eukaryota.
DR   InParanoid; Q5RA36; -.
DR   OrthoDB; 1575018at2759; -.
DR   Proteomes; UP000001595; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0008009; F:chemokine activity; IEA:InterPro.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR   GO; GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:UniProtKB.
DR   GO; GO:0019233; P:sensory perception of pain; ISS:UniProtKB.
DR   InterPro; IPR039809; Chemokine_b/g/d.
DR   InterPro; IPR000827; Chemokine_CC_CS.
DR   InterPro; IPR001811; Chemokine_IL8-like_dom.
DR   InterPro; IPR036048; Interleukin_8-like_sf.
DR   PANTHER; PTHR12015; PTHR12015; 1.
DR   Pfam; PF00048; IL8; 1.
DR   SMART; SM00199; SCY; 1.
DR   SUPFAM; SSF54117; SSF54117; 1.
DR   PROSITE; PS00472; SMALL_CYTOKINES_CC; 1.
PE   3: Inferred from homology;
KW   Chemotaxis; Cytokine; Disulfide bond; Glycoprotein; Inflammatory response;
KW   Pyrrolidone carboxylic acid; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000250"
FT   CHAIN           24..99
FT                   /note="C-C motif chemokine 2"
FT                   /id="PRO_0000005150"
FT   MOD_RES         24
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P13500"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        34..59
FT                   /evidence="ECO:0000250"
FT   DISULFID        35..75
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   99 AA;  11015 MW;  45FCA8CC64FF8A4F CRC64;
     MKVSAALLCL LLIAATFSPQ GLAQPDAINA PVTCCYNFTN RKISVQRLAS YRRITSSKCP
     KEAVIFKTIV AKEICADPKQ KWVQDSMDHL DKQTQTLKT