ID   CCL2_CAVPO              Reviewed;         120 AA.
AC   Q08782;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 120.
DE   RecName: Full=C-C motif chemokine 2;
DE   AltName: Full=Monocyte chemoattractant protein 1;
DE   AltName: Full=Monocyte chemotactic protein 1;
DE            Short=MCP-1;
DE   AltName: Full=Small-inducible cytokine A2;
DE   Flags: Precursor;
GN   Name=CCL2; Synonyms=MCP1, SCYA2;
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=Z; TISSUE=Spleen;
RX   PubMed=8496603;
RA   Yoshimura T.;
RT   "cDNA cloning of guinea pig monocyte chemoattractant protein-1 and
RT   expression of the recombinant protein.";
RL   J. Immunol. 150:5025-5032(1993).
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}.
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; L04985; AAA37047.1; -; mRNA.
DR   PIR; I48147; I48147.
DR   RefSeq; NP_001166397.1; NM_001172926.1.
DR   AlphaFoldDB; Q08782; -.
DR   SMR; Q08782; -.
DR   STRING; 10141.ENSCPOP00000012126; -.
DR   Ensembl; ENSCPOT00000013601; ENSCPOP00000012126; ENSCPOG00000013468.
DR   GeneID; 100135494; -.
DR   KEGG; cpoc:100135494; -.
DR   CTD; 6347; -.
DR   eggNOG; ENOG502S6ZP; Eukaryota.
DR   GeneTree; ENSGT01050000244851; -.
DR   HOGENOM; CLU_141716_1_0_1; -.
DR   InParanoid; Q08782; -.
DR   OMA; PITCCYT; -.
DR   OrthoDB; 1575018at2759; -.
DR   TreeFam; TF334888; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000013468; Expressed in zone of skin and 12 other tissues.
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   2: Evidence at transcript level;
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..120
FT                   /note="C-C motif chemokine 2"
FT                   /id="PRO_0000005144"
FT   REGION          91..120
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         24
FT                   /note="Pyrrolidone carboxylic acid"
FT                   /evidence="ECO:0000250|UniProtKB:P13500"
FT   CARBOHYD        97
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        34..73
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   120 AA;  13741 MW;  5905596851CF1C54 CRC64;
     MQRSSVLLCL LVIEATFCSL LMAQPDGVNT PTCCYTFNKQ IPLKRVKGYE RITSSRCPQE
     AVIFRTLKNK EVCADPTQKW VQDYIAKLDQ RTQQKQNSTA PQTSKPLNIR FTTQDPKNRS