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CCL25_CANLF
ID   CCL25_CANLF             Reviewed;         151 AA.
AC   Q68A93;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=C-C motif chemokine 25;
DE   AltName: Full=Small-inducible cytokine A25;
DE   Flags: Precursor;
GN   Name=CCL25;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Tsukui T., Sakaguchi M., Maeda S., Koyanagi M., Masuda K., Ohno K.,
RA   Tsujimoto H., Iwabuchi S.;
RT   "Expression analysis of gene in canine atopic dermatitis.";
RL   Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Potentially involved in T-cell development. Recombinant
CC       protein shows chemotactic activity on thymocytes, macrophages, THP-1
CC       cells, and dendritics cells but is inactive on peripheral blood
CC       lymphocytes and neutrophils. Binds to CCR9. Binds to atypical chemokine
CC       receptor ACKR4 and mediates the recruitment of beta-arrestin (ARRB1/2)
CC       to ACKR4 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC       {ECO:0000305}.
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DR   EMBL; AB164617; BAD42446.1; -; mRNA.
DR   RefSeq; NP_001005259.1; NM_001005259.1.
DR   RefSeq; XP_005632371.1; XM_005632314.2.
DR   RefSeq; XP_005632372.1; XM_005632315.2.
DR   RefSeq; XP_013977206.1; XM_014121731.1.
DR   AlphaFoldDB; Q68A93; -.
DR   SMR; Q68A93; -.
DR   STRING; 9612.ENSCAFP00000027121; -.
DR   PaxDb; Q68A93; -.
DR   Ensembl; ENSCAFT00030026204; ENSCAFP00030022881; ENSCAFG00030014118.
DR   Ensembl; ENSCAFT00040037911; ENSCAFP00040033045; ENSCAFG00040020493.
DR   GeneID; 448798; -.
DR   KEGG; cfa:448798; -.
DR   CTD; 6370; -.
DR   eggNOG; ENOG502S8D1; Eukaryota.
DR   HOGENOM; CLU_113773_0_0_1; -.
DR   InParanoid; Q68A93; -.
DR   OMA; WAPAVHA; -.
DR   OrthoDB; 1542802at2759; -.
DR   TreeFam; TF353160; -.
DR   Reactome; R-CFA-380108; Chemokine receptors bind chemokines.
DR   Reactome; R-CFA-418594; G alpha (i) signalling events.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0048020; F:CCR chemokine receptor binding; IBA:GO_Central.
DR   GO; GO:0008009; F:chemokine activity; IBA:GO_Central.
DR   GO; GO:0042379; F:chemokine receptor binding; ISS:UniProtKB.
DR   GO; GO:0071346; P:cellular response to interferon-gamma; IBA:GO_Central.
DR   GO; GO:0071347; P:cellular response to interleukin-1; IBA:GO_Central.
DR   GO; GO:0071356; P:cellular response to tumor necrosis factor; IBA:GO_Central.
DR   GO; GO:0070098; P:chemokine-mediated signaling pathway; IBA:GO_Central.
DR   GO; GO:0007186; P:G protein-coupled receptor signaling pathway; IBA:GO_Central.
DR   GO; GO:0006954; P:inflammatory response; IBA:GO_Central.
DR   GO; GO:0048247; P:lymphocyte chemotaxis; IBA:GO_Central.
DR   GO; GO:0002548; P:monocyte chemotaxis; IBA:GO_Central.
DR   GO; GO:0030593; P:neutrophil chemotaxis; IBA:GO_Central.
DR   GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IBA:GO_Central.
DR   GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GO_Central.
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; Inflammatory response;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000255"
FT   CHAIN           23..151
FT                   /note="C-C motif chemokine 25"
FT                   /id="PRO_0000005234"
FT   REGION          94..151
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        105..127
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        137..151
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   DISULFID        29..57
FT                   /evidence="ECO:0000250"
FT   DISULFID        30..73
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   151 AA;  17109 MW;  DC0CD4106B1F922B CRC64;
     MNLWLLVCLV ASLMGAWSTV HTQGVSEDCC LAYHHRARPR LLMRAQGYQR QEVSGSCNLP
     AVIFFFPKNK MLCVNPRVNW LPNVFKFLDN RNNTHSKQHL GSRRNLQDSH LGGQRSNTGM
     SRLAHSKSKS SRSTRSNKKK TSFLNMANPG P
 
 
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