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CCL27_HUMAN
ID   CCL27_HUMAN             Reviewed;         112 AA.
AC   Q9Y4X3;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 166.
DE   RecName: Full=C-C motif chemokine 27;
DE   AltName: Full=CC chemokine ILC;
DE   AltName: Full=Cutaneous T-cell-attracting chemokine;
DE            Short=CTACK;
DE   AltName: Full=ESkine;
DE   AltName: Full=IL-11 R-alpha-locus chemokine;
DE   AltName: Full=Skinkine;
DE   AltName: Full=Small-inducible cytokine A27;
DE   Flags: Precursor;
GN   Name=CCL27; Synonyms=ILC, SCYA27;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 25-30.
RC   TISSUE=Thymus;
RX   PubMed=10556532; DOI=10.1016/s0014-5793(99)01406-4;
RA   Ishikawa-Mochizuki I., Kitaura M., Baba M., Nakayama T., Izawa D., Imai T.,
RA   Yamada H., Hieshima K., Suzuki R., Nomiyama H., Yoshie O.;
RT   "Molecular cloning of a novel CC chemokine, interleukin-11 receptor alpha-
RT   locus chemokine (ILC), which is located on chromosome 9p13 and a potential
RT   homologue of a CC chemokine encoded by molluscum contagiosum virus.";
RL   FEBS Lett. 460:544-548(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=10588729; DOI=10.1073/pnas.96.25.14470;
RA   Morales J., Homey B., Vicari A.P., Hudak S., Oldham E., Hedrick J.,
RA   Orozco R., Copeland N.G., Jenkins N.A., McEvoy L.M., Zlotnik A.;
RT   "CTACK, a skin-associated chemokine that preferentially attracts skin-
RT   homing memory T cells.";
RL   Proc. Natl. Acad. Sci. U.S.A. 96:14470-14475(1999).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Skin;
RA   Zaballos A., Gutierrez J., Marquez G., Hromas R.;
RT   "CCL27, the human homologue of murine ALP chemokine.";
RL   Submitted (JUL-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   RECEPTOR INTERACTION.
RX   PubMed=10725697; DOI=10.4049/jimmunol.164.7.3465;
RA   Homey B., Wang W., Soto H., Buchanan M.E., Wiesenborn A., Catron D.,
RA   Muller A., McClanahan T.K., Dieu-Nosjean M.C., Orozco R., Ruzicka T.,
RA   Lehmann P., Oldham E., Zlotnik A.;
RT   "The orphan chemokine receptor G protein-coupled receptor-2 (GPR-2, CCR10)
RT   binds the skin-associated chemokine CCL27 (CTACK/ALP/ILC).";
RL   J. Immunol. 164:3465-3470(2000).
RN   [5]
RP   INTERACTION WITH TNFAIP6, AND MUTAGENESIS OF LYS-49.
RX   PubMed=27044744; DOI=10.1074/jbc.m116.720953;
RA   Dyer D.P., Salanga C.L., Johns S.C., Valdambrini E., Fuster M.M.,
RA   Milner C.M., Day A.J., Handel T.M.;
RT   "The Anti-inflammatory Protein TSG-6 Regulates Chemokine Function by
RT   Inhibiting Chemokine/Glycosaminoglycan Interactions.";
RL   J. Biol. Chem. 291:12627-12640(2016).
RN   [6]
RP   STRUCTURE BY NMR OF 25-112, SUBUNIT, AND DISULFIDE BONDS.
RX   PubMed=20200157; DOI=10.1074/jbc.m109.091108;
RA   Jansma A.L., Kirkpatrick J.P., Hsu A.R., Handel T.M., Nietlispach D.;
RT   "NMR analysis of the structure, dynamics, and unique oligomerization
RT   properties of the chemokine CCL27.";
RL   J. Biol. Chem. 285:14424-14437(2010).
CC   -!- FUNCTION: Chemotactic factor that attracts skin-associated memory T-
CC       lymphocytes. May play a role in mediating homing of lymphocytes to
CC       cutaneous sites. Binds to CCR10.
CC   -!- SUBUNIT: Monomer, dimer, and tetramer. Heparin avidly promotes
CC       oligomerization. Interacts with TNFAIP6 (via Link domain).
CC       {ECO:0000269|PubMed:20200157, ECO:0000269|PubMed:27044744}.
CC   -!- INTERACTION:
CC       Q9Y4X3; P51671: CCL11; NbExp=2; IntAct=EBI-16744026, EBI-727357;
CC       Q9Y4X3; P13501: CCL5; NbExp=2; IntAct=EBI-16744026, EBI-2848366;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q9Z1X0}.
CC   -!- TISSUE SPECIFICITY: Testis, thymus, placenta, ovary and skin.
CC   -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC       {ECO:0000305}.
CC   -!- WEB RESOURCE: Name=Wikipedia; Note=CCL27 entry;
CC       URL="https://en.wikipedia.org/wiki/CCL27";
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DR   EMBL; AB010445; BAA87046.1; -; mRNA.
DR   EMBL; AF082393; AAD41238.1; -; mRNA.
DR   EMBL; AJ243542; CAB46983.1; -; mRNA.
DR   CCDS; CCDS6569.1; -.
DR   RefSeq; NP_006655.1; NM_006664.3.
DR   PDB; 2KUM; NMR; -; A=25-112.
DR   PDBsum; 2KUM; -.
DR   AlphaFoldDB; Q9Y4X3; -.
DR   BMRB; Q9Y4X3; -.
DR   SMR; Q9Y4X3; -.
DR   BioGRID; 116061; 5.
DR   DIP; DIP-5872N; -.
DR   IntAct; Q9Y4X3; 4.
DR   STRING; 9606.ENSP00000259631; -.
DR   iPTMnet; Q9Y4X3; -.
DR   PhosphoSitePlus; Q9Y4X3; -.
DR   BioMuta; CCL27; -.
DR   DMDM; 7674366; -.
DR   MassIVE; Q9Y4X3; -.
DR   PaxDb; Q9Y4X3; -.
DR   PeptideAtlas; Q9Y4X3; -.
DR   PRIDE; Q9Y4X3; -.
DR   ProteomicsDB; 86261; -.
DR   Antibodypedia; 25618; 326 antibodies from 29 providers.
DR   DNASU; 10850; -.
DR   Ensembl; ENST00000259631.5; ENSP00000259631.4; ENSG00000213927.4.
DR   GeneID; 10850; -.
DR   KEGG; hsa:10850; -.
DR   MANE-Select; ENST00000259631.5; ENSP00000259631.4; NM_006664.4; NP_006655.1.
DR   UCSC; uc003zvm.1; human.
DR   CTD; 10850; -.
DR   DisGeNET; 10850; -.
DR   GeneCards; CCL27; -.
DR   HGNC; HGNC:10626; CCL27.
DR   HPA; ENSG00000213927; Tissue enriched (skin).
DR   MIM; 604833; gene.
DR   neXtProt; NX_Q9Y4X3; -.
DR   OpenTargets; ENSG00000213927; -.
DR   PharmGKB; PA35558; -.
DR   VEuPathDB; HostDB:ENSG00000213927; -.
DR   eggNOG; ENOG502SZGD; Eukaryota.
DR   GeneTree; ENSGT00530000063923; -.
DR   HOGENOM; CLU_2339025_0_0_1; -.
DR   InParanoid; Q9Y4X3; -.
DR   OMA; ANGDCHL; -.
DR   OrthoDB; 1574270at2759; -.
DR   PhylomeDB; Q9Y4X3; -.
DR   TreeFam; TF337014; -.
DR   PathwayCommons; Q9Y4X3; -.
DR   Reactome; R-HSA-380108; Chemokine receptors bind chemokines.
DR   Reactome; R-HSA-418594; G alpha (i) signalling events.
DR   SignaLink; Q9Y4X3; -.
DR   BioGRID-ORCS; 10850; 18 hits in 1070 CRISPR screens.
DR   EvolutionaryTrace; Q9Y4X3; -.
DR   GenomeRNAi; 10850; -.
DR   Pharos; Q9Y4X3; Tbio.
DR   PRO; PR:Q9Y4X3; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q9Y4X3; protein.
DR   Bgee; ENSG00000213927; Expressed in skin of abdomen and 90 other tissues.
DR   ExpressionAtlas; Q9Y4X3; baseline and differential.
DR   Genevisible; Q9Y4X3; HS.
DR   GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0031728; F:CCR3 chemokine receptor binding; IPI:UniProtKB.
DR   GO; GO:0008009; F:chemokine activity; IBA:GO_Central.
DR   GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; IDA:UniProtKB.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0006935; P:chemotaxis; TAS:ProtInc.
DR   GO; GO:0006955; P:immune response; TAS:ProtInc.
DR   GO; GO:0031640; P:killing of cells of another organism; IDA:UniProtKB.
DR   GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IBA:GO_Central.
DR   GO; GO:0010820; P:positive regulation of T cell chemotaxis; IBA:GO_Central.
DR   InterPro; IPR001811; Chemokine_IL8-like_dom.
DR   InterPro; IPR036048; Interleukin_8-like_sf.
DR   Pfam; PF00048; IL8; 1.
DR   SUPFAM; SSF54117; SSF54117; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytokine; Direct protein sequencing; Disulfide bond;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:10556532"
FT   CHAIN           25..112
FT                   /note="C-C motif chemokine 27"
FT                   /id="PRO_0000005239"
FT   DISULFID        33..62
FT                   /evidence="ECO:0000269|PubMed:20200157"
FT   DISULFID        34..77
FT                   /evidence="ECO:0000269|PubMed:20200157"
FT   VARIANT         78
FT                   /note="I -> V (in dbSNP:rs11575594)"
FT                   /id="VAR_022103"
FT   VARIANT         96
FT                   /note="L -> F (in dbSNP:rs11575584)"
FT                   /id="VAR_022104"
FT   MUTAGEN         49
FT                   /note="K->A: 9-fold reduction in binding affinity for Link
FT                   domain of TNFAIP6."
FT                   /evidence="ECO:0000269|PubMed:27044744"
FT   HELIX           44..47
FT                   /evidence="ECO:0007829|PDB:2KUM"
FT   STRAND          52..56
FT                   /evidence="ECO:0007829|PDB:2KUM"
FT   TURN            58..61
FT                   /evidence="ECO:0007829|PDB:2KUM"
FT   STRAND          62..64
FT                   /evidence="ECO:0007829|PDB:2KUM"
FT   STRAND          66..71
FT                   /evidence="ECO:0007829|PDB:2KUM"
FT   STRAND          74..78
FT                   /evidence="ECO:0007829|PDB:2KUM"
FT   HELIX           83..94
FT                   /evidence="ECO:0007829|PDB:2KUM"
FT   HELIX           96..98
FT                   /evidence="ECO:0007829|PDB:2KUM"
FT   TURN            106..110
FT                   /evidence="ECO:0007829|PDB:2KUM"
SQ   SEQUENCE   112 AA;  12618 MW;  7B5940E147ABF820 CRC64;
     MKGPPTFCSL LLLSLLLSPD PTAAFLLPPS TACCTQLYRK PLSDKLLRKV IQVELQEADG
     DCHLQAFVLH LAQRSICIHP QNPSLSQWFE HQERKLHGTL PKLNFGMLRK MG
 
 
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