CCL27_MOUSE
ID CCL27_MOUSE Reviewed; 120 AA.
AC Q9Z1X0; Q3KNL1; Q9DAU6; Q9DAZ4;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 13-DEC-2002, sequence version 2.
DT 03-AUG-2022, entry version 169.
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 Short=ALP;
DE Short=mILC;
DE AltName: Full=Skinkine;
DE AltName: Full=Small-inducible cytokine A27;
DE Flags: Precursor;
GN Name=Ccl27; Synonyms=Ilc, Scya27;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=10329455; DOI=10.1006/bbrc.1999.0507;
RA Hromas R., Broxmeyer H.E., Kim C., Christopherson K. II, Hou Y.-H.;
RT "Isolation of ALP, a novel divergent murine CC chemokine with a unique
RT carboxy terminal extension.";
RL Biochem. Biophys. Res. Commun. 258:737-740(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Placenta;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Thymus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RC TISSUE=Placenta, and Testis;
RX PubMed=10559234; DOI=10.1074/jbc.274.47.33496;
RA Baird J.W., Nibbs R.J.B., Komai-Koma M., Connolly J.A., Ottersbach K.,
RA Clark-Lewis I., Liew F.Y., Graham G.J.;
RT "ESkine, a novel beta-chemokine, is differentially spliced to produce
RT secretable and nuclear targeted isoforms.";
RL J. Biol. Chem. 274:33496-33503(1999).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12133963; DOI=10.4049/jimmunol.169.3.1387;
RA Gortz A., Nibbs R.J.B., McLean P., Jarmin D., Lambie W., Baird J.W.,
RA Graham G.J.;
RT "The chemokine ESkine/CCL27 displays novel modes of intracrine and
RT paracrine function.";
RL J. Immunol. 169:1387-1394(2002).
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. May play a role in cell migration during
CC embryogenesis. Nuclear forms may facilitate cellular migration by
CC inducing cytoskeletal relaxation. Binds to CCR10.
CC -!- SUBUNIT: Monomer, dimer, and tetramer. Heparin avidly promotes
CC oligomerization. Interacts with TNFAIP6 (via Link domain).
CC {ECO:0000250|UniProtKB:Q9Y4X3}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Secreted
CC {ECO:0000269|PubMed:10559234}. Nucleus {ECO:0000269|PubMed:10559234}.
CC Note=May also be nuclear when following receptor (CCR10)-mediated
CC internalization. {ECO:0000269|PubMed:10559234}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Nucleus
CC {ECO:0000269|PubMed:10559234, ECO:0000269|PubMed:12133963}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Z1X0-1; Sequence=Displayed;
CC Name=2; Synonyms=PESKY;
CC IsoId=Q9Z1X0-2; Sequence=VSP_001065;
CC -!- TISSUE SPECIFICITY: Isoform 1 is predominantly expressed in placenta
CC and weakly in skin. Isoform 2 is predominantly expressed in testes and
CC brain, weakly in kidney and liver and even lower in heart and muscle.
CC Low expression of both isoforms in other tissues.
CC -!- DEVELOPMENTAL STAGE: Expressed during development.
CC -!- SIMILARITY: Belongs to the intercrine beta (chemokine CC) family.
CC {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-2 is the initiator.
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; AF099931; AAD04163.1; -; mRNA.
DR EMBL; AB013398; BAA88474.1; -; mRNA.
DR EMBL; AF082392; AAD41237.1; -; mRNA.
DR EMBL; AK005520; BAB24095.1; -; mRNA.
DR EMBL; AK005398; BAB24001.1; -; mRNA.
DR EMBL; BC028511; AAH28511.1; -; mRNA.
DR EMBL; BC107226; AAI07227.1; -; mRNA.
DR CCDS; CCDS18072.1; -. [Q9Z1X0-1]
DR RefSeq; NP_001157518.1; NM_001164046.1. [Q9Z1X0-1]
DR RefSeq; NP_001186888.1; NM_001199959.1. [Q9Z1X0-1]
DR RefSeq; NP_001186890.1; NM_001199961.1. [Q9Z1X0-2]
DR RefSeq; NP_001186891.1; NM_001199962.1. [Q9Z1X0-2]
DR RefSeq; NP_001186894.1; NM_001199965.1. [Q9Z1X0-1]
DR RefSeq; NP_001254631.1; NM_001267702.1. [Q9Z1X0-2]
DR RefSeq; NP_001254633.1; NM_001267704.1. [Q9Z1X0-1]
DR RefSeq; NP_035466.1; NM_011336.1.
DR AlphaFoldDB; Q9Z1X0; -.
DR SMR; Q9Z1X0; -.
DR DIP; DIP-5905N; -.
DR STRING; 10090.ENSMUSP00000095726; -.
DR PhosphoSitePlus; Q9Z1X0; -.
DR PaxDb; Q9Z1X0; -.
DR PRIDE; Q9Z1X0; -.
DR DNASU; 20301; -.
DR Ensembl; ENSMUST00000098122; ENSMUSP00000095726; ENSMUSG00000073877. [Q9Z1X0-1]
DR Ensembl; ENSMUST00000108018; ENSMUSP00000103653; ENSMUSG00000073877. [Q9Z1X0-2]
DR Ensembl; ENSMUST00000177785; ENSMUSP00000137284; ENSMUSG00000096826. [Q9Z1X0-1]
DR GeneID; 100039863; -.
DR GeneID; 100040048; -.
DR GeneID; 20301; -.
DR KEGG; mmu:100039863; -.
DR KEGG; mmu:100040048; -.
DR KEGG; mmu:20301; -.
DR UCSC; uc008sln.2; mouse. [Q9Z1X0-1]
DR UCSC; uc012dcl.1; mouse. [Q9Z1X0-2]
DR CTD; 100040048; -.
DR CTD; 20301; -.
DR MGI; MGI:1343459; Ccl27.
DR VEuPathDB; HostDB:ENSMUSG00000073877; -.
DR VEuPathDB; HostDB:ENSMUSG00000093828; -.
DR VEuPathDB; HostDB:ENSMUSG00000095247; -.
DR VEuPathDB; HostDB:ENSMUSG00000096826; -.
DR eggNOG; ENOG502SZGD; Eukaryota.
DR GeneTree; ENSGT00530000063923; -.
DR HOGENOM; CLU_1885093_0_0_1; -.
DR InParanoid; Q9Z1X0; -.
DR OMA; PITTCCT; -.
DR OrthoDB; 1574270at2759; -.
DR PhylomeDB; Q9Z1X0; -.
DR TreeFam; TF337014; -.
DR Reactome; R-MMU-380108; Chemokine receptors bind chemokines.
DR Reactome; R-MMU-418594; G alpha (i) signalling events.
DR BioGRID-ORCS; 100039863; 2 hits in 28 CRISPR screens.
DR BioGRID-ORCS; 100039939; 1 hit in 5 CRISPR screens.
DR BioGRID-ORCS; 100040048; 5 hits in 35 CRISPR screens.
DR BioGRID-ORCS; 100861978; 1 hit in 5 CRISPR screens.
DR BioGRID-ORCS; 20301; 0 hits in 42 CRISPR screens.
DR ChiTaRS; Ccl27a; mouse.
DR PRO; PR:Q9Z1X0; -.
DR Proteomes; UP000000589; Chromosome 4.
DR RNAct; Q9Z1X0; protein.
DR Bgee; ENSMUSG00000073877; Expressed in spermatocyte and 65 other tissues.
DR Genevisible; Q9Z1X0; MM.
DR GO; GO:0005576; C:extracellular region; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0031728; F:CCR3 chemokine receptor binding; ISO:MGI.
DR GO; GO:0008009; F:chemokine activity; IDA:UniProtKB.
DR GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR GO; GO:0061844; P:antimicrobial humoral immune response mediated by antimicrobial peptide; ISO:MGI.
DR GO; GO:0060326; P:cell chemotaxis; IDA:UniProtKB.
DR GO; GO:0031640; P:killing of cells of another organism; ISO:MGI.
DR GO; GO:2000251; P:positive regulation of actin cytoskeleton reorganization; IDA:MGI.
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 SMART; SM00199; SCY; 1.
DR SUPFAM; SSF54117; SSF54117; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; Cytokine; Disulfide bond; Nucleus;
KW Reference proteome; Secreted; Signal.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..120
FT /note="C-C motif chemokine 27"
FT /id="PRO_0000005240"
FT DISULFID 34..63
FT /evidence="ECO:0000250"
FT DISULFID 35..78
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..24
FT /note="MMEGLSPASSLPLLLLLLSPAPEA -> MWRRERSPMSPTSQRLSLEAPSLP
FT LRSWHPWNKTKQKQE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_001065"
FT CONFLICT 115
FT /note="H -> N (in Ref. 1; AAD04163, 2; BAA88474, 3;
FT AAD41237 and 4; BAB24001)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 120 AA; 13464 MW; D1EEE1270AB580BF CRC64;
MMEGLSPASS LPLLLLLLSP APEAALPLPS STSCCTQLYR QPLPSRLLRR IVHMELQEAD
GDCHLQAVVL HLARRSVCVH PQNRSLARWL ERQGKRLQGT VPSLNLVLQK KMYSHPQQQN
