CXCR4_RAT
ID CXCR4_RAT Reviewed; 349 AA.
AC O08565; F1LPN8; Q8VD47;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 10-OCT-2018, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=C-X-C chemokine receptor type 4;
DE Short=CXC-R4;
DE Short=CXCR-4;
DE AltName: Full=Fusin;
DE AltName: Full=Leukocyte-derived seven transmembrane domain receptor;
DE Short=LESTR;
DE AltName: Full=Stromal cell-derived factor 1 receptor;
DE Short=SDF-1 receptor;
DE AltName: CD_antigen=CD184;
GN Name=Cxcr4; Synonyms=Cmkar4;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Wistar; TISSUE=Spleen;
RA Harrison J.K., Salafranca M.N.;
RT "Molecular cloning of rat CXCR4.";
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000312|EMBL:AAL47855.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=Holtzman {ECO:0000312|EMBL:AAL47855.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAL47855.1};
RA Simen A.A., Miller R.J.;
RT "Chemokine regulation of neuronal signaling and gp120 neurotoxicity.";
RL Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus {ECO:0000312|EMBL:AAH89804.1};
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).
CC -!- FUNCTION: Receptor for the C-X-C chemokine CXCL12/SDF-1 that transduces
CC a signal by increasing intracellular calcium ion levels and enhancing
CC MAPK1/MAPK3 activation. Involved in the AKT signaling cascade (By
CC similarity). Plays a role in regulation of cell migration, e.g. during
CC wound healing. Acts as a receptor for extracellular ubiquitin; leading
CC to enhanced intracellular calcium ions and reduced cellular cAMP
CC levels. Binds bacterial lipopolysaccharide (LPS) et mediates LPS-
CC induced inflammatory response, including TNF secretion by monocytes (By
CC similarity). Involved in hematopoiesis and in cardiac ventricular
CC septum formation. Also plays an essential role in vascularization of
CC the gastrointestinal tract, probably by regulating vascular branching
CC and/or remodeling processes in endothelial cells. Involved in
CC cerebellar development. In the CNS, could mediate hippocampal-neuron
CC survival (By similarity). {ECO:0000250|UniProtKB:P61073,
CC ECO:0000250|UniProtKB:P70658}.
CC -!- SUBUNIT: Monomer. Can form homodimers. Interacts with CD164. Interacts
CC with ARRB2; the interaction is dependent on the C-terminal
CC phosphorylation of CXCR4 and allows activation of MAPK1 and MAPK3.
CC Interacts with ARR3; the interaction is dependent on the C-terminal
CC phosphorylation of CXCR4 and modulates calcium mobilization. Interacts
CC with RNF113A; the interaction, enhanced by CXCL12, promotes CXCR4
CC ubiquitination and subsequent degradation. Interacts (via the
CC cytoplasmic C-terminal) with ITCH (via the WW domains I and II); the
CC interaction, enhanced by CXCL12, promotes CXCR4 ubiquitination and
CC leads to its degradation. Interacts with extracellular ubiquitin.
CC Interacts with DBN1; this interaction is enhanced by antigenic
CC stimulation. Following LPS binding, may form a complex with GDF5,
CC HSP90AA1 and HSPA8. {ECO:0000250|UniProtKB:P61073}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P61073};
CC Multi-pass membrane protein {ECO:0000250|UniProtKB:P61073}. Cell
CC junction {ECO:0000250}. Early endosome {ECO:0000250}. Late endosome
CC {ECO:0000250}. Lysosome {ECO:0000250}. Note=In unstimulated cells,
CC diffuse pattern on plasma membrane. On agonist stimulation, colocalizes
CC with ITCH at the plasma membrane where it becomes ubiquitinated (By
CC similarity). In the presence of antigen, distributes to the
CC immunological synapse forming at the T-cell-APC contact area, where it
CC localizes at the peripheral and distal supramolecular activation
CC cluster (SMAC) (By similarity). {ECO:0000250}.
CC -!- PTM: Phosphorylated on agonist stimulation. Rapidly phosphorylated on
CC serine and threonine residues in the C-terminal. Phosphorylation at
CC Ser-321 and Ser-322 leads to recruitment of ITCH, ubiquitination and
CC protein degradation. {ECO:0000250|UniProtKB:P61073}.
CC -!- PTM: Ubiquitinated after ligand binding, leading to its degradation.
CC Ubiquitinated by ITCH at the cell membrane on agonist stimulation. The
CC ubiquitin-dependent mechanism, endosomal sorting complex required for
CC transport (ESCRT), then targets CXCR4 for lysosomal degradation. This
CC process is dependent also on prior Ser-/Thr-phosphorylation in the C-
CC terminal of CXCR4. Also binding of ARRB1 to STAM negatively regulates
CC CXCR4 sorting to lysosomes though modulating ubiquitination of SFR5S.
CC {ECO:0000250|UniProtKB:P61073}.
CC -!- PTM: Sulfation is required for efficient binding of CXCL12/SDF-1alpha
CC and promotes its dimerization. {ECO:0000250|UniProtKB:P61073}.
CC -!- PTM: O- and N-glycosylated. N-glycosylation can mask coreceptor
CC function. The O-glycosylation chondroitin sulfate attachment does not
CC affect interaction with CXCL12/SDF-1alpha nor its coreceptor activity.
CC {ECO:0000250|UniProtKB:P61073}.
CC -!- SIMILARITY: Belongs to the G-protein coupled receptor 1 family.
CC {ECO:0000255|PROSITE-ProRule:PRU00521}.
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DR EMBL; U90610; AAB50408.1; -; mRNA.
DR EMBL; AF452185; AAL47855.1; -; mRNA.
DR EMBL; AABR07020898; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473958; EDM09871.1; -; Genomic_DNA.
DR EMBL; BC089804; AAH89804.1; -; mRNA.
DR RefSeq; NP_071541.2; NM_022205.3.
DR AlphaFoldDB; O08565; -.
DR SMR; O08565; -.
DR IntAct; O08565; 5.
DR MINT; O08565; -.
DR STRING; 10116.ENSRNOP00000005143; -.
DR BindingDB; O08565; -.
DR ChEMBL; CHEMBL5556; -.
DR DrugCentral; O08565; -.
DR GuidetoPHARMACOLOGY; 71; -.
DR GlyGen; O08565; 2 sites.
DR PhosphoSitePlus; O08565; -.
DR PaxDb; O08565; -.
DR PRIDE; O08565; -.
DR Ensembl; ENSRNOT00000005143; ENSRNOP00000005143; ENSRNOG00000003866.
DR GeneID; 60628; -.
DR KEGG; rno:60628; -.
DR UCSC; RGD:620465; rat.
DR CTD; 7852; -.
DR RGD; 620465; Cxcr4.
DR eggNOG; KOG3656; Eukaryota.
DR GeneTree; ENSGT01050000244848; -.
DR HOGENOM; CLU_009579_8_3_1; -.
DR InParanoid; O08565; -.
DR OMA; TIVHKWI; -.
DR OrthoDB; 773026at2759; -.
DR PhylomeDB; O08565; -.
DR Reactome; R-RNO-380108; Chemokine receptors bind chemokines.
DR Reactome; R-RNO-418594; G alpha (i) signalling events.
DR PRO; PR:O08565; -.
DR Proteomes; UP000002494; Chromosome 13.
DR Proteomes; UP000234681; Chromosome 13.
DR Bgee; ENSRNOG00000003866; Expressed in thymus and 20 other tissues.
DR ExpressionAtlas; O08565; baseline and differential.
DR GO; GO:0031252; C:cell leading edge; ISO:RGD.
DR GO; GO:0009986; C:cell surface; ISO:RGD.
DR GO; GO:0005911; C:cell-cell junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IDA:RGD.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0005769; C:early endosome; ISS:UniProtKB.
DR GO; GO:0005768; C:endosome; IDA:RGD.
DR GO; GO:0009897; C:external side of plasma membrane; ISO:RGD.
DR GO; GO:0030426; C:growth cone; ISO:RGD.
DR GO; GO:0016021; C:integral component of membrane; TAS:RGD.
DR GO; GO:0005770; C:late endosome; ISS:UniProtKB.
DR GO; GO:0005764; C:lysosome; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IDA:RGD.
DR GO; GO:0032991; C:protein-containing complex; ISO:RGD.
DR GO; GO:0003779; F:actin binding; ISO:RGD.
DR GO; GO:0019957; F:C-C chemokine binding; ISO:RGD.
DR GO; GO:0016493; F:C-C chemokine receptor activity; IBA:GO_Central.
DR GO; GO:0016494; F:C-X-C chemokine receptor activity; TAS:RGD.
DR GO; GO:0038147; F:C-X-C motif chemokine 12 receptor activity; ISS:UniProtKB.
DR GO; GO:0032027; F:myosin light chain binding; ISO:RGD.
DR GO; GO:0036094; F:small molecule binding; IMP:RGD.
DR GO; GO:0043130; F:ubiquitin binding; ISO:RGD.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; ISO:RGD.
DR GO; GO:0001667; P:ameboidal-type cell migration; ISO:RGD.
DR GO; GO:0035904; P:aorta development; ISO:RGD.
DR GO; GO:0007420; P:brain development; ISO:RGD.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; ISO:RGD.
DR GO; GO:0019722; P:calcium-mediated signaling; ISO:RGD.
DR GO; GO:0060048; P:cardiac muscle contraction; IMP:RGD.
DR GO; GO:0060326; P:cell chemotaxis; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IMP:RGD.
DR GO; GO:0071345; P:cellular response to cytokine stimulus; ISS:UniProtKB.
DR GO; GO:0071466; P:cellular response to xenobiotic stimulus; IEP:RGD.
DR GO; GO:0038160; P:CXCL12-activated CXCR4 signaling pathway; ISS:UniProtKB.
DR GO; GO:0050966; P:detection of mechanical stimulus involved in sensory perception of pain; IMP:RGD.
DR GO; GO:0050965; P:detection of temperature stimulus involved in sensory perception of pain; IMP:RGD.
DR GO; GO:0045446; P:endothelial cell differentiation; IMP:RGD.
DR GO; GO:0061154; P:endothelial tube morphogenesis; IMP:RGD.
DR GO; GO:0002064; P:epithelial cell development; IMP:RGD.
DR GO; GO:0007186; P:G protein-coupled receptor signaling pathway; ISO:RGD.
DR GO; GO:0048699; P:generation of neurons; ISO:RGD.
DR GO; GO:0007281; P:germ cell development; ISO:RGD.
DR GO; GO:0008354; P:germ cell migration; ISO:RGD.
DR GO; GO:0035701; P:hematopoietic stem cell migration; ISO:RGD.
DR GO; GO:0006955; P:immune response; IBA:GO_Central.
DR GO; GO:0001822; P:kidney development; ISO:RGD.
DR GO; GO:0008045; P:motor neuron axon guidance; ISO:RGD.
DR GO; GO:0043217; P:myelin maintenance; ISO:RGD.
DR GO; GO:0061351; P:neural precursor cell proliferation; ISO:RGD.
DR GO; GO:0022008; P:neurogenesis; IMP:RGD.
DR GO; GO:0001764; P:neuron migration; IDA:RGD.
DR GO; GO:0008038; P:neuron recognition; IEP:RGD.
DR GO; GO:0090280; P:positive regulation of calcium ion import; ISO:RGD.
DR GO; GO:0030335; P:positive regulation of cell migration; IMP:RGD.
DR GO; GO:0050921; P:positive regulation of chemotaxis; IMP:RGD.
DR GO; GO:0120162; P:positive regulation of cold-induced thermogenesis; ISS:YuBioLab.
DR GO; GO:0007204; P:positive regulation of cytosolic calcium ion concentration; IBA:GO_Central.
DR GO; GO:1903861; P:positive regulation of dendrite extension; IMP:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; ISO:RGD.
DR GO; GO:2000448; P:positive regulation of macrophage migration inhibitory factor signaling pathway; ISO:RGD.
DR GO; GO:1905322; P:positive regulation of mesenchymal stem cell migration; IMP:RGD.
DR GO; GO:0050769; P:positive regulation of neurogenesis; IMP:RGD.
DR GO; GO:0048714; P:positive regulation of oligodendrocyte differentiation; ISO:RGD.
DR GO; GO:0001934; P:positive regulation of protein phosphorylation; ISO:RGD.
DR GO; GO:0035470; P:positive regulation of vascular wound healing; IMP:RGD.
DR GO; GO:0051924; P:regulation of calcium ion transport; IMP:RGD.
DR GO; GO:0030155; P:regulation of cell adhesion; ISO:RGD.
DR GO; GO:0030334; P:regulation of cell migration; ISO:RGD.
DR GO; GO:0050920; P:regulation of chemotaxis; IMP:RGD.
DR GO; GO:0043067; P:regulation of programmed cell death; IMP:RGD.
DR GO; GO:0050792; P:regulation of viral process; IDA:RGD.
DR GO; GO:0014823; P:response to activity; IEP:RGD.
DR GO; GO:0001666; P:response to hypoxia; ISO:RGD.
DR GO; GO:0043278; P:response to morphine; IEP:RGD.
DR GO; GO:0014070; P:response to organic cyclic compound; IMP:RGD.
DR GO; GO:1990478; P:response to ultrasound; IEP:RGD.
DR GO; GO:0042098; P:T cell proliferation; ISO:RGD.
DR GO; GO:0022029; P:telencephalon cell migration; IMP:RGD.
DR GO; GO:0003281; P:ventricular septum development; ISO:RGD.
DR InterPro; IPR022726; Chemokine_CXCR4_N_dom.
DR InterPro; IPR000355; Chemokine_rcpt.
DR InterPro; IPR001277; CXCR4/ACKR2.
DR InterPro; IPR000276; GPCR_Rhodpsn.
DR InterPro; IPR017452; GPCR_Rhodpsn_7TM.
DR Pfam; PF00001; 7tm_1; 1.
DR Pfam; PF12109; CXCR4_N; 1.
DR PRINTS; PR00657; CCCHEMOKINER.
DR PRINTS; PR00645; CXCCHMKINER4.
DR PRINTS; PR00237; GPCRRHODOPSN.
DR PROSITE; PS00237; G_PROTEIN_RECEP_F1_1; 1.
DR PROSITE; PS50262; G_PROTEIN_RECEP_F1_2; 1.
PE 2: Evidence at transcript level;
KW Cell junction; Cell membrane; Disulfide bond; Endosome;
KW G-protein coupled receptor; Glycoprotein; Isopeptide bond; Lysosome;
KW Membrane; Phosphoprotein; Proteoglycan; Receptor; Reference proteome;
KW Sulfation; Transducer; Transmembrane; Transmembrane helix; Ubl conjugation.
FT CHAIN 1..349
FT /note="C-X-C chemokine receptor type 4"
FT /id="PRO_0000069358"
FT TOPO_DOM 1..35
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 36..60
FT /note="Helical; Name=1"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT TOPO_DOM 61..74
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 75..96
FT /note="Helical; Name=2"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT TOPO_DOM 97..107
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 108..127
FT /note="Helical; Name=3"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT TOPO_DOM 128..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 152..171
FT /note="Helical; Name=4"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT TOPO_DOM 172..192
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 193..213
FT /note="Helical; Name=5"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT TOPO_DOM 214..238
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 239..258
FT /note="Helical; Name=6"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT TOPO_DOM 259..279
FT /note="Extracellular"
FT /evidence="ECO:0000305"
FT TRANSMEM 280..299
FT /note="Helical; Name=7"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT TOPO_DOM 300..349
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1..18
FT /note="Important for chemokine binding and signaling"
FT /evidence="ECO:0000250"
FT REGION 91..94
FT /note="Chemokine binding"
FT /evidence="ECO:0000250"
FT REGION 110..114
FT /note="Chemokine binding"
FT /evidence="ECO:0000250"
FT REGION 132..144
FT /note="Involved in dimerization; when bound to chemokine"
FT /evidence="ECO:0000250"
FT REGION 183..187
FT /note="Chemokine binding, important for signaling"
FT /evidence="ECO:0000250"
FT REGION 188..207
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
FT REGION 263..265
FT /note="Involved in dimerization"
FT /evidence="ECO:0000250"
FT REGION 325..349
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 130..132
FT /note="Important for signaling"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 332..349
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 168
FT /note="Chemokine binding"
FT /evidence="ECO:0000250"
FT SITE 285
FT /note="Chemokine binding"
FT /evidence="ECO:0000250"
FT MOD_RES 9
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT MOD_RES 18
FT /note="Sulfotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT MOD_RES 316
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT MOD_RES 318
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT MOD_RES 321
FT /note="Phosphoserine; by PKC and GRK6"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT MOD_RES 322
FT /note="Phosphoserine; by PKC and GRK6"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT MOD_RES 327
FT /note="Phosphoserine; by GRK6"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT MOD_RES 336
FT /note="Phosphoserine; by GRK6"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT MOD_RES 345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT CARBOHYD 8
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000250"
FT CARBOHYD 15
FT /note="O-linked (Xyl...) (chondroitin sulfate) serine"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT DISULFID 25..271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT DISULFID 106..183
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00521"
FT CROSSLNK 328
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:P61073"
FT CONFLICT 143..144
FT /note="RP -> SA (in Ref. 1; AAB50408)"
SQ SEQUENCE 349 AA; 39429 MW; 09D19860D3D2CB8A CRC64;
MEIYTSDNYS EEVGSGDYDS NKEPCFRDEN ENFNRIFLPT IYFIIFLTGI VGNGLVILVM
GYQKKLRSMT DKYRLHLSVA DLLFVITLPF WAVDAMADWY FGKFLCKAVH IIYTVNLYSS
VLILAFISLD RYLAIVHATN SQRPRKLLAE KAVYVGVWIP ALLLTIPDII FADVSQGDGR
YICDRLYPDS LWMVVFQFQH IMVGLILPGI VILSCYCIII SKLSHSKGHQ KRKALKTTVI
LILAFFACWL PYYVGISIDS FILLEVIKQG CEFESVVHKW ISITEALAFF HCCLNPILYA
FLGAKFKSSA QHALNSMSRG SSLKILSKGK RGGHSSVSTE SESSSFHSS
