IL16_MACMU
ID IL16_MACMU Reviewed; 630 AA.
AC O62675;
DT 27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Pro-interleukin-16;
DE Contains:
DE RecName: Full=Interleukin-16;
DE Short=IL-16;
DE AltName: Full=Lymphocyte chemoattractant factor;
DE Short=LCF;
GN Name=IL16;
OS Macaca mulatta (Rhesus macaque).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Macaca.
OX NCBI_TaxID=9544;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=9510557; DOI=10.1007/s002510050374;
RA Bannert N., Adler H.S., Werner A., Baier M., Kurth R.;
RT "Molecular cloning and sequence analysis of interleukin 16 from nonhuman
RT primates and from the mouse.";
RL Immunogenetics 47:390-397(1998).
CC -!- FUNCTION: Interleukin-16 stimulates a migratory response in CD4+
CC lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for IL-2
CC and IL-15 responsiveness. Also induces T-lymphocyte expression of
CC interleukin 2 receptor. Ligand for CD4 (By similarity). {ECO:0000250}.
CC -!- FUNCTION: Pro-interleukin-16 is involved in cell cycle progression in
CC T-cells. Appears to be involved in transcriptional regulation of SKP2
CC and is probably part of a transcriptional repression complex on the
CC core promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the
CC DNA-binding subunit the GABP transcription factor complex) and HDAC3
CC thus maintaining transcriptional repression and blocking cell cycle
CC progression in resting T-cells (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homotetramer (Probable). Pro-interleukin-16 interacts (via PDZ
CC 2 domain) with PPP1R12A, PPP1R12B and PPP1R12C. Pro-interleukin-16
CC interacts with GRIN2A. Pro-interleukin-16 interacts with GABPB1. Pro-
CC interleukin-16 interacts (via PDZ 3 domain) with HDAC3 (By similarity).
CC {ECO:0000250, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: [Interleukin-16]: Secreted {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Pro-interleukin-16]: Cytoplasm. Nucleus
CC {ECO:0000250}.
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DR EMBL; AF017107; AAC16035.1; -; mRNA.
DR RefSeq; NP_001027980.1; NM_001032808.1.
DR AlphaFoldDB; O62675; -.
DR SMR; O62675; -.
DR STRING; 9544.ENSMMUP00000015164; -.
DR GeneID; 574100; -.
DR KEGG; mcc:574100; -.
DR CTD; 3603; -.
DR eggNOG; KOG3528; Eukaryota.
DR InParanoid; O62675; -.
DR Proteomes; UP000006718; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0042609; F:CD4 receptor binding; IBA:GO_Central.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
DR GO; GO:0030595; P:leukocyte chemotaxis; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 2.
DR InterPro; IPR020450; IL-16.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 2.
DR PRINTS; PR01931; INTRLEUKIN16.
DR SMART; SM00228; PDZ; 2.
DR SUPFAM; SSF50156; SSF50156; 2.
DR PROSITE; PS50106; PDZ; 2.
PE 2: Evidence at transcript level;
KW Chemotaxis; Cytokine; Cytoplasm; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Secreted; Transcription;
KW Transcription regulation.
FT CHAIN 1..630
FT /note="Pro-interleukin-16"
FT /id="PRO_0000377545"
FT CHAIN 510..630
FT /note="Interleukin-16"
FT /evidence="ECO:0000250"
FT /id="PRO_0000015416"
FT DOMAIN 410..495
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 532..617
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 30..268
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 316..343
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..500
FT /note="Interaction with PPP1R12A, PPP1R12B and PPP1R12C"
FT /evidence="ECO:0000250"
FT COMPBIAS 35..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..165
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 229..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 220
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14005"
SQ SEQUENCE 630 AA; 66563 MW; 9689007AB1781EDD CRC64;
MDYSFDTTAE DPWVRISDCI KNLFSPIMSE NPGHMPLQPN ASLSEEDGTQ GHPDGNPPKL
DTANGTPKVY KSADRSTVKK GPPVAPKPAW FRQSLKGLRN RASDPRGLPD PALSTQPAPA
SREHLGPHIR ASSSSSIKQR ISSFETFGSS QLPDKGAQRL SLQPSSGEAA KPLGKHEGGR
FSGLLGRGAA PTLVPQQPEQ VLPSGSPAAT EARDPGVSES PPPGLQPNQK TLPTGSDPLL
RLLPTQTEKS QGPVLKMPSQ RARSFPLTRS QSCETKLLDE KTSKLYSISS QVSSAVMKSL
LCLPSSLSCA QTPCIPKEGA SPTSSSNEDS AANGSAETSA SDTGFSLNLS ELREYTEGLT
EAKEDDDGDH SSHQSGQSVI SLLSSEELKQ LIEEVKVLDE ATLKQLDSIH VTILHKEEGA
GLGFSLAGGA DLENKVITVH KVFPNGLASQ EGTIQKGNEV LSINGKSLKG TTHNDALAIL
RQAREPRQAV IVTRKLTAES MPDLNSTTDS AASASAASDV SVESSAEATV YTVTLEKMSA
GLGFSLEGGK GSLHGDKPLT INRIFKGAAS EQSETIQPGD EILQLAGTAM QGLTRFEAWN
IIKALPDGPV TIVIRRKSLQ PKETTAAADS
