ID   IL16_MACFA              Reviewed;         630 AA.
AC   O62676;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 88.
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 fascicularis (Crab-eating macaque) (Cynomolgus monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Macaca.
OX   NCBI_TaxID=9541;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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; AF017108; AAC16036.1; -; Genomic_DNA.
DR   AlphaFoldDB; O62676; -.
DR   SMR; O62676; -.
DR   STRING; 9541.XP_005560322.1; -.
DR   eggNOG; KOG3528; Eukaryota.
DR   Proteomes; UP000233100; 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:0005125; F:cytokine activity; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
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   3: Inferred from homology;
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_0000377544"
FT   CHAIN           510..630
FT                   /note="Interleukin-16"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015414"
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;  66551 MW;  968915A081781EDD 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 TTVIRRKSLQ PKETTAAADS