ID   IL16_SAISC              Reviewed;         627 AA.
AC   O62677;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 81.
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   Saimiri sciureus (Common squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=9521;
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; AF017109; AAC16037.1; -; mRNA.
DR   AlphaFoldDB; O62677; -.
DR   SMR; O62677; -.
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   2: Evidence at transcript level;
KW   Chemotaxis; Cytokine; Cytoplasm; Nucleus; Phosphoprotein; Repeat; Secreted;
KW   Transcription; Transcription regulation.
FT   CHAIN           1..627
FT                   /note="Pro-interleukin-16"
FT                   /id="PRO_0000377548"
FT   CHAIN           507..627
FT                   /note="Interleukin-16"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015422"
FT   DOMAIN          407..492
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          529..614
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          34..136
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          162..267
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          316..337
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          401..497
FT                   /note="Interaction with PPP1R12A, PPP1R12B and PPP1R12C"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        34..49
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        194..210
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        217..237
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        317..337
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         217
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14005"
SQ   SEQUENCE   627 AA;  66221 MW;  8DB5C53BA10BE38F CRC64;
     MDYSFDTTAE DPWVRISDCI KNLFSPIMTE NHSHMPLQPN VSLSEGDGTQ GHPDGTPPKL
     ETANGTPKVY RPADSSTVKK GPPVAPKPAW FRQSLKGLRN RASDPRRLPD PALSVQPVPA
     SREHPGPHTQ ASSIKQRISS FETFGSSQRL DKGAQRLSLQ LSSGEAAKPV GKHEGGRLPG
     LLGRGAVPTL APQETEQVLP SGSPAASEAT DPGVSESPPP GRQPSEKTLP PSPDPLLRLL
     PTQTEESQGP VLKMPSQRAR SFPLTRSQSC ETKLLDEKTS KLYSISSQVS SAVMKSLLCL
     PSSISWGQAP CIPKEGASPT SLSNEDSAAN GCAETSGSDT GFSLNLSELR EYTEGLTEAK
     EADDGDHSSP QSGQSVISLL SSEELKQLIE EVKDLDEATL KQLDSIHVTI LHKEEGAGLG
     FSLAGGADLE NKVITVHRVF PNGLASQEGT IQKGNEVLSI NGKSLKGTTH NDALAILRQA
     REPRQAVIVT RKLTPETVPD LNSSTDSAAS ASAASDVSVD STAEATVCTV TLEKMSGGLG
     FSLEGGKGSL QGDKPLTINR IFKGAASEQS ETVQPGDEIL HLAGTAMQGL TRFEAWNIIK
     ALPDGPVTIV IKRKSMQSKG TSAAGDS