ID   IL16_CHLAE              Reviewed;         631 AA.
AC   O62674;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   25-MAY-2022, entry version 84.
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   Chlorocebus aethiops (Green monkey) (Cercopithecus aethiops).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Chlorocebus.
OX   NCBI_TaxID=9534;
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; AF017106; AAC16034.1; -; mRNA.
DR   PIR; S62401; S62401.
DR   AlphaFoldDB; O62674; -.
DR   SMR; O62674; -.
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..631
FT                   /note="Pro-interleukin-16"
FT                   /id="PRO_0000377542"
FT   CHAIN           511..631
FT                   /note="Interleukin-16"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015410"
FT   DOMAIN          411..496
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          533..618
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          30..269
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          317..344
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          405..501
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..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        230..255
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         221
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14005"
SQ   SEQUENCE   631 AA;  66640 MW;  3FC0CB78AD347224 CRC64;
     MDYSFDTTAE DPWVRISDCI KNLFSPIMSE NPGHMPLQPN ASLSEEDGTQ GHPDGNPPKL
     DTANGTPKVY KSADRSTVKK GPPVAPKPAW FRQSLKGLRN RASDPRGLPD PALSTQPAPA
     SREHLGPHIR ASSSSSSIKQ RISSFETFGS SQLPDKGAQR LSLQPSSGEA AKPLGKHEGG
     RFSGLLGRGA APTLVPQQPE QVLPSGSPAA TEARDPGVSE SPPPGLQPNQ KTLPTGSDPL
     LRLLSTQTEK SQGPVLKMPS QRARSFPLTR SQSCETKLLD EKTSKLYSIS SQVSSAVMKS
     LLCLPSSLSC AQTPCIPKEG ASPTSSSNED SAANGSAETS ASDTGFSLNL SELREYTEGL
     TEAKEDDDGD HSSHQSGQSV ISLLSSEELK QLIEEVKVLD EATLKQLDSI HVTILHKEEG
     AGLGFSLAGG ADLENKVITV HKVFPNGLAS QEGTIQKGNE VLSINGKSLK GTTHNDALAI
     LRQAREPRQA VIVTRKLTAE SMPDLNSTTD SAASASAASD VSVESSAEAT VYTVTLEKMS
     AGLGFSLEGG KGSLHGDKPL TINRIFKGAA SEQSETIQPG DEILQLAGTA MQGLTRFEAW
     NIIKALPDGP VTIVIRRKSL QPKETTAAAD S