ID   IL16_AOTTR              Reviewed;         632 AA.
AC   O62678;
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   Aotus trivirgatus (Three-striped night monkey) (Douroucouli).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Aotidae;
OC   Aotus.
OX   NCBI_TaxID=9505;
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; AF017110; AAC16038.1; -; mRNA.
DR   AlphaFoldDB; O62678; -.
DR   SMR; O62678; -.
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..632
FT                   /note="Pro-interleukin-16"
FT                   /id="PRO_0000377540"
FT   CHAIN           512..632
FT                   /note="Interleukin-16"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015408"
FT   DOMAIN          412..497
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          534..619
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          30..270
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          320..347
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          406..502
FT                   /note="Interaction with PPP1R12A, PPP1R12B and PPP1R12C"
FT                   /evidence="ECO:0000250"
FT   REGION          497..520
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        30..71
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        126..170
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..256
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        501..520
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         222
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14005"
SQ   SEQUENCE   632 AA;  66616 MW;  75072045E684BDEE CRC64;
     MDYSFDTTAE DPWVRISDCI KNLFSPMMTE NHSHMPLQPN ASLSEDDGTQ GHSDGTPPKL
     ETANGTSKVY RPADSSAVKK GPPVAPKPAW FRQSLKGLRN RASDPRRLPD PALSTQPGPA
     SREHPGPHTQ ASSSSSSSIK QRISSFETFG SSQRPDRGAQ RLSLQLSSGE ATKPVGKHEG
     GRLPGLLGRG AAPTLAPQET EQLLSSGSPA ASEVRDPGVS ESPPTGRQPS EKTLPPGPDP
     LLQLLSTQTE ESQGPVLKMP SQRARSFPLT RSQSCETKLL DEKTSKLYSI SSQVSSAVMK
     SLLCLPSSIT WGQTPCIPRE GASATSSSNA DSAANGSAET SGSDTGFSLN LSELREYTEG
     LTEAKEADDG DHCSPQSGQS VISLLSSEEL KKLIEEVKDL DEATLKQLDS IHVTILHKEE
     GAGLGFSLAG GADLENKVIT VHRVFPNGLA SQEGTIQKGN EVLSINGKSL KGTTHNDALA
     ILRQAREPRQ AVIVTRKPTP ETAPDLNSST DSAASVSAAS DVSVDSTAEA TVCTVTLEKM
     SGGLGFSLEG GKGSLHGDKP LTINRIFKGA ASEQSETVQP GDEILHLAGT AMQGLTRFEA
     WNIIKALPDG PVTIVIKRKS MQSKGTPAAG DS