IL16_PANTR
ID IL16_PANTR Reviewed; 631 AA.
AC O62666;
DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 25-MAY-2022, entry version 112.
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 Pan troglodytes (Chimpanzee).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pan.
OX NCBI_TaxID=9598;
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; AF007879; AAC16030.1; -; mRNA.
DR RefSeq; NP_001009028.1; NM_001009028.1.
DR RefSeq; XP_009427855.1; XM_009429580.2.
DR AlphaFoldDB; O62666; -.
DR SMR; O62666; -.
DR STRING; 9598.ENSPTRP00000012595; -.
DR PaxDb; O62666; -.
DR GeneID; 449644; -.
DR CTD; 3603; -.
DR eggNOG; KOG3528; Eukaryota.
DR InParanoid; O62666; -.
DR Proteomes; UP000002277; 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..631
FT /note="Pro-interleukin-16"
FT /id="PRO_0000377547"
FT CHAIN 511..631
FT /note="Interleukin-16"
FT /evidence="ECO:0000250"
FT /id="PRO_0000015420"
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 31..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..340
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 127..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..235
FT /note="Pro 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; 66656 MW; 7FF9E4EBE623ECB5 CRC64;
MDYSFDTTAE DPWVRISDCI KNLFSPIMSE SHGHMPLQPN ASLNEEDGTQ GHPDGTPPKL
DTANGTPKVY KSADSSTVKK GPPVAPKPAW FRQSLKGLRN RASDPRGLPD PALSTQPAPA
SREHLGSHIR ASSSSSSIRQ RISSFETFGS SQLPDKGAQR LSLQPSSGEA AKPLGKHEEG
RFSGLLGRGA APTLVPQQPE QVLSSGSPAA SEARDPGVSE SPPPGRQPNQ KTLPPGPDPL
LRLLSTQTEE SQGPVLKMPS QRARSFPLTR SQSCETKLLD EKTSKLYSIS SQVSSAVMKS
LLCLPSSISC AQTPCIPKEG ASPTSSSNED SAANGSAETS ALDTGFSLNL SELREYTEGL
TEAKEDDDGD HSSLQSGQSV ISLLSSEELK KLIEEVKVLD EATLKQLDSI HVTILHKEEG
AGLGFSLAGG ADLENKVITV HRVFPNGLAS QEGTIQKGNE VLSINGKSLK GTTHNDALAI
LRQAREPRQA VIVTRKLTPE AMPDLNSSTD SAASASAASD VSVESTAEAT VCTVTLEKMS
AGLGFSLEGG KGSLHGDKPL TINRIFKGAA SEQSETVQPG DEILQLAGTA MQGLTRFEAW
NIIKALPDGP VTIVIRRKSL QSKETTAAGD S
