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Pro-interleukin-16 [Cleaved into: Interleukin-16 (IL-16) (Lymphocyte chemoattractant factor) (LCF)]

 IL16_HUMAN              Reviewed;        1332 AA.
Q14005; A6NM20; A8MU65; B5TY35; B9EGR6; H3BVH5; Q16435; Q6VVE6;
Q6ZMQ7; Q9UP18;
01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
16-JUN-2009, sequence version 4.
25-OCT-2017, entry version 170.
RecName: Full=Pro-interleukin-16;
Contains:
RecName: Full=Interleukin-16;
Short=IL-16;
AltName: Full=Lymphocyte chemoattractant factor;
Short=LCF;
Name=IL16;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH PPP1R12A;
PPP1R12B; PPP1R12C AND GRIN2A.
PubMed=12923170; DOI=10.1074/jbc.M306669200;
Bannert N., Vollhardt K., Asomuddinov B., Haag M., Koenig H.,
Norley S., Kurth R.;
"PDZ domain-mediated interaction of interleukin-16 precursor proteins
with myosin phosphatase targeting subunits.";
J. Biol. Chem. 278:42190-42199(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=19906316; DOI=10.1186/1471-2164-10-518;
Wang P., Yu P., Gao P., Shi T., Ma D.;
"Discovery of novel human transcript variants by analysis of intronic
single-block EST with polyadenylation site.";
BMC Genomics 10:518-518(2009).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
TISSUE=Peripheral blood;
Kornfeld H.;
Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Cerebellum;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Testis;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 685-1332.
PubMed=9990060; DOI=10.1073/pnas.96.4.1541;
Bannert N., Avots A., Baier M., Serfling E., Kurth R.;
"GA-binding protein factors, in concert with the coactivator CREB
binding protein/p300, control the induction of the interleukin 16
promoter in T lymphocytes.";
Proc. Natl. Acad. Sci. U.S.A. 96:1541-1546(1999).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 685-1332, AND VARIANTS GLN-889;
LEU-906 AND LYS-1147.
SeattleSNPs variation discovery resource;
Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 942-1332.
PubMed=8609984; DOI=10.1038/381030a0;
Bannert N., Baier M., Werner A., Kurth R.;
"Interleukin-16 or not?";
Nature 381:30-30(1996).
[10]
NUCLEOTIDE SEQUENCE [MRNA] OF 1203-1332, AND SUBUNIT.
TISSUE=Peripheral blood;
PubMed=7910967; DOI=10.1073/pnas.91.11.5109;
Cruikshank W.W., Center D.M., Nisar N., Wu M., Natke B.C.,
Theodore A.C., Kornfeld H.;
"Molecular and functional analysis of a lymphocyte chemoattractant
factor: association of biologic function with CD4 expression.";
Proc. Natl. Acad. Sci. U.S.A. 91:5109-5113(1994).
[11]
NUCLEOTIDE SEQUENCE [MRNA] OF 1203-1332.
Du Y., Du G.X., Hou L.H., Wang H.T.;
"Cloning, expression and purification of human interleukin-16.";
Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 15:25-27(1999).
[12]
PROTEIN SEQUENCE OF 1212-1220, PROTEOLYTIC PROCESSING, AND MUTAGENESIS
OF ASP-1211.
PubMed=9422780; DOI=10.1074/jbc.273.2.1144;
Zhang Y., Center D.M., Wu D.M., Cruikshank W.W., Yuan J.,
Andrews D.W., Kornfeld H.;
"Processing and activation of pro-interleukin-16 by caspase-3.";
J. Biol. Chem. 273:1144-1149(1998).
[13]
SUBCELLULAR LOCATION (PRO-INTERLEUKIN-16), AND MUTAGENESIS OF
780-LYS-LYS-781 AND 797-LYS--ARG-802.
PubMed=11032842; DOI=10.1074/jbc.M008513200;
Zhang Y., Kornfeld H., Cruikshank W.W., Kim S., Reardon C.C.,
Center D.M.;
"Nuclear translocation of the N-terminal prodomain of interleukin-
16.";
J. Biol. Chem. 276:1299-1303(2001).
[14]
INDUCTION.
PubMed=11276202; DOI=10.1038/86318;
Feske S., Giltnane J., Dolmetsch R., Staudt L.M., Rao A.;
"Gene regulation mediated by calcium signals in T lymphocytes.";
Nat. Immunol. 2:316-324(2001).
[15]
PHOSPHORYLATION, AND MUTAGENESIS OF SER-743 AND THR-757.
PubMed=12450396; DOI=10.1021/bi020163v;
Wilson K.C., Cruikshank W.W., Center D.M., Zhang Y.;
"Prointerleukin-16 contains a functional CcN motif that regulates
nuclear localization.";
Biochemistry 41:14306-14312(2002).
[16]
INTERACTION WITH HTLV-1 TAX, AND SUBCELLULAR LOCATION.
PubMed=12620798; DOI=10.1016/S0042-6822(02)00056-9;
Wilson K.C., Center D.M., Cruikshank W.W., Zhang Y.;
"Binding of HTLV-1 tax oncoprotein to the precursor of interleukin-16,
a T cell PDZ domain-containing protein.";
Virology 306:60-67(2003).
[17]
FUNCTION (PRO-INTERLEUKIN-16), AND SUBCELLULAR LOCATION.
PubMed=14734747; DOI=10.4049/jimmunol.172.3.1654;
Center D.M., Cruikshank W.W., Zhang Y.;
"Nuclear pro-IL-16 regulation of T cell proliferation: p27(KIP1)-
dependent G0/G1 arrest mediated by inhibition of Skp2 transcription.";
J. Immunol. 172:1654-1660(2004).
[18]
FUNCTION (PRO-INTERLEUKIN-16), SUBCELLULAR LOCATION
(PRO-INTERLEUKIN-16), AND INTERACTION WITH GABPB1 AND HDAC3.
PubMed=18097041; DOI=10.4049/jimmunol.180.1.402;
Zhang Y., Tuzova M., Xiao Z.X., Cruikshank W.W., Center D.M.;
"Pro-IL-16 recruits histone deacetylase 3 to the Skp2 core promoter
through interaction with transcription factor GABP.";
J. Immunol. 180:402-408(2008).
[19]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-922, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[21]
STRUCTURE BY NMR OF 1203-1332.
PubMed=9699630; DOI=10.1038/1376;
Muehlhahn P., Zweckstetter M., Georgescu J., Ciosto C., Renner C.,
Lanzendoerfer M., Lang K., Ambrosius D., Baier M., Kurth R.,
Holak T.A.;
"Structure of interleukin 16 resembles a PDZ domain with an occluded
peptide binding site.";
Nat. Struct. Biol. 5:682-686(1998).
[22]
STRUCTURE BY NMR OF 1103-1209.
RIKEN structural genomics initiative (RSGI);
"Solution structures of the PDZ domain of human interleukin-16.";
Submitted (NOV-2005) to the PDB data bank.
-!- FUNCTION: Interleukin-16 stimulates a migratory response in CD4+
lymphocytes, monocytes, and eosinophils. Primes CD4+ T-cells for
IL-2 and IL-15 responsiveness. Also induces T-lymphocyte
expression of interleukin 2 receptor. Ligand for CD4.
-!- FUNCTION: Isoform 1 may act as a scaffolding protein that anchors
ion channels in the membrane.
-!- FUNCTION: Isoform 3 is involved in cell cycle progression in T-
cells. Appears to be involved in transcriptional regulation of
SKP2 and is probably part of a transcriptional repression complex
on the core promoter of the SKP2 gene. May act as a scaffold for
GABPB1 (the DNA-binding subunit the GABP transcription factor
complex) and HDAC3 thus maintaining transcriptional repression and
blocking cell cycle progression in resting T-cells.
-!- SUBUNIT: Homotetramer (Probable). According to PubMed:9699630, the
formation of a homotetrameric protein complex is not required for
the chemo-attractant function. Isoform 3 interacts (via PDZ 3
domain) with PPP1R12A, PPP1R12B and PPP1R12C. Isoform 1 interacts
with PPP1R12B. Isoform 3 interacts with GRIN2A. Isoform 3
interacts with GABPB1. Isoform 3 interacts (via PDZ 3 domain) with
HDAC3. Isoform 1 interacts with GRIN2D, KCNJ10, KCNJ15 and CACNA1C
(By similarity). Isoform 3 interacts with HTLV-1 tax.
{ECO:0000250, ECO:0000269|PubMed:12620798,
ECO:0000269|PubMed:12923170, ECO:0000269|PubMed:18097041,
ECO:0000269|PubMed:7910967, ECO:0000305}.
-!- SUBCELLULAR LOCATION: Interleukin-16: Secreted.
-!- SUBCELLULAR LOCATION: Isoform 1: Cytoplasm {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Isoform 3: Cytoplasm. Nucleus.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
Name=1; Synonyms=nPro-IL-16;
IsoId=Q14005-1; Sequence=Displayed;
Note=Produced by alternative promoter usage. Is probably
proteolytically processed to yield IL-16.;
Name=2;
IsoId=Q14005-2; Sequence=VSP_037459;
Note=Produced by alternative splicing of isoform 1. Is probably
proteolytically processed to yield IL-16.;
Name=3; Synonyms=Pro-IL-16;
IsoId=Q14005-3; Sequence=VSP_037458;
Note=Produced by alternative promoter usage. Is proteolytically
processed to yield IL-16.;
Name=4;
IsoId=Q14005-4; Sequence=VSP_037458, VSP_037459, VSP_057192;
-!- TISSUE SPECIFICITY: Isoform 3 is expressed in hemopoietic tissues,
such as resting T-cells, but is undetectable during active T-cell
proliferation.
-!- INDUCTION: Isoform 3 is down-regulated in T-cells after TCR
activation. {ECO:0000269|PubMed:11276202}.
-!- PTM: Isoform 3 is synthesized as a chemo-attractant inactive
precursor in hemopoietic tissues and is proteolytically cleaved by
caspase-3 to yield IL-16. {ECO:0000269|PubMed:9422780}.
-!- WEB RESOURCE: Name=SeattleSNPs;
URL="http://pga.gs.washington.edu/data/il16/";
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EMBL; AY324389; AAQ86961.1; -; mRNA.
EMBL; FJ032370; ACI00236.1; -; mRNA.
EMBL; M90391; AAD04636.1; -; mRNA.
EMBL; AK131530; BAD18668.1; -; mRNA.
EMBL; AC036196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; AC103858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF456108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC136660; AAI36661.1; -; mRNA.
EMBL; AF077011; AAD15990.1; -; Genomic_DNA.
EMBL; AY497901; AAR89904.1; -; Genomic_DNA.
EMBL; S81601; AAB36371.2; -; mRNA.
EMBL; AF053412; AAC12732.1; -; mRNA.
CCDS; CCDS10317.1; -. [Q14005-3]
CCDS; CCDS42069.1; -. [Q14005-1]
CCDS; CCDS53966.1; -. [Q14005-2]
PIR; I59298; I59298.
RefSeq; NP_001165599.1; NM_001172128.1. [Q14005-2]
RefSeq; NP_004504.3; NM_004513.5. [Q14005-3]
RefSeq; NP_757366.2; NM_172217.3. [Q14005-1]
RefSeq; XP_005254403.1; XM_005254346.4. [Q14005-3]
RefSeq; XP_011519822.1; XM_011521520.2. [Q14005-1]
RefSeq; XP_016877630.1; XM_017022141.1. [Q14005-1]
RefSeq; XP_016877631.1; XM_017022142.1. [Q14005-2]
UniGene; Hs.459095; -.
PDB; 1I16; NMR; -; A=1203-1332.
PDB; 1X6D; NMR; -; A=1103-1208.
PDB; 5FB8; X-ray; 2.07 A; C=1224-1323.
PDBsum; 1I16; -.
PDBsum; 1X6D; -.
PDBsum; 5FB8; -.
ProteinModelPortal; Q14005; -.
SMR; Q14005; -.
BioGrid; 109816; 25.
DIP; DIP-6006N; -.
IntAct; Q14005; 8.
MINT; MINT-7006013; -.
STRING; 9606.ENSP00000302935; -.
iPTMnet; Q14005; -.
PhosphoSitePlus; Q14005; -.
BioMuta; IL16; -.
DMDM; 239938922; -.
EPD; Q14005; -.
MaxQB; Q14005; -.
PaxDb; Q14005; -.
PeptideAtlas; Q14005; -.
PRIDE; Q14005; -.
Ensembl; ENST00000302987; ENSP00000302935; ENSG00000172349. [Q14005-1]
Ensembl; ENST00000394652; ENSP00000378147; ENSG00000172349. [Q14005-3]
Ensembl; ENST00000394660; ENSP00000378155; ENSG00000172349. [Q14005-2]
GeneID; 3603; -.
KEGG; hsa:3603; -.
UCSC; uc002bgg.4; human. [Q14005-1]
CTD; 3603; -.
DisGeNET; 3603; -.
EuPathDB; HostDB:ENSG00000172349.16; -.
GeneCards; IL16; -.
HGNC; HGNC:5980; IL16.
HPA; CAB005247; -.
HPA; HPA018467; -.
MIM; 603035; gene.
neXtProt; NX_Q14005; -.
OpenTargets; ENSG00000172349; -.
PharmGKB; PA29793; -.
eggNOG; KOG3528; Eukaryota.
eggNOG; ENOG4110362; LUCA.
GeneTree; ENSGT00760000119017; -.
HOVERGEN; HBG000100; -.
InParanoid; Q14005; -.
OMA; NSAPPHR; -.
OrthoDB; EOG091G0G6P; -.
PhylomeDB; Q14005; -.
TreeFam; TF326303; -.
Reactome; R-HSA-449836; Other interleukin signaling.
SIGNOR; Q14005; -.
EvolutionaryTrace; Q14005; -.
GeneWiki; Interleukin_16; -.
GenomeRNAi; 3603; -.
PMAP-CutDB; Q14005; -.
PRO; PR:Q14005; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000172349; -.
CleanEx; HS_IL16; -.
ExpressionAtlas; Q14005; baseline and differential.
Genevisible; Q14005; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; TAS:ProtInc.
GO; GO:0016607; C:nuclear speck; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0042609; F:CD4 receptor binding; IPI:CAFA.
GO; GO:0005125; F:cytokine activity; IEA:UniProtKB-KW.
GO; GO:0006955; P:immune response; TAS:ProtInc.
GO; GO:0050930; P:induction of positive chemotaxis; IEA:Ensembl.
GO; GO:0030595; P:leukocyte chemotaxis; IEA:Ensembl.
GO; GO:0051924; P:regulation of calcium ion transport; IDA:CAFA.
GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW.
GO; GO:0016032; P:viral process; IEA:UniProtKB-KW.
InterPro; IPR020450; IL-16.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
Pfam; PF00595; PDZ; 3.
PRINTS; PR01931; INTRLEUKIN16.
SMART; SM00228; PDZ; 4.
SUPFAM; SSF50156; SSF50156; 4.
PROSITE; PS50106; PDZ; 4.
1: Evidence at protein level;
3D-structure; Alternative promoter usage; Alternative splicing;
Chemotaxis; Complete proteome; Cytokine; Cytoplasm;
Direct protein sequencing; Host-virus interaction; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Repeat; Secreted;
Transcription; Transcription regulation.
CHAIN 1 1332 Pro-interleukin-16.
/FTId=PRO_0000377543.
CHAIN 1212 1332 Interleukin-16.
/FTId=PRO_0000015412.
DOMAIN 216 302 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 355 440 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1112 1197 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1234 1319 PDZ 4. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
REGION 183 452 Interaction with GRIN2A.
{ECO:0000269|PubMed:12923170}.
REGION 1034 1118 Interaction with HTLV-1 tax.
REGION 1106 1202 Interaction with PPP1R12A, PPP1R12B and
PPP1R12C. {ECO:0000269|PubMed:12923170}.
MOD_RES 922 922 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 701 Missing (in isoform 3 and isoform 4).
{ECO:0000303|PubMed:19906316,
ECO:0000303|Ref.3}.
/FTId=VSP_037458.
VAR_SEQ 1228 1228 Missing (in isoform 2 and isoform 4).
{ECO:0000303|PubMed:14702039,
ECO:0000303|PubMed:15489334,
ECO:0000303|PubMed:19906316}.
/FTId=VSP_037459.
VAR_SEQ 1239 1332 KMSAGLGFSLEGGKGSLHGDKPLTINRIFKGAASEQSETVQ
PGDEILQLGGTAMQGLTRFEAWNIIKALPDGPVTIVIRRKS
LQSKETTAAGDS -> DVGRAGLQPGRREGLPTRRQASHH
(in isoform 4).
{ECO:0000303|PubMed:19906316}.
/FTId=VSP_057192.
VARIANT 434 434 P -> S (in dbSNP:rs4072111).
/FTId=VAR_058310.
VARIANT 889 889 R -> Q (in dbSNP:rs17875512).
{ECO:0000269|Ref.8}.
/FTId=VAR_019203.
VARIANT 906 906 S -> L (in dbSNP:rs17875513).
{ECO:0000269|Ref.8}.
/FTId=VAR_019204.
VARIANT 1027 1027 S -> T (in dbSNP:rs34101586).
/FTId=VAR_034013.
VARIANT 1147 1147 N -> K (in dbSNP:rs11556218).
{ECO:0000269|Ref.8}.
/FTId=VAR_019205.
VARIANT 1176 1176 H -> R (in dbSNP:rs34159341).
/FTId=VAR_053372.
MUTAGEN 743 743 S->A: Reduces phosphorylation and nuclear
localization.
{ECO:0000269|PubMed:12450396}.
MUTAGEN 757 757 T->A: Reduces phosphorylation. Enhances
nuclear localization.
{ECO:0000269|PubMed:12450396}.
MUTAGEN 780 781 KK->AA: Reduces nuclear localization of
pro-interleukin-16; when associated with
797-AGLANA-802.
{ECO:0000269|PubMed:11032842}.
MUTAGEN 797 802 KGLRNR->AGLANA: Reduces nuclear
localization of pro-interleukin-16; when
associated with 780-AA-781.
{ECO:0000269|PubMed:11032842}.
MUTAGEN 1211 1211 D->A: Abolishes proteolytic cleavage.
{ECO:0000269|PubMed:9422780}.
CONFLICT 273 273 E -> G (in Ref. 1; AAQ86961).
{ECO:0000305}.
CONFLICT 427 427 H -> R (in Ref. 6; AAI36661).
{ECO:0000305}.
CONFLICT 805 805 D -> E (in Ref. 1; AAD04636).
{ECO:0000305}.
CONFLICT 934 934 L -> F (in Ref. 1; AAD04636).
{ECO:0000305}.
CONFLICT 942 944 LRL -> PRE (in Ref. 5). {ECO:0000305}.
CONFLICT 1020 1020 E -> A (in Ref. 1; AAD04636).
{ECO:0000305}.
STRAND 1111 1117 {ECO:0000244|PDB:1X6D}.
STRAND 1125 1129 {ECO:0000244|PDB:1X6D}.
STRAND 1132 1135 {ECO:0000244|PDB:1X6D}.
STRAND 1140 1144 {ECO:0000244|PDB:1X6D}.
STRAND 1146 1148 {ECO:0000244|PDB:1X6D}.
HELIX 1149 1153 {ECO:0000244|PDB:1X6D}.
HELIX 1175 1184 {ECO:0000244|PDB:1X6D}.
STRAND 1187 1196 {ECO:0000244|PDB:1X6D}.
STRAND 1200 1202 {ECO:0000244|PDB:1X6D}.
STRAND 1209 1212 {ECO:0000244|PDB:1I16}.
STRAND 1230 1239 {ECO:0000244|PDB:5FB8}.
STRAND 1241 1243 {ECO:0000244|PDB:1I16}.
STRAND 1244 1254 {ECO:0000244|PDB:5FB8}.
STRAND 1257 1266 {ECO:0000244|PDB:5FB8}.
STRAND 1273 1275 {ECO:0000244|PDB:1I16}.
STRAND 1283 1287 {ECO:0000244|PDB:5FB8}.
HELIX 1292 1294 {ECO:0000244|PDB:1I16}.
HELIX 1297 1306 {ECO:0000244|PDB:5FB8}.
STRAND 1309 1319 {ECO:0000244|PDB:5FB8}.
SEQUENCE 1332 AA; 141752 MW; EDF68567B2AF120C CRC64;
MESHSRAGKS RKSAKFRSIS RSLMLCNAKT SDDGSSPDEK YPDPFEISLA QGKEGIFHSS
VQLADTSEAG PSSVPDLALA SEAAQLQAAG NDRGKTCRRI FFMKESSTAS SREKPGKLEA
QSSNFLFPKA CHQRARSNST SVNPYCTREI DFPMTKKSAA PTDRQPYSLC SNRKSLSQQL
DCPAGKAAGT SRPTRSLSTA QLVQPSGGLQ ASVISNIVLM KGQAKGLGFS IVGGKDSIYG
PIGIYVKTIF AGGAAAADGR LQEGDEILEL NGESMAGLTH QDALQKFKQA KKGLLTLTVR
TRLTAPPSLC SHLSPPLCRS LSSSTCITKD SSSFALESPS APISTAKPNY RIMVEVSLQK
EAGVGLGIGL CSVPYFQCIS GIFVHTLSPG SVAHLDGRLR CGDEIVEISD SPVHCLTLNE
VYTILSHCDP GPVPIIVSRH PDPQVSEQQL KEAVAQAVEN TKFGKERHQW SLEGVKRLES
SWHGRPTLEK EREKNSAPPH RRAQKVMIRS SSDSSYMSGS PGGSPGSGSA EKPSSDVDIS
THSPSLPLAR EPVVLSIASS RLPQESPPLP ESRDSHPPLR LKKSFEILVR KPMSSKPKPP
PRKYFKSDSD PQKSLEEREN SSCSSGHTPP TCGQEARELL PLLLPQEDTA GRSPSASAGC
PGPGIGPQTK SSTEGEPGWR RASPVTQTSP IKHPLLKRQA RMDYSFDTTA EDPWVRISDC
IKNLFSPIMS ENHGHMPLQP NASLNEEEGT QGHPDGTPPK LDTANGTPKV YKSADSSTVK
KGPPVAPKPA WFRQSLKGLR NRASDPRGLP DPALSTQPAP ASREHLGSHI RASSSSSSIR
QRISSFETFG SSQLPDKGAQ RLSLQPSSGE AAKPLGKHEE GRFSGLLGRG AAPTLVPQQP
EQVLSSGSPA ASEARDPGVS ESPPPGRQPN QKTLPPGPDP LLRLLSTQAE ESQGPVLKMP
SQRARSFPLT RSQSCETKLL DEKTSKLYSI SSQVSSAVMK SLLCLPSSIS CAQTPCIPKE
GASPTSSSNE DSAANGSAET SALDTGFSLN LSELREYTEG LTEAKEDDDG DHSSLQSGQS
VISLLSSEEL KKLIEEVKVL DEATLKQLDG IHVTILHKEE GAGLGFSLAG GADLENKVIT
VHRVFPNGLA SQEGTIQKGN EVLSINGKSL KGTTHHDALA ILRQAREPRQ AVIVTRKLTP
EAMPDLNSST DSAASASAAS DVSVESTAEA TVCTVTLEKM SAGLGFSLEG GKGSLHGDKP
LTINRIFKGA ASEQSETVQP GDEILQLGGT AMQGLTRFEA WNIIKALPDG PVTIVIRRKS
LQSKETTAAG DS


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