IL16_HUMAN
ID IL16_HUMAN Reviewed; 1332 AA.
AC Q14005; A6NM20; A8MU65; B5TY35; B9EGR6; H3BVH5; Q16435; Q6VVE6; Q6ZMQ7;
AC Q9UP18;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 4.
DT 03-AUG-2022, entry version 203.
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 Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH PPP1R12A;
RP PPP1R12B; PPP1R12C AND GRIN2A.
RX PubMed=12923170; DOI=10.1074/jbc.m306669200;
RA Bannert N., Vollhardt K., Asomuddinov B., Haag M., Koenig H., Norley S.,
RA Kurth R.;
RT "PDZ domain-mediated interaction of interleukin-16 precursor proteins with
RT myosin phosphatase targeting subunits.";
RL J. Biol. Chem. 278:42190-42199(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
RX PubMed=19906316; DOI=10.1186/1471-2164-10-518;
RA Wang P., Yu P., Gao P., Shi T., Ma D.;
RT "Discovery of novel human transcript variants by analysis of intronic
RT single-block EST with polyadenylation site.";
RL BMC Genomics 10:518-518(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC TISSUE=Peripheral blood;
RA Kornfeld H.;
RL Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Cerebellum;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 685-1332.
RX PubMed=9990060; DOI=10.1073/pnas.96.4.1541;
RA Bannert N., Avots A., Baier M., Serfling E., Kurth R.;
RT "GA-binding protein factors, in concert with the coactivator CREB binding
RT protein/p300, control the induction of the interleukin 16 promoter in T
RT lymphocytes.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:1541-1546(1999).
RN [8]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 685-1332, AND VARIANTS GLN-889;
RP LEU-906 AND LYS-1147.
RG SeattleSNPs variation discovery resource;
RL Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 942-1332.
RX PubMed=8609984; DOI=10.1038/381030a0;
RA Bannert N., Baier M., Werner A., Kurth R.;
RT "Interleukin-16 or not?";
RL Nature 381:30-30(1996).
RN [10]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1203-1332, AND SUBUNIT.
RC TISSUE=Peripheral blood;
RX PubMed=7910967; DOI=10.1073/pnas.91.11.5109;
RA Cruikshank W.W., Center D.M., Nisar N., Wu M., Natke B.C., Theodore A.C.,
RA Kornfeld H.;
RT "Molecular and functional analysis of a lymphocyte chemoattractant factor:
RT association of biologic function with CD4 expression.";
RL Proc. Natl. Acad. Sci. U.S.A. 91:5109-5113(1994).
RN [11]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1203-1332.
RA Du Y., Du G.X., Hou L.H., Wang H.T.;
RT "Cloning, expression and purification of human interleukin-16.";
RL Xi Bao Yu Fen Zi Mian Yi Xue Za Zhi 15:25-27(1999).
RN [12]
RP PROTEIN SEQUENCE OF 1212-1220, PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF
RP ASP-1211.
RX PubMed=9422780; DOI=10.1074/jbc.273.2.1144;
RA Zhang Y., Center D.M., Wu D.M., Cruikshank W.W., Yuan J., Andrews D.W.,
RA Kornfeld H.;
RT "Processing and activation of pro-interleukin-16 by caspase-3.";
RL J. Biol. Chem. 273:1144-1149(1998).
RN [13]
RP SUBCELLULAR LOCATION (PRO-INTERLEUKIN-16), AND MUTAGENESIS OF
RP 780-LYS-LYS-781 AND 797-LYS--ARG-802.
RX PubMed=11032842; DOI=10.1074/jbc.m008513200;
RA Zhang Y., Kornfeld H., Cruikshank W.W., Kim S., Reardon C.C., Center D.M.;
RT "Nuclear translocation of the N-terminal prodomain of interleukin-16.";
RL J. Biol. Chem. 276:1299-1303(2001).
RN [14]
RP INDUCTION.
RX PubMed=11276202; DOI=10.1038/86318;
RA Feske S., Giltnane J., Dolmetsch R., Staudt L.M., Rao A.;
RT "Gene regulation mediated by calcium signals in T lymphocytes.";
RL Nat. Immunol. 2:316-324(2001).
RN [15]
RP PHOSPHORYLATION, AND MUTAGENESIS OF SER-743 AND THR-757.
RX PubMed=12450396; DOI=10.1021/bi020163v;
RA Wilson K.C., Cruikshank W.W., Center D.M., Zhang Y.;
RT "Prointerleukin-16 contains a functional CcN motif that regulates nuclear
RT localization.";
RL Biochemistry 41:14306-14312(2002).
RN [16]
RP INTERACTION WITH HTLV-1 TAX (MICROBIAL INFECTION), AND SUBCELLULAR
RP LOCATION.
RX PubMed=12620798; DOI=10.1016/s0042-6822(02)00056-9;
RA Wilson K.C., Center D.M., Cruikshank W.W., Zhang Y.;
RT "Binding of HTLV-1 tax oncoprotein to the precursor of interleukin-16, a T
RT cell PDZ domain-containing protein.";
RL Virology 306:60-67(2003).
RN [17]
RP FUNCTION (PRO-INTERLEUKIN-16), AND SUBCELLULAR LOCATION.
RX PubMed=14734747; DOI=10.4049/jimmunol.172.3.1654;
RA Center D.M., Cruikshank W.W., Zhang Y.;
RT "Nuclear pro-IL-16 regulation of T cell proliferation: p27(KIP1)-dependent
RT G0/G1 arrest mediated by inhibition of Skp2 transcription.";
RL J. Immunol. 172:1654-1660(2004).
RN [18]
RP FUNCTION (PRO-INTERLEUKIN-16), SUBCELLULAR LOCATION (PRO-INTERLEUKIN-16),
RP AND INTERACTION WITH GABPB1 AND HDAC3.
RX PubMed=18097041; DOI=10.4049/jimmunol.180.1.402;
RA Zhang Y., Tuzova M., Xiao Z.X., Cruikshank W.W., Center D.M.;
RT "Pro-IL-16 recruits histone deacetylase 3 to the Skp2 core promoter through
RT interaction with transcription factor GABP.";
RL J. Immunol. 180:402-408(2008).
RN [19]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-922, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP STRUCTURE BY NMR OF 1203-1332.
RX PubMed=9699630; DOI=10.1038/1376;
RA Muehlhahn P., Zweckstetter M., Georgescu J., Ciosto C., Renner C.,
RA Lanzendoerfer M., Lang K., Ambrosius D., Baier M., Kurth R., Holak T.A.;
RT "Structure of interleukin 16 resembles a PDZ domain with an occluded
RT peptide binding site.";
RL Nat. Struct. Biol. 5:682-686(1998).
RN [22]
RP STRUCTURE BY NMR OF 1103-1209.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structures of the PDZ domain of human interleukin-16.";
RL Submitted (NOV-2005) to the PDB data bank.
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.
CC -!- FUNCTION: [Isoform 1]: May act as a scaffolding protein that anchors
CC ion channels in the membrane.
CC -!- FUNCTION: Isoform 3 is involved in cell cycle progression in T-cells.
CC Appears to be involved in transcriptional regulation of SKP2 and is
CC probably part of a transcriptional repression complex on the core
CC promoter of the SKP2 gene. May act as a scaffold for GABPB1 (the DNA-
CC binding subunit the GABP transcription factor complex) and HDAC3 thus
CC maintaining transcriptional repression and blocking cell cycle
CC progression in resting T-cells.
CC -!- SUBUNIT: Homotetramer (Probable). According to PubMed:9699630, the
CC formation of a homotetrameric protein complex is not required for the
CC chemo-attractant function. Isoform 3 interacts (via PDZ 3 domain) with
CC PPP1R12A, PPP1R12B and PPP1R12C. Isoform 1 interacts with PPP1R12B.
CC Isoform 3 interacts with GRIN2A. Isoform 3 interacts with GABPB1.
CC Isoform 3 interacts (via PDZ 3 domain) with HDAC3. Isoform 1 interacts
CC with GRIN2D, KCNJ10, KCNJ15 and CACNA1C (By similarity). {ECO:0000250,
CC ECO:0000269|PubMed:12923170, ECO:0000269|PubMed:18097041,
CC ECO:0000269|PubMed:7910967, ECO:0000305}.
CC -!- SUBUNIT: (Microbial infection) Isoform 3 interacts with HTLV-1 tax.
CC {ECO:0000269|PubMed:12620798}.
CC -!- INTERACTION:
CC Q14005-2; P08133: ANXA6; NbExp=3; IntAct=EBI-17178971, EBI-352541;
CC Q14005-2; Q86V38: ATN1; NbExp=3; IntAct=EBI-17178971, EBI-11954292;
CC Q14005-2; P46379-2: BAG6; NbExp=3; IntAct=EBI-17178971, EBI-10988864;
CC Q14005-2; Q9H2G9: BLZF1; NbExp=3; IntAct=EBI-17178971, EBI-2548012;
CC Q14005-2; A0A087WZT3: BOLA2B; NbExp=3; IntAct=EBI-17178971, EBI-12006120;
CC Q14005-2; Q13137: CALCOCO2; NbExp=3; IntAct=EBI-17178971, EBI-739580;
CC Q14005-2; Q14012: CAMK1; NbExp=3; IntAct=EBI-17178971, EBI-6380130;
CC Q14005-2; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-17178971, EBI-3866279;
CC Q14005-2; Q52MB2: CCDC184; NbExp=3; IntAct=EBI-17178971, EBI-10179526;
CC Q14005-2; Q9P209: CEP72; NbExp=3; IntAct=EBI-17178971, EBI-739498;
CC Q14005-2; Q96A83-2: COL26A1; NbExp=3; IntAct=EBI-17178971, EBI-21553822;
CC Q14005-2; P02489: CRYAA; NbExp=3; IntAct=EBI-17178971, EBI-6875961;
CC Q14005-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-17178971, EBI-3867333;
CC Q14005-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-17178971, EBI-10976677;
CC Q14005-2; Q16829: DUSP7; NbExp=3; IntAct=EBI-17178971, EBI-1265847;
CC Q14005-2; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-17178971, EBI-356015;
CC Q14005-2; O95967: EFEMP2; NbExp=3; IntAct=EBI-17178971, EBI-743414;
CC Q14005-2; P00488: F13A1; NbExp=3; IntAct=EBI-17178971, EBI-2565863;
CC Q14005-2; Q86V42: FAM124A; NbExp=7; IntAct=EBI-17178971, EBI-744506;
CC Q14005-2; Q14192: FHL2; NbExp=3; IntAct=EBI-17178971, EBI-701903;
CC Q14005-2; Q5TD97: FHL5; NbExp=5; IntAct=EBI-17178971, EBI-750641;
CC Q14005-2; Q9C0B1-2: FTO; NbExp=3; IntAct=EBI-17178971, EBI-18138793;
CC Q14005-2; Q06547: GABPB1; NbExp=3; IntAct=EBI-17178971, EBI-618165;
CC Q14005-2; P14136: GFAP; NbExp=3; IntAct=EBI-17178971, EBI-744302;
CC Q14005-2; O14908-2: GIPC1; NbExp=3; IntAct=EBI-17178971, EBI-25913156;
CC Q14005-2; Q08379: GOLGA2; NbExp=3; IntAct=EBI-17178971, EBI-618309;
CC Q14005-2; A6NEM1: GOLGA6L9; NbExp=3; IntAct=EBI-17178971, EBI-5916454;
CC Q14005-2; P28799: GRN; NbExp=3; IntAct=EBI-17178971, EBI-747754;
CC Q14005-2; Q96ED9-2: HOOK2; NbExp=3; IntAct=EBI-17178971, EBI-10961706;
CC Q14005-2; O75031: HSF2BP; NbExp=3; IntAct=EBI-17178971, EBI-7116203;
CC Q14005-2; P04792: HSPB1; NbExp=3; IntAct=EBI-17178971, EBI-352682;
CC Q14005-2; P42858: HTT; NbExp=15; IntAct=EBI-17178971, EBI-466029;
CC Q14005-2; Q96N16: JAKMIP1; NbExp=3; IntAct=EBI-17178971, EBI-2680803;
CC Q14005-2; Q63ZY3: KANK2; NbExp=6; IntAct=EBI-17178971, EBI-2556193;
CC Q14005-2; Q7L273: KCTD9; NbExp=3; IntAct=EBI-17178971, EBI-4397613;
CC Q14005-2; Q96L93-6: KIF16B; NbExp=3; IntAct=EBI-17178971, EBI-10988217;
CC Q14005-2; O60333-2: KIF1B; NbExp=3; IntAct=EBI-17178971, EBI-10975473;
CC Q14005-2; Q9BVG8-5: KIFC3; NbExp=3; IntAct=EBI-17178971, EBI-14069005;
CC Q14005-2; O14901: KLF11; NbExp=3; IntAct=EBI-17178971, EBI-948266;
CC Q14005-2; Q92876: KLK6; NbExp=3; IntAct=EBI-17178971, EBI-2432309;
CC Q14005-2; Q15323: KRT31; NbExp=3; IntAct=EBI-17178971, EBI-948001;
CC Q14005-2; O43790: KRT86; NbExp=3; IntAct=EBI-17178971, EBI-9996498;
CC Q14005-2; Q07627: KRTAP1-1; NbExp=4; IntAct=EBI-17178971, EBI-11959885;
CC Q14005-2; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-17178971, EBI-11749135;
CC Q14005-2; P60410: KRTAP10-8; NbExp=3; IntAct=EBI-17178971, EBI-10171774;
CC Q14005-2; Q9BYR8: KRTAP3-1; NbExp=3; IntAct=EBI-17178971, EBI-9996449;
CC Q14005-2; Q96JM7-2: L3MBTL3; NbExp=3; IntAct=EBI-17178971, EBI-11985629;
CC Q14005-2; Q8TCE9: LGALS14; NbExp=3; IntAct=EBI-17178971, EBI-10274069;
CC Q14005-2; P02545: LMNA; NbExp=3; IntAct=EBI-17178971, EBI-351935;
CC Q14005-2; Q8TAP4-4: LMO3; NbExp=3; IntAct=EBI-17178971, EBI-11742507;
CC Q14005-2; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-17178971, EBI-739832;
CC Q14005-2; Q8WWY6: MBD3L1; NbExp=3; IntAct=EBI-17178971, EBI-12516603;
CC Q14005-2; Q9UJV3-2: MID2; NbExp=6; IntAct=EBI-17178971, EBI-10172526;
CC Q14005-2; Q8N344: MIER2; NbExp=5; IntAct=EBI-17178971, EBI-3504938;
CC Q14005-2; Q5JR59-3: MTUS2; NbExp=3; IntAct=EBI-17178971, EBI-11522433;
CC Q14005-2; P15173: MYOG; NbExp=3; IntAct=EBI-17178971, EBI-3906629;
CC Q14005-2; P07196: NEFL; NbExp=3; IntAct=EBI-17178971, EBI-475646;
CC Q14005-2; Q86UR1-2: NOXA1; NbExp=6; IntAct=EBI-17178971, EBI-12025760;
CC Q14005-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-17178971, EBI-741158;
CC Q14005-2; O43482: OIP5; NbExp=3; IntAct=EBI-17178971, EBI-536879;
CC Q14005-2; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-17178971, EBI-350517;
CC Q14005-2; Q99471: PFDN5; NbExp=3; IntAct=EBI-17178971, EBI-357275;
CC Q14005-2; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-17178971, EBI-79165;
CC Q14005-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-17178971, EBI-25882629;
CC Q14005-2; Q96I34: PPP1R16A; NbExp=3; IntAct=EBI-17178971, EBI-710402;
CC Q14005-2; Q9NQX0: PRDM6; NbExp=3; IntAct=EBI-17178971, EBI-11320284;
CC Q14005-2; P60891: PRPS1; NbExp=3; IntAct=EBI-17178971, EBI-749195;
CC Q14005-2; Q9NZ81: PRR13; NbExp=3; IntAct=EBI-17178971, EBI-740924;
CC Q14005-2; O43586: PSTPIP1; NbExp=3; IntAct=EBI-17178971, EBI-1050964;
CC Q14005-2; Q17RH5: RAPGEF2; NbExp=3; IntAct=EBI-17178971, EBI-12414415;
CC Q14005-2; Q9BYM8: RBCK1; NbExp=3; IntAct=EBI-17178971, EBI-2340624;
CC Q14005-2; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-17178971, EBI-396669;
CC Q14005-2; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-17178971, EBI-748621;
CC Q14005-2; Q12824-2: SMARCB1; NbExp=3; IntAct=EBI-17178971, EBI-358436;
CC Q14005-2; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-17178971, EBI-12288855;
CC Q14005-2; Q7Z699: SPRED1; NbExp=6; IntAct=EBI-17178971, EBI-5235340;
CC Q14005-2; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-17178971, EBI-11139477;
CC Q14005-2; Q9UBB9: TFIP11; NbExp=3; IntAct=EBI-17178971, EBI-1105213;
CC Q14005-2; Q96RU7: TRIB3; NbExp=3; IntAct=EBI-17178971, EBI-492476;
CC Q14005-2; P36406: TRIM23; NbExp=3; IntAct=EBI-17178971, EBI-740098;
CC Q14005-2; P14373: TRIM27; NbExp=3; IntAct=EBI-17178971, EBI-719493;
CC Q14005-2; Q8IWZ5: TRIM42; NbExp=3; IntAct=EBI-17178971, EBI-5235829;
CC Q14005-2; Q5T124-6: UBXN11; NbExp=3; IntAct=EBI-17178971, EBI-11524408;
CC Q14005-2; Q8N6Y0: USHBP1; NbExp=3; IntAct=EBI-17178971, EBI-739895;
CC Q14005-2; O76024: WFS1; NbExp=3; IntAct=EBI-17178971, EBI-720609;
CC Q14005-2; Q9GZV5: WWTR1; NbExp=3; IntAct=EBI-17178971, EBI-747743;
CC Q14005-2; O15060: ZBTB39; NbExp=3; IntAct=EBI-17178971, EBI-9995672;
CC Q14005-2; Q9NZV7: ZIM2; NbExp=3; IntAct=EBI-17178971, EBI-11962760;
CC Q14005-2; P52747: ZNF143; NbExp=3; IntAct=EBI-17178971, EBI-2849334;
CC Q14005-2; P49910: ZNF165; NbExp=3; IntAct=EBI-17178971, EBI-741694;
CC Q14005-2; Q6S9Z5: ZNF474; NbExp=3; IntAct=EBI-17178971, EBI-17269964;
CC Q14005-2; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-17178971, EBI-11035148;
CC Q14005-2; Q7Z3I7: ZNF572; NbExp=3; IntAct=EBI-17178971, EBI-10172590;
CC Q14005-2; Q9P0T4: ZNF581; NbExp=3; IntAct=EBI-17178971, EBI-745520;
CC Q14005-2; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-17178971, EBI-4395669;
CC Q14005-2; Q6NX45: ZNF774; NbExp=3; IntAct=EBI-17178971, EBI-10251462;
CC Q14005-2; Q9ULD5: ZNF777; NbExp=6; IntAct=EBI-17178971, EBI-11975599;
CC Q14005-2; Q9Y2P0: ZNF835; NbExp=3; IntAct=EBI-17178971, EBI-5667516;
CC Q14005-2; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-17178971, EBI-527853;
CC -!- SUBCELLULAR LOCATION: [Interleukin-16]: Secreted.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Cytoplasm. Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=nPro-IL-16;
CC IsoId=Q14005-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14005-2; Sequence=VSP_037459;
CC Name=3; Synonyms=Pro-IL-16;
CC IsoId=Q14005-3; Sequence=VSP_037458;
CC Name=4;
CC IsoId=Q14005-4; Sequence=VSP_037458, VSP_037459, VSP_057192;
CC -!- TISSUE SPECIFICITY: [Isoform 3]: Expressed in hemopoietic tissues, such
CC as resting T-cells, but undetectable during active T-cell
CC proliferation.
CC -!- INDUCTION: [Isoform 3]: Down-regulated in T-cells after TCR activation.
CC {ECO:0000269|PubMed:11276202}.
CC -!- PTM: [Isoform 3]: Synthesized as a chemo-attractant inactive precursor
CC in hemopoietic tissues, and proteolytically cleaved by caspase-3 to
CC yield IL-16. {ECO:0000269|PubMed:9422780}.
CC -!- MISCELLANEOUS: [Isoform 1]: Produced by alternative promoter usage. Is
CC probably proteolytically processed to yield IL-16.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
CC 1. Is probably proteolytically processed to yield IL-16. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage. Is
CC proteolytically processed to yield IL-16. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=SeattleSNPs;
CC URL="http://pga.gs.washington.edu/data/il16/";
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DR EMBL; AY324389; AAQ86961.1; -; mRNA.
DR EMBL; FJ032370; ACI00236.1; -; mRNA.
DR EMBL; M90391; AAD04636.1; -; mRNA.
DR EMBL; AK131530; BAD18668.1; -; mRNA.
DR EMBL; AC036196; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC103858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; KF456108; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC136660; AAI36661.1; -; mRNA.
DR EMBL; AF077011; AAD15990.1; -; Genomic_DNA.
DR EMBL; AY497901; AAR89904.1; -; Genomic_DNA.
DR EMBL; S81601; AAB36371.2; -; mRNA.
DR EMBL; AF053412; AAC12732.1; -; mRNA.
DR CCDS; CCDS10317.1; -. [Q14005-3]
DR CCDS; CCDS42069.1; -. [Q14005-1]
DR CCDS; CCDS53966.1; -. [Q14005-2]
DR PIR; I59298; I59298.
DR RefSeq; NP_001165599.1; NM_001172128.1. [Q14005-2]
DR RefSeq; NP_004504.3; NM_004513.5. [Q14005-3]
DR RefSeq; NP_757366.2; NM_172217.3. [Q14005-1]
DR RefSeq; XP_005254403.1; XM_005254346.4.
DR RefSeq; XP_011519822.1; XM_011521520.2.
DR RefSeq; XP_016877630.1; XM_017022141.1.
DR RefSeq; XP_016877631.1; XM_017022142.1.
DR PDB; 1I16; NMR; -; A=1203-1332.
DR PDB; 1X6D; NMR; -; A=1103-1208.
DR PDB; 5FB8; X-ray; 2.07 A; C=1224-1323.
DR PDBsum; 1I16; -.
DR PDBsum; 1X6D; -.
DR PDBsum; 5FB8; -.
DR AlphaFoldDB; Q14005; -.
DR SMR; Q14005; -.
DR BioGRID; 109816; 110.
DR DIP; DIP-6006N; -.
DR IntAct; Q14005; 110.
DR MINT; Q14005; -.
DR STRING; 9606.ENSP00000302935; -.
DR CarbonylDB; Q14005; -.
DR GlyGen; Q14005; 3 sites, 1 O-linked glycan (3 sites).
DR iPTMnet; Q14005; -.
DR PhosphoSitePlus; Q14005; -.
DR BioMuta; IL16; -.
DR DMDM; 239938922; -.
DR CPTAC; CPTAC-926; -.
DR EPD; Q14005; -.
DR jPOST; Q14005; -.
DR MassIVE; Q14005; -.
DR MaxQB; Q14005; -.
DR PaxDb; Q14005; -.
DR PeptideAtlas; Q14005; -.
DR PRIDE; Q14005; -.
DR ProteomicsDB; 43219; -.
DR ProteomicsDB; 59788; -. [Q14005-1]
DR ProteomicsDB; 59789; -. [Q14005-2]
DR ProteomicsDB; 59790; -. [Q14005-3]
DR ABCD; Q14005; 1 sequenced antibody.
DR Antibodypedia; 3932; 765 antibodies from 46 providers.
DR CPTC; Q14005; 1 antibody.
DR DNASU; 3603; -.
DR Ensembl; ENST00000394652.6; ENSP00000378147.2; ENSG00000172349.18. [Q14005-3]
DR Ensembl; ENST00000394660.6; ENSP00000378155.2; ENSG00000172349.18. [Q14005-2]
DR Ensembl; ENST00000683961.1; ENSP00000508085.1; ENSG00000172349.18. [Q14005-1]
DR GeneID; 3603; -.
DR KEGG; hsa:3603; -.
DR MANE-Select; ENST00000683961.1; ENSP00000508085.1; NM_172217.5; NP_757366.2.
DR UCSC; uc002bgg.4; human. [Q14005-1]
DR CTD; 3603; -.
DR DisGeNET; 3603; -.
DR GeneCards; IL16; -.
DR HGNC; HGNC:5980; IL16.
DR HPA; ENSG00000172349; Tissue enhanced (lymphoid).
DR MIM; 603035; gene.
DR neXtProt; NX_Q14005; -.
DR OpenTargets; ENSG00000172349; -.
DR PharmGKB; PA29793; -.
DR VEuPathDB; HostDB:ENSG00000172349; -.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000156178; -.
DR HOGENOM; CLU_007677_0_0_1; -.
DR InParanoid; Q14005; -.
DR OMA; TCKERPL; -.
DR OrthoDB; 225688at2759; -.
DR PhylomeDB; Q14005; -.
DR TreeFam; TF326303; -.
DR PathwayCommons; Q14005; -.
DR Reactome; R-HSA-449836; Other interleukin signaling.
DR SignaLink; Q14005; -.
DR SIGNOR; Q14005; -.
DR BioGRID-ORCS; 3603; 10 hits in 1079 CRISPR screens.
DR ChiTaRS; IL16; human.
DR EvolutionaryTrace; Q14005; -.
DR GeneWiki; Interleukin_16; -.
DR GenomeRNAi; 3603; -.
DR Pharos; Q14005; Tbio.
DR PRO; PR:Q14005; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q14005; protein.
DR Bgee; ENSG00000172349; Expressed in granulocyte and 135 other tissues.
DR ExpressionAtlas; Q14005; baseline and differential.
DR Genevisible; Q14005; HS.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005576; C:extracellular region; TAS:Reactome.
DR GO; GO:0005615; C:extracellular space; TAS:ProtInc.
DR GO; GO:0090543; C:Flemming body; IDA:HPA.
DR GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042609; F:CD4 receptor binding; IPI:CAFA.
DR GO; GO:0005125; F:cytokine activity; IBA:GO_Central.
DR GO; GO:0019221; P:cytokine-mediated signaling pathway; ISS:ARUK-UCL.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0050930; P:induction of positive chemotaxis; IBA:GO_Central.
DR GO; GO:0030595; P:leukocyte chemotaxis; IBA:GO_Central.
DR GO; GO:0050729; P:positive regulation of inflammatory response; IDA:ARUK-UCL.
DR GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; IDA:ARUK-UCL.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; IDA:ARUK-UCL.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; IDA:ARUK-UCL.
DR GO; GO:1902565; P:positive regulation of neutrophil activation; ISS:ARUK-UCL.
DR GO; GO:0051924; P:regulation of calcium ion transport; IDA:CAFA.
DR Gene3D; 2.30.42.10; -; 4.
DR InterPro; IPR020450; IL-16.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF00595; PDZ; 3.
DR PRINTS; PR01931; INTRLEUKIN16.
DR SMART; SM00228; PDZ; 4.
DR SUPFAM; SSF50156; SSF50156; 4.
DR PROSITE; PS50106; PDZ; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing; Chemotaxis;
KW Cytokine; Cytoplasm; Direct protein sequencing; Host-virus interaction;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Secreted;
KW Transcription; Transcription regulation.
FT CHAIN 1..1332
FT /note="Pro-interleukin-16"
FT /id="PRO_0000377543"
FT CHAIN 1212..1332
FT /note="Interleukin-16"
FT /id="PRO_0000015412"
FT DOMAIN 216..302
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 355..440
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1112..1197
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1234..1319
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 183..452
FT /note="Interaction with GRIN2A"
FT /evidence="ECO:0000269|PubMed:12923170"
FT REGION 481..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 560..706
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 732..970
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1019..1041
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1034..1118
FT /note="Interaction with HTLV-1 tax"
FT REGION 1106..1202
FT /note="Interaction with PPP1R12A, PPP1R12B and PPP1R12C"
FT /evidence="ECO:0000269|PubMed:12923170"
FT COMPBIAS 481..500
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 508..542
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 575..589
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 601..617
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 666..693
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 736..750
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 828..867
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..936
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 922
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT VAR_SEQ 1..701
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:19906316, ECO:0000303|Ref.3"
FT /id="VSP_037458"
FT VAR_SEQ 1228
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:19906316"
FT /id="VSP_037459"
FT VAR_SEQ 1239..1332
FT /note="KMSAGLGFSLEGGKGSLHGDKPLTINRIFKGAASEQSETVQPGDEILQLGGT
FT AMQGLTRFEAWNIIKALPDGPVTIVIRRKSLQSKETTAAGDS -> DVGRAGLQPGRRE
FT GLPTRRQASHH (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:19906316"
FT /id="VSP_057192"
FT VARIANT 434
FT /note="P -> S (in dbSNP:rs4072111)"
FT /id="VAR_058310"
FT VARIANT 889
FT /note="R -> Q (in dbSNP:rs17875512)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_019203"
FT VARIANT 906
FT /note="S -> L (in dbSNP:rs17875513)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_019204"
FT VARIANT 1027
FT /note="S -> T (in dbSNP:rs34101586)"
FT /id="VAR_034013"
FT VARIANT 1147
FT /note="N -> K (in dbSNP:rs11556218)"
FT /evidence="ECO:0000269|Ref.8"
FT /id="VAR_019205"
FT VARIANT 1176
FT /note="H -> R (in dbSNP:rs34159341)"
FT /id="VAR_053372"
FT MUTAGEN 743
FT /note="S->A: Reduces phosphorylation and nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:12450396"
FT MUTAGEN 757
FT /note="T->A: Reduces phosphorylation. Enhances nuclear
FT localization."
FT /evidence="ECO:0000269|PubMed:12450396"
FT MUTAGEN 780..781
FT /note="KK->AA: Reduces nuclear localization of pro-
FT interleukin-16; when associated with 797-AGLANA-802."
FT /evidence="ECO:0000269|PubMed:11032842"
FT MUTAGEN 797..802
FT /note="KGLRNR->AGLANA: Reduces nuclear localization of pro-
FT interleukin-16; when associated with 780-AA-781."
FT /evidence="ECO:0000269|PubMed:11032842"
FT MUTAGEN 1211
FT /note="D->A: Abolishes proteolytic cleavage."
FT /evidence="ECO:0000269|PubMed:9422780"
FT CONFLICT 273
FT /note="E -> G (in Ref. 1; AAQ86961)"
FT /evidence="ECO:0000305"
FT CONFLICT 427
FT /note="H -> R (in Ref. 6; AAI36661)"
FT /evidence="ECO:0000305"
FT CONFLICT 805
FT /note="D -> E (in Ref. 1; AAD04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 934
FT /note="L -> F (in Ref. 1; AAD04636)"
FT /evidence="ECO:0000305"
FT CONFLICT 942..944
FT /note="LRL -> PRE (in Ref. 5)"
FT /evidence="ECO:0000305"
FT CONFLICT 1020
FT /note="E -> A (in Ref. 1; AAD04636)"
FT /evidence="ECO:0000305"
FT STRAND 1111..1117
FT /evidence="ECO:0007829|PDB:1X6D"
FT STRAND 1125..1129
FT /evidence="ECO:0007829|PDB:1X6D"
FT STRAND 1132..1135
FT /evidence="ECO:0007829|PDB:1X6D"
FT STRAND 1140..1144
FT /evidence="ECO:0007829|PDB:1X6D"
FT STRAND 1146..1148
FT /evidence="ECO:0007829|PDB:1X6D"
FT HELIX 1149..1153
FT /evidence="ECO:0007829|PDB:1X6D"
FT HELIX 1175..1184
FT /evidence="ECO:0007829|PDB:1X6D"
FT STRAND 1187..1196
FT /evidence="ECO:0007829|PDB:1X6D"
FT STRAND 1200..1202
FT /evidence="ECO:0007829|PDB:1X6D"
FT STRAND 1209..1212
FT /evidence="ECO:0007829|PDB:1I16"
FT STRAND 1230..1239
FT /evidence="ECO:0007829|PDB:5FB8"
FT STRAND 1241..1243
FT /evidence="ECO:0007829|PDB:1I16"
FT STRAND 1244..1254
FT /evidence="ECO:0007829|PDB:5FB8"
FT STRAND 1257..1266
FT /evidence="ECO:0007829|PDB:5FB8"
FT STRAND 1273..1275
FT /evidence="ECO:0007829|PDB:1I16"
FT STRAND 1283..1287
FT /evidence="ECO:0007829|PDB:5FB8"
FT HELIX 1292..1294
FT /evidence="ECO:0007829|PDB:1I16"
FT HELIX 1297..1306
FT /evidence="ECO:0007829|PDB:5FB8"
FT STRAND 1309..1319
FT /evidence="ECO:0007829|PDB:5FB8"
SQ 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
