ID   IL16_MOUSE              Reviewed;        1322 AA.
AC   O54824; O70236; Q3TEM4; Q5DTR5; Q8R0G5; Q9QZP6;
DT   27-SEP-2004, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 3.
DT   27-MAR-2024, entry version 178.
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   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY (ISOFORM 2).
RC   STRAIN=NFS; TISSUE=Spleen;
RX   PubMed=9637508;
RA   Keane J., Nicoll J., Kim S., Wu D.M.H., Cruikshank W.W., Brazer W.,
RA   Natke B., Zhang Y., Center D.M., Kornfeld H.;
RT   "Conservation of structure and function between human and murine IL-16.";
RL   J. Immunol. 160:5945-5954(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
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).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION (ISOFORM 1),
RP   TISSUE SPECIFICITY (ISOFORM 1), INTERACTION WITH GRIN2A; GRIN2D; KCNJ10;
RP   KCNJ15 AND CACNA1C, AND PROTEOLYTIC PROCESSING.
RX   PubMed=10479680; DOI=10.1523/jneurosci.19-18-07770.1999;
RA   Kurschner C., Yuzaki M.;
RT   "Neuronal interleukin-16 (NIL-16): a dual function PDZ domain protein.";
RL   J. Neurosci. 19:7770-7780(1999).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   STRAIN=C57BL/6J; TISSUE=Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Fetal brain;
RA   Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA   Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT   complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT   screening of terminal sequences of cDNA clones randomly sampled from size-
RT   fractionated libraries.";
RL   Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   STRAIN=C57BL/6J, and FVB/N; TISSUE=Brain, and Salivary gland;
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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Lung, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
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 ion
CC       channels in the membrane.
CC   -!- FUNCTION: Isoform 2 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). Isoform 2 interacts with GRIN2A.
CC       Isoform 1 interacts with GRIN2D, KCNJ10, KCNJ15 and CACNA1C. Isoform 2
CC       interacts (via PDZ 3 domain) with PPP1R12A, PPP1R12B and PPP1R12C.
CC       Isoform 1 interacts with PPP1R12B. Isoform 3 interacts with GABPB1.
CC       Isoform 2 interacts (via PDZ 3 domain) with HDAC3 (By similarity).
CC       {ECO:0000250, ECO:0000305}.
CC   -!- INTERACTION:
CC       O54824; Q7TS72: Itpkc; NbExp=3; IntAct=EBI-641708, EBI-648015;
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: [Isoform 1]: Cytoplasm
CC       {ECO:0000269|PubMed:10479680}. Note=Colocalizes with GRIN2C in neuronal
CC       cell bodies and neurites.
CC   -!- SUBCELLULAR LOCATION: [Isoform 2]: Cytoplasm. Nucleus {ECO:0000250}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative promoter usage; Named isoforms=2;
CC       Name=1; Synonyms=NIL-16;
CC         IsoId=O54824-1; Sequence=Displayed;
CC       Name=2; Synonyms=Pro-IL-16;
CC         IsoId=O54824-2; Sequence=VSP_037460;
CC   -!- TISSUE SPECIFICITY: Isoform 1 is expressed in neurons of the cerebellum
CC       and hippocampus. Isoform 2 is expressed in thymus, spleen and lung.
CC   -!- PTM: Synthesized as a chemo-attractant inactive precursor which is
CC       proteolytically cleaved by caspase-3 to yield IL-16.
CC       {ECO:0000269|PubMed:10479680}.
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 promoter usage. Is
CC       proteolytically processed to yield IL-16. {ECO:0000305}.
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DR   EMBL; AF006001; AAC04383.1; -; mRNA.
DR   EMBL; AF017111; AAC16039.1; -; mRNA.
DR   EMBL; AF175292; AAD55393.1; -; mRNA.
DR   EMBL; AK038319; BAC29967.1; -; mRNA.
DR   EMBL; AK169551; BAE41224.1; -; mRNA.
DR   EMBL; AK220455; BAD90484.1; -; mRNA.
DR   EMBL; CH466543; EDL06877.1; -; Genomic_DNA.
DR   EMBL; BC026894; AAH26894.1; -; mRNA.
DR   EMBL; BC058709; AAH58709.1; -; mRNA.
DR   CCDS; CCDS21412.1; -. [O54824-1]
DR   CCDS; CCDS90266.1; -. [O54824-2]
DR   RefSeq; NP_034681.2; NM_010551.3. [O54824-1]
DR   RefSeq; XP_006507449.1; XM_006507386.3. [O54824-1]
DR   RefSeq; XP_011239983.1; XM_011241681.2. [O54824-1]
DR   AlphaFoldDB; O54824; -.
DR   SMR; O54824; -.
DR   BioGRID; 200618; 16.
DR   ELM; O54824; -.
DR   IntAct; O54824; 13.
DR   MINT; O54824; -.
DR   STRING; 10090.ENSMUSP00000001792; -.
DR   GlyGen; O54824; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; O54824; -.
DR   PhosphoSitePlus; O54824; -.
DR   EPD; O54824; -.
DR   jPOST; O54824; -.
DR   MaxQB; O54824; -.
DR   PaxDb; 10090-ENSMUSP00000001792; -.
DR   PeptideAtlas; O54824; -.
DR   ProteomicsDB; 267230; -. [O54824-1]
DR   ProteomicsDB; 267231; -. [O54824-2]
DR   Antibodypedia; 3932; 824 antibodies from 46 providers.
DR   DNASU; 16170; -.
DR   Ensembl; ENSMUST00000001792.12; ENSMUSP00000001792.5; ENSMUSG00000001741.13. [O54824-1]
DR   Ensembl; ENSMUST00000145610.8; ENSMUSP00000146496.2; ENSMUSG00000001741.13. [O54824-2]
DR   GeneID; 16170; -.
DR   KEGG; mmu:16170; -.
DR   UCSC; uc009idr.1; mouse. [O54824-2]
DR   UCSC; uc009ids.1; mouse. [O54824-1]
DR   AGR; MGI:1270855; -.
DR   CTD; 3603; -.
DR   MGI; MGI:1270855; Il16.
DR   VEuPathDB; HostDB:ENSMUSG00000001741; -.
DR   eggNOG; KOG3528; Eukaryota.
DR   GeneTree; ENSGT00940000156178; -.
DR   HOGENOM; CLU_007677_0_0_1; -.
DR   InParanoid; O54824; -.
DR   OMA; FFTKEAS; -.
DR   OrthoDB; 3848080at2759; -.
DR   PhylomeDB; O54824; -.
DR   TreeFam; TF326303; -.
DR   Reactome; R-MMU-449836; Other interleukin signaling.
DR   BioGRID-ORCS; 16170; 1 hit in 80 CRISPR screens.
DR   ChiTaRS; Il16; mouse.
DR   PRO; PR:O54824; -.
DR   Proteomes; UP000000589; Chromosome 7.
DR   RNAct; O54824; Protein.
DR   Bgee; ENSMUSG00000001741; Expressed in chordate pharynx and 147 other cell types or tissues.
DR   ExpressionAtlas; O54824; baseline and differential.
DR   GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR   GO; GO:0005829; C:cytosol; ISO:MGI.
DR   GO; GO:0005615; C:extracellular space; IEA:UniProtKB-KW.
DR   GO; GO:0090543; C:Flemming body; ISO:MGI.
DR   GO; GO:0005925; C:focal adhesion; ISO:MGI.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0042609; F:CD4 receptor binding; ISO:MGI.
DR   GO; GO:0005125; F:cytokine activity; IDA:MGI.
DR   GO; GO:0050930; P:induction of positive chemotaxis; IDA:MGI.
DR   GO; GO:0030595; P:leukocyte chemotaxis; IDA:MGI.
DR   GO; GO:0050729; P:positive regulation of inflammatory response; ISO:MGI.
DR   GO; GO:0032730; P:positive regulation of interleukin-1 alpha production; ISO:MGI.
DR   GO; GO:0032735; P:positive regulation of interleukin-12 production; ISO:MGI.
DR   GO; GO:0032755; P:positive regulation of interleukin-6 production; ISO:MGI.
DR   GO; GO:0051924; P:regulation of calcium ion transport; ISO:MGI.
DR   CDD; cd00992; PDZ_signaling; 4.
DR   Gene3D; 2.30.42.10; -; 4.
DR   InterPro; IPR020450; IL-16.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR036034; PDZ_sf.
DR   PANTHER; PTHR48396; PRO-INTERLEUKIN-16; 1.
DR   PANTHER; PTHR48396:SF2; PRO-INTERLEUKIN-16; 1.
DR   Pfam; PF00595; PDZ; 4.
DR   PRINTS; PR01931; INTRLEUKIN16.
DR   SMART; SM00228; PDZ; 4.
DR   SUPFAM; SSF50156; PDZ domain-like; 4.
DR   PROSITE; PS50106; PDZ; 4.
DR   Genevisible; O54824; MM.
PE   1: Evidence at protein level;
KW   Alternative promoter usage; Chemotaxis; Cytokine; Cytoplasm; Nucleus;
KW   Phosphoprotein; Reference proteome; Repeat; Secreted; Transcription;
KW   Transcription regulation.
FT   CHAIN           1..1322
FT                   /note="Pro-interleukin-16"
FT                   /id="PRO_0000377546"
FT   CHAIN           1205..1322
FT                   /note="Interleukin-16"
FT                   /evidence="ECO:0000250"
FT                   /id="PRO_0000015418"
FT   DOMAIN          213..299
FT                   /note="PDZ 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          352..437
FT                   /note="PDZ 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          1105..1190
FT                   /note="PDZ 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   DOMAIN          1226..1309
FT                   /note="PDZ 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT   REGION          104..147
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          183..449
FT                   /note="Interaction with GRIN2A"
FT                   /evidence="ECO:0000250"
FT   REGION          480..633
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          651..695
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          729..963
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1099..1195
FT                   /note="Interaction with PPP1R12A, PPP1R12B and PPP1R12C"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        104..146
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        480..497
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        505..519
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        531..545
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        568..588
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        600..623
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        660..682
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        729..745
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        825..868
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        887..908
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        935..949
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         917
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q14005"
FT   VAR_SEQ         1..698
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334,
FT                   ECO:0000303|PubMed:16141072, ECO:0000303|PubMed:9510557,
FT                   ECO:0000303|PubMed:9637508"
FT                   /id="VSP_037460"
FT   CONFLICT        264
FT                   /note="I -> S (in Ref. 5; BAD90484)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        733
FT                   /note="T -> R (in Ref. 1; AAC04383)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        921
FT                   /note="G -> S (in Ref. 2; AAC16039)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1067
FT                   /note="S -> P (in Ref. 2; AAC16039)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1224
FT                   /note="V -> A (in Ref. 2; AAC16039)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1262..1264
FT                   /note="TEQ -> DRT (in Ref. 1; AAC04383)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1322 AA;  141435 MW;  DDB94003A5DCB738 CRC64;
     MEPHGHSGKS RKSTKFRSIS RSLILCNAKT SDDGSSPDEK YPDPFETSLC QGKEGFFHSS
     MQLADTFEAG LSNIPDLALA SDSAQLAAAG SDRGKHCRKM FFMKESSSTS SKEKSGKPEA
     QSSSFLFPKA CHQRTRSNST SVNPYSAGEI DFPMTKKSAA PTDRQPYSLC SNRKSLSQQL
     DYPILGTARP TRSLSTAQLG QLSGGLQASV ISNIVLMKGQ AKGLGFSIVG GKDSIYGPIG
     IYVKSIFAGG AAAADGRLQE GDEILELNGE SMAGLTHQDA LQKFKQAKKG LLTLTVRTRL
     TTPPSLCSHL SPPLCRSLSS STCGAQDSSP FSLESPASPA STAKPNYRIM VEVSLKKEAG
     VGLGIGLCSI PYFQCISGIF VHTLSPGSVA HLDGRLRCGD EIVEINDSPV HCLTLNEVYT
     ILSHCDPGPV PIIVSRHPDP QVSEQQLKEA VAQAVEGVKF GKDRHQWSLE GVKRLESSWH
     GRPTLEKERE KHSAPPHRRA QKIMVRSSSD SSYMSGSPGG SPCSAGAEPQ PSEREGSTHS
     PSLSPGEEQE PCPGVPSRPQ QESPPLPESL ERESHPPLRL KKSFEILVRK PTSSKPKPPP
     RKYFKNDSEP QKKLEEKEKV TDPSGHTLPT CSQETRELLP LLLQEDTAGR APCTAACCPG
     PAASTQTSSS TEGESRRSAS PETPASPGKH PLLKRQARMD YSFDITAEDP WVRISDCIKN
     LFSPIMSENH SHTPLQPNTS LGEEDGTQGC PEGGLSKMDA ANGAPRVYKS ADGSTVKKGP
     PVAPKPAWFR QSLKGLRNRA PDPRRPPEVA SAIQPTPVSR DPPGPQPQAS SSIRQRISSF
     ENFGSSQLPD RGVQRLSLQP SSGETTKFPG KQDGGRFSGL LGQGATVTAK HRQTEVESMS
     TTFPNSSEVR DPGLPESPPP GQRPSTKALS PDPLLRLLTT QSEDTQGPGL KMPSQRARSF
     PLTRTQSCET KLLDEKASKL YSISSQLSSA VMKSLLCLPS SVSCGQITCI PKERVSPKSP
     CNNSSAAEGF GEAMASDTGF SLNLSELREY SEGLTEPGET EDRNHCSSQA GQSVISLLSA
     EELEKLIEEV RVLDEATLKQ LDSIHVTILH KEEGAGLGFS LAGGADLENK VITVHRVFPN
     GLASQEGTIQ KGNEVLSING KSLKGATHND ALAILRQARD PRQAVIVTRR TTVEATHDLN
     SSTDSAASAS AASDISVESK EATVCTVTLE KTSAGLGFSL EGGKGSLHGD KPLTINRIFK
     GTEQGEMVQP GDEILQLAGT AVQGLTRFEA WNVIKALPDG PVTIVIRRTS LQCKQTTASA
     DS
//