ID   TINAG_HUMAN             Reviewed;         476 AA.
AC   Q9UJW2; Q5T467; Q9UJW1; Q9ULZ4;
DT   15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT   11-JAN-2011, sequence version 3.
DT   10-OCT-2018, entry version 148.
DE   RecName: Full=Tubulointerstitial nephritis antigen;
DE            Short=TIN-Ag;
GN   Name=TINAG;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606 {ECO:0000312|EMBL:AAF08931.1};
RN   [1] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND
RP   VARIANT PRO-158.
RC   TISSUE=Kidney {ECO:0000269|PubMed:10652240};
RX   PubMed=10652240; DOI=10.1006/bbrc.2000.2103;
RA   Ikeda M., Takemura T., Hino S., Yoshioka K.;
RT   "Molecular cloning, expression, and chromosomal localization of a
RT   human tubulointerstitial nephritis antigen.";
RL   Biochem. Biophys. Res. Commun. 268:225-230(2000).
RN   [2] {ECO:0000305}
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY,
RP   SUBCELLULAR LOCATION, AND VARIANT PRO-158.
RC   TISSUE=Kidney {ECO:0000269|PubMed:10752525};
RX   PubMed=10752525;
RA   Zhou B., Nelson T.R., Kashtan C., Gleason B., Michael A.F., Vlassi M.,
RA   Charonis A.S.;
RT   "Identification of two alternatively spliced forms of human
RT   tubulointerstitial nephritis antigen (TIN-Ag).";
RL   J. Am. Soc. Nephrol. 11:658-668(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Kidney;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA   Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA   Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA   Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA   Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA   Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA   Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA   Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA   Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA   Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA   Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA   Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA   Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA   Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA   Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA   McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA   Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA   Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA   Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA   Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA   Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA   Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA   Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA   Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA   Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA   Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6] {ECO:0000305}
RP   IDENTIFICATION, AND INVOLVEMENT IN TUBULOINTERSTITIAL NEPHRITIS.
RC   TISSUE=Kidney {ECO:0000269|PubMed:3553704};
RX   PubMed=3553704; DOI=10.1038/ki.1987.69;
RA   Fliger F.D., Wieslander J., Brentjens J.R., Andres G.A.,
RA   Butkowski R.J.;
RT   "Identification of a target antigen in human anti-tubular basement
RT   membrane nephritis.";
RL   Kidney Int. 31:800-807(1987).
RN   [7] {ECO:0000305}
RP   TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX   PubMed=1762287; DOI=10.1038/ki.1991.283;
RA   Butkowski R.J., Kleppel M.M., Katz A., Michael A.F., Fish A.J.;
RT   "Distribution of tubulointerstitial nephritis antigen and evidence for
RT   multiple forms.";
RL   Kidney Int. 40:838-846(1991).
RN   [8] {ECO:0000305}
RP   DISEASE.
RX   PubMed=1466368; DOI=10.1016/0002-9343(92)90205-P;
RA   Katz A., Fish A.J., Santamaria P., Nevins T.E., Kim Y.,
RA   Butkowski R.J.;
RT   "Role of antibodies to tubulointerstitial nephritis antigen in human
RT   anti-tubular basement membrane nephritis associated with membranous
RT   nephropathy.";
RL   Am. J. Med. 93:691-698(1992).
RN   [9] {ECO:0000305}
RP   FUNCTION.
RX   PubMed=8770961; DOI=10.1038/ki.1996.20;
RA   Chen Y., Krishnamurti U., Wayner E.A., Michael A.F., Charonis A.S.;
RT   "Receptors in proximal tubular epithelial cells for tubulointerstitial
RT   nephritis antigen.";
RL   Kidney Int. 49:153-157(1996).
RN   [10] {ECO:0000305}
RP   DEVELOPMENTAL STAGE.
RX   PubMed=9643646; DOI=10.3109/03008209809028899;
RA   Nelson T.R., Kim Y., Michael A.F., Butkowski R.J., Charonis A.S.;
RT   "Tubulointerstitial nephritis antigen (TIN-ag) is expressed in
RT   distinct segments of the developing human nephron.";
RL   Connect. Tissue Res. 37:53-60(1998).
CC   -!- FUNCTION: Mediates adhesion of proximal tubule epithelial cells
CC       via integrins alpha3-beta1 and alphaV-beta3. This is a non
CC       catalytic peptidase C1 family protein.
CC       {ECO:0000269|PubMed:8770961}.
CC   -!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
CC       matrix, basement membrane {ECO:0000269|PubMed:10752525,
CC       ECO:0000269|PubMed:1762287}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1; Synonyms=TIN1 {ECO:0000269|PubMed:10752525};
CC         IsoId=Q9UJW2-1; Sequence=Displayed;
CC         Note=Major isoform.;
CC       Name=2; Synonyms=TIN2 {ECO:0000269|PubMed:10752525};
CC         IsoId=Q9UJW2-2; Sequence=VSP_050567, VSP_050568;
CC   -!- TISSUE SPECIFICITY: Expressed in the kidney cortex, small
CC       intestine and cornea. {ECO:0000269|PubMed:10652240,
CC       ECO:0000269|PubMed:10752525, ECO:0000269|PubMed:1762287}.
CC   -!- DEVELOPMENTAL STAGE: Initially observed in the Bowman capsule
CC       during early glomerular capillary loop formation in the kidney. In
CC       more developmentally mature glomeruli, following transition from
CC       early to mid-capillary loop stage, expression is higher in the
CC       proximal tubular basement membrane than in the distal basement
CC       membrane and Bowman capsule. {ECO:0000269|PubMed:9643646}.
CC   -!- PTM: It has been suggested that the active SMB domain may be
CC       permitted considerable disulfide bond heterogeneity or
CC       variability, thus 2 alternate disulfide patterns based on 3D
CC       structures are described with 1 disulfide bond conserved in both.
CC   -!- MISCELLANEOUS: Antibodies against TINAG are found in sera of
CC       patients with tubulointerstitial nephritis, a rare autoimmune
CC       disorder that causes acute and chronic renal injury.
CC   -!- SIMILARITY: Belongs to the peptidase C1 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU10090}.
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DR   EMBL; AB022277; BAA84949.1; -; mRNA.
DR   EMBL; AF195116; AAF08931.1; -; mRNA.
DR   EMBL; AF195117; AAF08932.1; -; mRNA.
DR   EMBL; AK312918; BAG35763.1; -; mRNA.
DR   EMBL; AL359380; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL589946; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX04437.1; -; Genomic_DNA.
DR   CCDS; CCDS4955.1; -. [Q9UJW2-1]
DR   PIR; JC7189; JC7189.
DR   RefSeq; NP_055279.3; NM_014464.3. [Q9UJW2-1]
DR   UniGene; Hs.127011; -.
DR   ProteinModelPortal; Q9UJW2; -.
DR   SMR; Q9UJW2; -.
DR   BioGrid; 118107; 27.
DR   IntAct; Q9UJW2; 2.
DR   STRING; 9606.ENSP00000259782; -.
DR   MEROPS; C01.973; -.
DR   iPTMnet; Q9UJW2; -.
DR   PhosphoSitePlus; Q9UJW2; -.
DR   BioMuta; TINAG; -.
DR   DMDM; 317373501; -.
DR   EPD; Q9UJW2; -.
DR   PaxDb; Q9UJW2; -.
DR   PeptideAtlas; Q9UJW2; -.
DR   PRIDE; Q9UJW2; -.
DR   ProteomicsDB; 84670; -.
DR   ProteomicsDB; 84671; -. [Q9UJW2-2]
DR   DNASU; 27283; -.
DR   Ensembl; ENST00000259782; ENSP00000259782; ENSG00000137251. [Q9UJW2-1]
DR   GeneID; 27283; -.
DR   KEGG; hsa:27283; -.
DR   UCSC; uc003pcj.3; human. [Q9UJW2-1]
DR   CTD; 27283; -.
DR   DisGeNET; 27283; -.
DR   EuPathDB; HostDB:ENSG00000137251.15; -.
DR   GeneCards; TINAG; -.
DR   H-InvDB; HIX0025004; -.
DR   HGNC; HGNC:14599; TINAG.
DR   HPA; HPA035427; -.
DR   MIM; 606749; gene.
DR   neXtProt; NX_Q9UJW2; -.
DR   OpenTargets; ENSG00000137251; -.
DR   PharmGKB; PA37905; -.
DR   eggNOG; KOG1544; Eukaryota.
DR   eggNOG; ENOG410YN9K; LUCA.
DR   GeneTree; ENSGT00900000140859; -.
DR   HOGENOM; HOG000241342; -.
DR   HOVERGEN; HBG053961; -.
DR   InParanoid; Q9UJW2; -.
DR   OMA; AWWYLRK; -.
DR   OrthoDB; EOG091G0A2N; -.
DR   PhylomeDB; Q9UJW2; -.
DR   TreeFam; TF313765; -.
DR   GeneWiki; TINAG; -.
DR   GenomeRNAi; 27283; -.
DR   PRO; PR:Q9UJW2; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   Bgee; ENSG00000137251; Expressed in 38 organ(s), highest expression level in kidney epithelium.
DR   CleanEx; HS_TINAG; -.
DR   ExpressionAtlas; Q9UJW2; baseline and differential.
DR   Genevisible; Q9UJW2; HS.
DR   GO; GO:0005604; C:basement membrane; IDA:UniProtKB.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004197; F:cysteine-type endopeptidase activity; TAS:ProtInc.
DR   GO; GO:0000166; F:nucleotide binding; TAS:ProtInc.
DR   GO; GO:0030247; F:polysaccharide binding; IEA:InterPro.
DR   GO; GO:0005044; F:scavenger receptor activity; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IDA:UniProtKB.
DR   GO; GO:0006955; P:immune response; IEA:InterPro.
DR   InterPro; IPR038765; Papain_like_cys_pep_sf.
DR   InterPro; IPR025661; Pept_asp_AS.
DR   InterPro; IPR013128; Peptidase_C1A.
DR   InterPro; IPR000668; Peptidase_C1A_C.
DR   InterPro; IPR001212; Somatomedin_B_dom.
DR   InterPro; IPR033164; TINAG.
DR   PANTHER; PTHR12411; PTHR12411; 1.
DR   PANTHER; PTHR12411:SF274; PTHR12411:SF274; 1.
DR   Pfam; PF00112; Peptidase_C1; 1.
DR   Pfam; PF01033; Somatomedin_B; 1.
DR   SMART; SM00645; Pept_C1; 1.
DR   SMART; SM00201; SO; 1.
DR   SUPFAM; SSF54001; SSF54001; 1.
DR   PROSITE; PS00524; SMB_1; 1.
DR   PROSITE; PS50958; SMB_2; 1.
DR   PROSITE; PS00640; THIOL_PROTEASE_ASN; 1.
PE   2: Evidence at transcript level;
KW   Alternative splicing; Basement membrane; Cell adhesion;
KW   Complete proteome; Disulfide bond; Extracellular matrix; Glycoprotein;
KW   Polymorphism; Reference proteome; Secreted.
FT   CHAIN         1    476       Tubulointerstitial nephritis antigen.
FT                                /FTId=PRO_0000050600.
FT   DOMAIN       59    107       SMB. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00350}.
FT   SITE         49     50       Cleavage; by furin. {ECO:0000255}.
FT   CARBOHYD     38     38       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    175    175       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    314    314       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    360    360       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    455    455       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID     63     70       Alternate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00350}.
FT   DISULFID     70    102       Alternate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00350}.
FT   DISULFID     81     95       Alternate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00350}.
FT   DISULFID     81     83       Alternate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00350}.
FT   DISULFID     87     94       {ECO:0000255|PROSITE-ProRule:PRU00350}.
FT   DISULFID     95    102       Alternate. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00350}.
FT   VAR_SEQ     119    169       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10752525}.
FT                                /FTId=VSP_050567.
FT   VAR_SEQ     209    300       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10752525}.
FT                                /FTId=VSP_050568.
FT   VARIANT       3      3       T -> A (in dbSNP:rs16885197).
FT                                /FTId=VAR_047091.
FT   VARIANT      22     22       Q -> R (in dbSNP:rs2297980).
FT                                /FTId=VAR_047092.
FT   VARIANT     158    158       S -> P (in dbSNP:rs1058768).
FT                                {ECO:0000269|PubMed:10652240,
FT                                ECO:0000269|PubMed:10752525}.
FT                                /FTId=VAR_047093.
FT   VARIANT     413    413       V -> I (in dbSNP:rs34011963).
FT                                /FTId=VAR_047094.
FT   VARIANT     433    433       I -> L (in dbSNP:rs3736352).
FT                                /FTId=VAR_047095.
FT   CONFLICT      7      8       IL -> FS (in Ref. 2; AAF08931/AAF08932).
FT                                {ECO:0000305}.
FT   CONFLICT    175    175       N -> I (in Ref. 2; AAF08932).
FT                                {ECO:0000305}.
FT   CONFLICT    199    199       P -> L (in Ref. 1; BAA84949).
FT                                {ECO:0000305}.
FT   CONFLICT    333    333       H -> D (in Ref. 2; AAF08931/AAF08932).
FT                                {ECO:0000305}.
FT   CONFLICT    381    381       R -> H (in Ref. 1; BAA84949).
FT                                {ECO:0000305}.
FT   CONFLICT    421    421       L -> R (in Ref. 2; AAF08932).
FT                                {ECO:0000305}.
FT   CONFLICT    437    437       S -> F (in Ref. 2; AAF08931/AAF08932).
FT                                {ECO:0000305}.
FT   CONFLICT    463    463       I -> V (in Ref. 2; AAF08931/AAF08932).
FT                                {ECO:0000305}.
SQ   SEQUENCE   476 AA;  54605 MW;  6D90C734DAC3A5AE CRC64;
     MWTGYKILIF SYLTTEIWME KQYLSQREVD LEAYFTRNHT VLQGTRFKRA IFQGQYCRNF
     GCCEDRDDGC VTEFYAANAL CYCDKFCDRE NSDCCPDYKS FCREEKEWPP HTQPWYPEGC
     FKDGQHYEEG SVIKENCNSC TCSGQQWKCS QHVCLVRSEL IEQVNKGDYG WTAQNYSQFW
     GMTLEDGFKF RLGTLPPSPM LLSMNEMTAS LPATTDLPEF FVASYKWPGW THGPLDQKNC
     AASWAFSTAS VAADRIAIQS KGRYTANLSP QNLISCCAKN RHGCNSGSID RAWWYLRKRG
     LVSHACYPLF KDQNATNNGC AMASRSDGRG KRHATKPCPN NVEKSNRIYQ CSPPYRVSSN
     ETEIMKEIMQ NGPVQAIMQV REDFFHYKTG IYRHVTSTNK ESEKYRKLQT HAVKLTGWGT
     LRGAQGQKEK FWIAANSWGK SWGENGYFRI LRGVNESDIE KLIIAAWGQL TSSDEP
//