ID Q31135_MOUSE Unreviewed; 263 AA. AC Q31135; DT 01-NOV-1996, integrated into UniProtKB/TrEMBL. DT 01-NOV-1996, sequence version 1. DT 27-MAR-2024, entry version 205. DE SubName: Full=H2-Ab1 protein {ECO:0000313|EMBL:AAH08168.1}; DE Flags: Precursor; GN Name=H2-Ab1 {ECO:0000313|MGI:MGI:103070}; 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 {ECO:0000313|EMBL:AAA39547.1}; RN [1] {ECO:0000313|EMBL:AAA39547.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=2882518; DOI=10.1073/pnas.84.8.2435; RA Acha-Orbea H., McDevitt H.O.; RT "The first external domain of the nonobese diabetic mouse class II I-A beta RT chain is unique."; RL Proc. Natl. Acad. Sci. U.S.A. 84:2435-2439(1987). RN [2] {ECO:0000313|EMBL:BAE33331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE33331.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE33890.1}; RX PubMed=10349636; DOI=10.1016/S0076-6879(99)03004-9; RA Carninci P., Hayashizaki Y.; RT "High-efficiency full-length cDNA cloning."; RL Methods Enzymol. 303:19-44(1999). RN [3] {ECO:0000313|EMBL:BAE33331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE33331.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE33890.1}; RX PubMed=11042159; DOI=10.1101/gr.145100; RA Carninci P., Shibata Y., Hayatsu N., Sugahara Y., Shibata K., Itoh M., RA Konno H., Okazaki Y., Muramatsu M., Hayashizaki Y.; RT "Normalization and subtraction of cap-trapper-selected cDNAs to prepare RT full-length cDNA libraries for rapid discovery of new genes."; RL Genome Res. 10:1617-1630(2000). RN [4] {ECO:0000313|EMBL:BAE33331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE33331.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE33890.1}; RX PubMed=11076861; DOI=10.1101/gr.152600; RA Shibata K., Itoh M., Aizawa K., Nagaoka S., Sasaki N., Carninci P., RA Konno H., Akiyama J., Nishi K., Kitsunai T., Tashiro H., Itoh M., Sumi N., RA Ishii Y., Nakamura S., Hazama M., Nishine T., Harada A., Yamamoto R., RA Matsumoto H., Sakaguchi S., Ikegami T., Kashiwagi K., Fujiwake S., RA Inoue K., Togawa Y., Izawa M., Ohara E., Watahiki M., Yoneda Y., RA Ishikawa T., Ozawa K., Tanaka T., Matsuura S., Kawai J., Okazaki Y., RA Muramatsu M., Inoue Y., Kira A., Hayashizaki Y.; RT "RIKEN integrated sequence analysis (RISA) system--384-format sequencing RT pipeline with 384 multicapillary sequencer."; RL Genome Res. 10:1757-1771(2000). RN [5] {ECO:0007829|PDB:1F3J} RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 31-217, GLYCOSYLATION AT ASN-46, RP AND DISULFIDE BONDS. RX PubMed=10894169; DOI=10.1016/S1074-7613(00)80220-4; RA Latek R.R., Suri A., Petzold S.J., Nelson C.A., Kanagawa O., Unanue E.R., RA Fremont D.H.; RT "Structural basis of peptide binding and presentation by the type I RT diabetes-associated MHC class II molecule of NOD mice."; RL Immunity 12:699-710(2000). RN [6] {ECO:0007829|PDB:1ES0} RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 24-25 AND 30-214, AND DISULFIDE RP BONDS. RX PubMed=10775108; DOI=10.1126/science.288.5465.505; RA Corper A.L., Stratmann T., Apostolopoulos V., Scott C.A., Garcia K.C., RA Kang A.S., Wilson I.A., Teyton L.; RT "A structural framework for deciphering the link between I-Ag7 and RT autoimmune diabetes."; RL Science 288:505-511(2000). RN [7] {ECO:0000313|EMBL:BAE33331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE33331.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE33890.1}; RX PubMed=11217851; DOI=10.1038/35055500; RG The RIKEN Genome Exploration Research Group Phase II Team and the FANTOM Consortium; RT "Functional annotation of a full-length mouse cDNA collection."; RL Nature 409:685-690(2001). RN [8] {ECO:0000313|EMBL:BAE33331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE33331.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE33890.1}; RX PubMed=12466851; DOI=10.1038/nature01266; RG The FANTOM Consortium and the RIKEN Genome Exploration Research Group Phase I and II Team; RT "Analysis of the mouse transcriptome based on functional annotation of RT 60,770 full-length cDNAs."; RL Nature 420:563-573(2002). RN [9] {ECO:0000313|EMBL:AAH08168.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NMRI {ECO:0000313|EMBL:AAH08168.1}; RC TISSUE=Mammary tumor. WAP-Tag model. 5 months old RC {ECO:0000313|EMBL:AAH08168.1}; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RA Gerhard D.S., Wagner L., Feingold E.A., Shenmen C.M., Grouse L.H., RA Schuler G., Klein S.L., Old S., Rasooly R., Good P., Guyer M., Peck A.M., RA Derge J.G., Lipman D., Collins F.S., Jang W., Sherry S., Feolo M., RA Misquitta L., Lee E., Rotmistrovsky K., Greenhut S.F., Schaefer C.F., RA Buetow K., Bonner T.I., Haussler D., Kent J., Kiekhaus M., Furey T., RA Brent M., Prange C., Schreiber K., Shapiro N., Bhat N.K., Hopkins R.F., RA Hsie F., Driscoll T., Soares M.B., Casavant T.L., Scheetz T.E., RA Brown-stein M.J., Usdin T.B., Toshiyuki S., Carninci P., Piao Y., RA Dudekula D.B., Ko M.S., Kawakami K., Suzuki Y., Sugano S., Gruber C.E., RA Smith M.R., Simmons B., Moore T., Waterman R., Johnson S.L., Ruan Y., RA Wei C.L., Mathavan S., Gunaratne P.H., Wu J., Garcia A.M., Hulyk S.W., RA Fuh E., Yuan Y., Sneed A., Kowis C., Hodgson A., Muzny D.M., McPherson J., RA Gibbs R.A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., RA Sanchez A., Whiting M., Madari A., Young A.C., Wetherby K.D., Granite S.J., RA Kwong P.N., Brinkley C.P., Pearson R.L., Bouffard G.G., Blakesly R.W., RA Green E.D., Dickson M.C., Rodriguez A.C., Grimwood J., Schmutz J., RA Myers R.M., Butterfield Y.S., Griffith M., Griffith O.L., Krzywinski M.I., RA Liao N., Morin R., Morrin R., Palmquist D., Petrescu A.S., Skalska U., RA Smailus D.E., Stott J.M., Schnerch A., Schein J.E., Jones S.J., Holt R.A., RA Baross A., Marra M.A., Clifton S., Makowski K.A., Bosak S., Malek J.; 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 [10] {ECO:0000313|EMBL:BAE33331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE33331.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE33890.1}; RA Chen C.-T., Hsu E.; RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases. RN [11] {ECO:0000313|EMBL:BAE42176.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE42176.1}; RA Gurgel C.F., Fujii M.T., Guimaraes S.M.P.B., Fredericq S.; RL Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases. RN [12] {ECO:0000313|EMBL:BAE33331.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=NOD {ECO:0000313|EMBL:BAE33331.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE33890.1}; 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 [13] {ECO:0000313|EMBL:BAE33331.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=NOD {ECO:0000313|EMBL:BAE33331.1}; RC TISSUE=Activated spleen {ECO:0000313|EMBL:BAE33890.1}; RX PubMed=16141073; DOI=10.1126/science.1112009; RG RIKEN Genome Exploration Research Group and Genome Science Group (Genome Network Project Core Group) and the FANTOM Consortium; RT "Antisense Transcription in the Mammalian Transcriptome."; RL Science 309:1564-1566(2005). RN [14] {ECO:0007829|PDB:3CUP} RP X-RAY CRYSTALLOGRAPHY (3.09 ANGSTROMS) OF 28-214, AND DISULFIDE BONDS. RA Yoshida K., Corper A.L., Puckett C., Sim J., Valerie M.-D., Jabri B., RA Wilson I.A., Teyton L.; RT "Crystal structure of the MHC class II molecule I-Ag7 in complex with the RT peptide GAD221-235."; RL Submitted (APR-2008) to the PDB data bank. RN [15] {ECO:0007829|PDB:3MBE} RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 28-214, AND DISULFIDE BONDS. RX PubMed=20407212; DOI=10.1172/JCI41502; RA Yoshida K., Corper A.L., Herro R., Jabri B., Wilson I.A., Teyton L.; RT "The diabetogenic mouse MHC class II molecule I-Ag7 is endowed with a RT switch that modulates TCR affinity."; RL J. Clin. Invest. 120:1578-1590(2010). RN [16] {ECO:0007829|PDB:5DMK} RP X-RAY CRYSTALLOGRAPHY (2.45 ANGSTROMS) OF 31-215, AND DISULFIDE BONDS. RX PubMed=26453556; DOI=10.1073/pnas.1517862112; RA Jin N., Wang Y., Crawford F., White J., Marrack P., Dai S., Kappler J.W.; RT "N-terminal additions to the WE14 peptide of chromogranin A create strong RT autoantigen agonists in type 1 diabetes."; RL Proc. Natl. Acad. Sci. U.S.A. 112:13318-13323(2015). RN [17] {ECO:0007829|PDB:6BLQ, ECO:0007829|PDB:6BLR} RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) OF 21-217, AND DISULFIDE BONDS. RX PubMed=29255035; DOI=10.1073/pnas.1716527115; RA Wang Y., Sosinowski T., Novikov A., Crawford F., Neau D.B., Yang J., RA Kwok W.W., Marrack P., Kappler J.W., Dai S.; RT "C-terminal modification of the insulin B:11-23 peptide creates RT superagonists in mouse and human type 1 diabetes."; RL Proc. Natl. Acad. Sci. U.S.A. 115:162-167(2018). RN [18] {ECO:0007829|PDB:6DFS, ECO:0007829|PDB:6DFW} RP X-RAY CRYSTALLOGRAPHY (3.10 ANGSTROMS) OF 21-217, AND DISULFIDE BONDS. RX PubMed=30952805; DOI=10.1126/sciimmunol.aav7517; RA Wang Y., Sosinowski T., Novikov A., Crawford F., White J., Jin N., Liu Z., RA Zou J., Neau D., Davidson H.W., Nakayama M., Kwok W.W., Gapin L., RA Marrack P., Kappler J.W., Dai S.; RT "How C-terminal additions to insulin B-chain fragments create superagonists RT for T cells in mouse and human type 1 diabetes."; RL Sci. Immunol. 4:eaav7517-eaav7517(2019). RN [19] {ECO:0007829|PDB:7QHP, ECO:0007829|PDB:7Z50} RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 28-224, AND DISULFIDE BONDS. RX PubMed=35967292; DOI=10.3389/fimmu.2022.924311; RA Erausquin E., Serra P., Parras D., Santamaria P., Lopez-Sagaseta J.; RT "Structural plasticity in I-Ag7 links autoreactivity to hybrid RT insulin peptides in type I diabetes."; RL Front. Immunol. 13:924311-924311(2022). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single- CC pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}. CC -!- SIMILARITY: Belongs to the MHC class II family. CC {ECO:0000256|ARBA:ARBA00007394}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; M15848; AAA39547.1; -; mRNA. DR EMBL; BC008168; AAH08168.1; -; mRNA. DR EMBL; AK155573; BAE33331.1; -; mRNA. DR EMBL; AK156899; BAE33890.1; -; mRNA. DR EMBL; AK171005; BAE42176.1; -; mRNA. DR EMBL; AK171211; BAE42316.1; -; mRNA. DR EMBL; AK171281; BAE42364.1; -; mRNA. DR PIR; A25911; A25911. DR PIR; A27595; A27595. DR PDB; 1ES0; X-ray; 2.60 A; B=24-25, B=30-214. DR PDB; 1F3J; X-ray; 3.10 A; B/E=31-217. DR PDB; 3CUP; X-ray; 3.09 A; B=20-20, B=28-214. DR PDB; 3MBE; X-ray; 2.89 A; B/F=28-214. DR PDB; 5DMK; X-ray; 2.45 A; B/D/F/H=31-215. DR PDB; 6BLQ; X-ray; 1.80 A; B=21-217. DR PDB; 6BLR; X-ray; 1.96 A; B=21-217. DR PDB; 6BLX; X-ray; 2.32 A; B=21-217. DR PDB; 6DFS; X-ray; 3.10 A; D=21-217. DR PDB; 6DFW; X-ray; 3.20 A; B/D=21-217. DR PDB; 7QHP; X-ray; 1.82 A; B=21-226. DR PDB; 7Z50; X-ray; 2.65 A; B/D=28-224. DR PDBsum; 1ES0; -. DR PDBsum; 1F3J; -. DR PDBsum; 3CUP; -. DR PDBsum; 3MBE; -. DR PDBsum; 5DMK; -. DR PDBsum; 6BLQ; -. DR PDBsum; 6BLR; -. DR PDBsum; 6BLX; -. DR PDBsum; 6DFS; -. DR PDBsum; 6DFW; -. DR IntAct; Q31135; 1. DR AGR; MGI:103070; -. DR MGI; MGI:103070; H2-Ab1. DR ChiTaRS; H2-Ab1; mouse. DR GO; GO:0009986; C:cell surface; IEA:UniProt. DR GO; GO:0005769; C:early endosome; IEA:UniProt. DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProt. DR GO; GO:0042613; C:MHC class II protein complex; IEA:UniProtKB-KW. DR GO; GO:0005771; C:multivesicular body; IEA:UniProt. DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW. DR GO; GO:0019886; P:antigen processing and presentation of exogenous peptide antigen via MHC class II; IEA:UniProt. DR CDD; cd21001; IgC1_MHC_II_beta_HLA-DQ_I-A; 1. DR Gene3D; 2.60.40.10; Immunoglobulins; 1. DR InterPro; IPR007110; Ig-like_dom. DR InterPro; IPR036179; Ig-like_dom_sf. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR003006; Ig/MHC_CS. DR InterPro; IPR003597; Ig_C1-set. DR InterPro; IPR011162; MHC_I/II-like_Ag-recog. DR InterPro; IPR014745; MHC_II_a/b_N. DR InterPro; IPR000353; MHC_II_b_N. DR PANTHER; PTHR19944:SF101; HLA CLASS II HISTOCOMPATIBILITY ANTIGEN, DQ BETA 1 CHAIN; 1. DR PANTHER; PTHR19944; MHC CLASS II-RELATED; 1. DR Pfam; PF07654; C1-set; 1. DR Pfam; PF00969; MHC_II_beta; 1. DR SMART; SM00407; IGc1; 1. DR SMART; SM00921; MHC_II_beta; 1. DR SUPFAM; SSF48726; Immunoglobulin; 1. DR SUPFAM; SSF54452; MHC antigen-recognition domain; 1. DR PROSITE; PS50835; IG_LIKE; 1. DR PROSITE; PS00290; IG_MHC; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0007829|PDB:1ES0, ECO:0007829|PDB:1F3J}; KW Adaptive immunity {ECO:0000256|ARBA:ARBA00023130}; KW Glycoprotein {ECO:0000256|ARBA:ARBA00023180}; KW Immunity {ECO:0000256|ARBA:ARBA00022859}; KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius}; KW MHC II {ECO:0000256|ARBA:ARBA00023182}; Signal {ECO:0000256|SAM:SignalP}; KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, KW ECO:0000256|SAM:Phobius}. FT SIGNAL 1..27 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 28..263 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5015097376" FT TRANSMEM 225..245 FT /note="Helical" FT /evidence="ECO:0000256|SAM:Phobius" FT DOMAIN 123..211 FT /note="Ig-like" FT /evidence="ECO:0000259|PROSITE:PS50835" FT CARBOHYD 46 FT /note="N-acetyl-D-glucosamine 1" FT /evidence="ECO:0007829|PDB:7Z50" FT CARBOHYD 46 FT /note="N-acetyl-D-glucosamine 2" FT /evidence="ECO:0007829|PDB:1F3J, ECO:0007829|PDB:6BLQ" FT CARBOHYD 46 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0007829|PDB:1F3J, ECO:0007829|PDB:6BLQ" FT CARBOHYD 49 FT /note="N-acetyl-D-glucosamine 2" FT /evidence="ECO:0007829|PDB:1F3J, ECO:0007829|PDB:6BLQ" FT DISULFID 42..104 FT /evidence="ECO:0007829|PDB:1ES0, ECO:0007829|PDB:1F3J" FT DISULFID 143..199 FT /evidence="ECO:0007829|PDB:1ES0, ECO:0007829|PDB:1F3J" SQ SEQUENCE 263 AA; 29828 MW; BF790988F79547E5 CRC64; MALQIPSLLL SAAVVVLMVL SSPGTEGGDS ERHFVHQFKG ECYFTNGTQR IRLVTRYIYN REEYLRFDSD VGEYRAVTEL GRHSAEYYNK QYLERTRAEL DTACRHNYEE TEVPTSLRRL EQPNVAISLS RTEALNHHNT LVCSVTDFYP AKIKVRWFRN GQEETVGVSS TQLIRNGDWT FQVLVMLEMT PHQGEVYTCH VEHPSLKSPI TVEWRAQSES ARSKMLSGIG GCVLGVIFLG LGLFIRHRSQ KGPRGPPPAG LLQ //