MGT4B_MOUSE
ID MGT4B_MOUSE Reviewed; 548 AA.
AC Q812F8; Q3U2D9; Q812F9; Q8R0L4;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Alpha-1,3-mannosyl-glycoprotein 4-beta-N-acetylglucosaminyltransferase B {ECO:0000305};
DE EC=2.4.1.145 {ECO:0000250|UniProtKB:Q9UQ53};
DE AltName: Full=N-glycosyl-oligosaccharide-glycoprotein N-acetylglucosaminyltransferase IVb;
DE Short=GlcNAc-T IVb;
DE Short=GnT-IVb;
DE Short=N-acetylglucosaminyltransferase IVb;
DE AltName: Full=UDP-N-acetylglucosamine: alpha-1,3-D-mannoside beta-1,4-N-acetylglucosaminyltransferase IVb;
GN Name=Mgat4b {ECO:0000312|MGI:MGI:2143974};
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 [GENOMIC DNA / MRNA].
RC STRAIN=129/SvJ;
RX PubMed=10372966; DOI=10.1023/a:1006951519522;
RA Yoshida A., Minowa M.T., Takamatsu S., Hara T., Ikenaga H., Takeuchi M.;
RT "A novel second isoenzyme of the human UDP-N-acetylglucosamine:alpha1,3-D-
RT mannoside beta1,4-N-acetylglucosaminyltransferase family: cDNA cloning,
RT expression, and chromosomal assignment.";
RL Glycoconj. J. 15:1115-1123(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-495.
RC STRAIN=NOD;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 208-548.
RC STRAIN=FVB/N; TISSUE=Colon;
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).
CC -!- FUNCTION: Glycosyltransferase that catalyze the transfer of GlcNAc from
CC UDP-GlcNAc to the GlcNAcbeta1-2Manalpha1-3 arm of the core structure of
CC N-linked glycans through a beta1-4 linkage and participates in the
CC production of tri- and tetra-antennary N-linked sugar chains. Prefers
CC complex-type N-glycans over hybrid-types. Has lower affinities for
CC donors or acceptors than MGAT4A, suggesting that, under physiological
CC conditions, it is not the main contributor in N-glycan biosynthesis.
CC {ECO:0000250|UniProtKB:Q9UQ53}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-
CC glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-
CC (1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-
CC beta-D-Man-(1->4)-beta-D-GlcNAcl-(1->4)-beta-D-GlcNAc}-L-asparaginyl-
CC [protein] + UDP; Xref=Rhea:RHEA:16057, Rhea:RHEA-COMP:13526,
CC Rhea:RHEA-COMP:14374, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:60651, ChEBI:CHEBI:139507;
CC EC=2.4.1.145; Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16058;
CC Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-L-
CC asparaginyl-[protein] + UDP-N-acetyl-alpha-D-glucosamine = H(+) +
CC N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-
CC [alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-beta-D-
CC GlcNAc}-L-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69615,
CC Rhea:RHEA-COMP:14369, Rhea:RHEA-COMP:17732, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:60615,
CC ChEBI:CHEBI:187873; Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69616;
CC Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[beta-D-GlcNAc-
CC (1->2)-{beta-D-GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-GlcNAc-(1->2)-{beta-D-
CC GlcNAc-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69619, Rhea:RHEA-COMP:17733, Rhea:RHEA-COMP:17734,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187874, ChEBI:CHEBI:187875;
CC Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69620;
CC Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-[alpha-D-Fuc-(1->6)]-
CC beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-acetyl-alpha-D-
CC glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-D-GlcNAc-
CC (1->4)]-alpha-D-Man-(1->3)-[alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-[alpha-D-Fuc-(1->6)]-beta-D-GlcNAc}-asparaginyl-
CC [protein] + UDP; Xref=Rhea:RHEA:69623, Rhea:RHEA-COMP:17735,
CC Rhea:RHEA-COMP:17736, ChEBI:CHEBI:15378, ChEBI:CHEBI:57705,
CC ChEBI:CHEBI:58223, ChEBI:CHEBI:187876, ChEBI:CHEBI:187877;
CC Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69624;
CC Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-Gal-(1->4)-beta-D-GlcNAc-(1->2)-alpha-D-Man-
CC (1->3)-[beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-Gal-(1->4)-beta-D-
CC GlcNAc-(1->2)-[beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[beta-D-
CC GlcNAc-(1->2)-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-
CC (1->4)-beta-D-GlcNAc}-L-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69627, Rhea:RHEA-COMP:17737, Rhea:RHEA-COMP:17738,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187878, ChEBI:CHEBI:187879;
CC Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69628;
CC Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-[alpha-D-Man-
CC (1->3)-{alpha-D-Man-(1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-
CC beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP-N-
CC acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-[beta-
CC D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-[alpha-D-Man-(1->3)-{alpha-D-Man-
CC (1->6)}-alpha-D-Man-(1->6)]-beta-D-Man-(1->4)-beta-D-GlcNAc-(1->4)-
CC beta-D-GlcNAc}-asparaginyl-[protein] + UDP; Xref=Rhea:RHEA:69631,
CC Rhea:RHEA-COMP:17739, Rhea:RHEA-COMP:17740, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57705, ChEBI:CHEBI:58223, ChEBI:CHEBI:187880,
CC ChEBI:CHEBI:187881; Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69632;
CC Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(4)-{beta-D-GlcNAc-(1->2)-alpha-D-Man-(1->3)-beta-D-Man-
CC (1->4)-beta-D-GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] +
CC UDP-N-acetyl-alpha-D-glucosamine = H(+) + N(4)-{beta-D-GlcNAc-(1->2)-
CC [beta-D-GlcNAc-(1->4)]-alpha-D-Man-(1->3)-beta-D-Man-(1->4)-beta-D-
CC GlcNAc-(1->4)-beta-D-GlcNAc}-asparaginyl-[protein] + UDP;
CC Xref=Rhea:RHEA:69635, Rhea:RHEA-COMP:17741, Rhea:RHEA-COMP:17742,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:57705, ChEBI:CHEBI:58223,
CC ChEBI:CHEBI:187882, ChEBI:CHEBI:187883;
CC Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:69636;
CC Evidence={ECO:0000250|UniProtKB:Q9UQ53};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000250|UniProtKB:O77836};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000250|UniProtKB:Q9UQ53}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000250|UniProtKB:Q9D4R2}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q9D4R2}. Note=A processed soluble form also
CC exists. {ECO:0000250|UniProtKB:Q9UQ53}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q9UQ53}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 54 family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH26638.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH31613.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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; AB053218; BAC55019.1; -; mRNA.
DR EMBL; AB053219; BAC55020.1; -; Genomic_DNA.
DR EMBL; AL627187; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK155336; BAE33202.1; -; mRNA.
DR EMBL; BC026638; AAH26638.1; ALT_INIT; mRNA.
DR EMBL; BC031613; AAH31613.1; ALT_INIT; mRNA.
DR CCDS; CCDS24630.1; -.
DR RefSeq; NP_666038.3; NM_145926.3.
DR AlphaFoldDB; Q812F8; -.
DR SMR; Q812F8; -.
DR BioGRID; 222108; 1.
DR STRING; 10090.ENSMUSP00000043346; -.
DR CAZy; GT54; Glycosyltransferase Family 54.
DR GlyGen; Q812F8; 2 sites.
DR iPTMnet; Q812F8; -.
DR PhosphoSitePlus; Q812F8; -.
DR MaxQB; Q812F8; -.
DR PaxDb; Q812F8; -.
DR PeptideAtlas; Q812F8; -.
DR PRIDE; Q812F8; -.
DR ProteomicsDB; 295900; -.
DR Antibodypedia; 29519; 80 antibodies from 17 providers.
DR DNASU; 103534; -.
DR Ensembl; ENSMUST00000041725; ENSMUSP00000043346; ENSMUSG00000036620.
DR GeneID; 103534; -.
DR KEGG; mmu:103534; -.
DR UCSC; uc007iry.2; mouse.
DR CTD; 11282; -.
DR MGI; MGI:2143974; Mgat4b.
DR VEuPathDB; HostDB:ENSMUSG00000036620; -.
DR eggNOG; ENOG502QPQJ; Eukaryota.
DR GeneTree; ENSGT00940000156526; -.
DR HOGENOM; CLU_027046_3_0_1; -.
DR InParanoid; Q812F8; -.
DR OMA; KKNFITT; -.
DR OrthoDB; 593094at2759; -.
DR PhylomeDB; Q812F8; -.
DR TreeFam; TF324570; -.
DR Reactome; R-MMU-975577; N-Glycan antennae elongation.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 103534; 5 hits in 73 CRISPR screens.
DR ChiTaRS; Mgat4b; mouse.
DR PRO; PR:Q812F8; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q812F8; protein.
DR Bgee; ENSMUSG00000036620; Expressed in ectoplacental cone and 248 other tissues.
DR ExpressionAtlas; Q812F8; baseline and differential.
DR Genevisible; Q812F8; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR GO; GO:0005793; C:endoplasmic reticulum-Golgi intermediate compartment; IBA:GO_Central.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0008375; F:acetylglucosaminyltransferase activity; IDA:MGI.
DR GO; GO:0008454; F:alpha-1,3-mannosylglycoprotein 4-beta-N-acetylglucosaminyltransferase activity; ISS:UniProtKB.
DR GO; GO:0016757; F:glycosyltransferase activity; IDA:MGI.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006486; P:protein glycosylation; ISS:UniProtKB.
DR GO; GO:0006487; P:protein N-linked glycosylation; IGI:MGI.
DR InterPro; IPR006759; Glyco_transf_54.
DR PANTHER; PTHR12062; PTHR12062; 1.
PE 2: Evidence at transcript level;
KW Coiled coil; Glycoprotein; Glycosyltransferase; Golgi apparatus; Membrane;
KW Metal-binding; Reference proteome; Signal-anchor; Transferase;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..548
FT /note="Alpha-1,3-mannosyl-glycoprotein 4-beta-N-
FT acetylglucosaminyltransferase B"
FT /id="PRO_0000288594"
FT TOPO_DOM 1..7
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 8..28
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 29..548
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT COILED 36..83
FT /evidence="ECO:0000255"
FT CARBOHYD 87
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 103
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 395..396
FT /note="EH -> SY (in Ref. 1; BAC55019)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 548 AA; 63302 MW; A66F88F4A05FBF27 CRC64;
MRLRNGTFLT LLLFCLCAFL SLSWYAALSG QKGDVVDIYQ REFLALRDRL HAAEQESLKR
SKELNLVLEE IKRAVSERQA LRDGEGNRTW GRLTEDPRLK PWNVSHRHVL HLPTVFHHLP
HLLAKESSLQ PAVRVGQGRT GVSVVMGIPS VRREVHSYLT DTLHSLISEL SPQEKEDSVI
VVLIAETDPQ YTSAVTENIK ALFPTEIHSG LLEVISPSPH FYPDFSRLRE SFGDPKERVR
WRTKQNLDYC FLMMYAQSKG IYYVQLEDDI VAKPNYLSTM KNFALQQPSE DWMILEFSQL
GFIGKMFKSL DLSLIVEFIL MFYRDKPIDW LLDHILWVKV CNPEKDAKHC DRQKANLRIR
FKPSLFQHVG THSSLAGKIQ KLKDKDFGKH ALRKEHVNPP AEVSTSLKTY QHFTLEKAYL
REDFFWAFTP AAGDFIRFRF FQPLRLERFF FRSGNIEHPE DKLFNTSVEV LPFDNPQSEK
EALQEGRSAT LRYPRSPDGY LQIGSFYKGV AEGEVDPAFG PLEALRLSIQ TDSPVWVILS
EIFLKKAD
