CHST4_MOUSE
ID CHST4_MOUSE Reviewed; 388 AA.
AC Q9R1I1; Q9WUE5;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Carbohydrate sulfotransferase 4;
DE EC=2.8.2.- {ECO:0000269|PubMed:10435581, ECO:0000269|PubMed:16227985};
DE AltName: Full=Galactose/N-acetylglucosamine/N-acetylglucosamine 6-O-sulfotransferase 3;
DE Short=GST-3;
DE AltName: Full=High endothelial cells N-acetylglucosamine 6-O-sulfotransferase;
DE Short=HEC-GlcNAc6ST;
DE AltName: Full=L-selectin ligand sulfotransferase;
DE Short=LSST;
DE AltName: Full=N-acetylglucosamine 6-O-sulfotransferase 2;
DE Short=GlcNAc6ST-2;
DE Short=Gn6st-2;
GN Name=Chst4; Synonyms=Gst3;
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], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RX PubMed=10435581; DOI=10.1016/s1074-7613(00)80083-7;
RA Hiraoka N., Petryniak B., Nakayama J., Tsuboi S., Suzuki M., Yeh J.-C.,
RA Izawa D., Tanaka T., Miyasaka M., Lowe J.B., Fukuda M.;
RT "A novel, high endothelial venule-specific sulfotransferase expresses 6-
RT sulfo sialyl Lewis(x), an L-selectin ligand displayed by CD34.";
RL Immunity 11:79-89(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=C57BL/6J; TISSUE=Tonsil;
RX PubMed=10330415; DOI=10.1083/jcb.145.4.899;
RA Bistrup A., Bhakta S., Lee J.K., Belov Y.Y., Gunn M.D., Zuo F.-R.,
RA Huang C.-C., Kannagi R., Rosen S.D., Hemmerich S.;
RT "Sulfotransferases of two specificities function in the reconstitution of
RT high endothelial cell ligands for L-selectin.";
RL J. Cell Biol. 145:899-910(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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].
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).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=11520459; DOI=10.1016/s1074-7613(01)00188-1;
RA Hemmerich S., Bistrup A., Singer M.S., van Zante A., Lee J.K., Tsay D.,
RA Peters M., Carminati J.L., Brennan T.J., Carver-Moore K., Leviten M.,
RA Fuentes M.E., Ruddle N.H., Rosen S.D.;
RT "Sulfation of L-selectin ligands by an HEV-restricted sulfotransferase
RT regulates lymphocyte homing to lymph nodes.";
RL Immunity 15:237-247(2001).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14597732; DOI=10.1084/jem.20030057;
RA van Zante A., Gauguet J.-M., Bistrup A., Tsay D., von Andrian U.H.,
RA Rosen S.D.;
RT "Lymphocyte-HEV interactions in lymph nodes of a sulfotransferase-deficient
RT mouse.";
RL J. Exp. Med. 198:1289-1300(2003).
RN [7]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=15111310; DOI=10.1016/s0002-9440(10)63722-4;
RA Bistrup A., Tsay D., Shenoy P., Singer M.S., Bangia N., Luther S.A.,
RA Cyster J.G., Ruddle N.H., Rosen S.D.;
RT "Detection of a sulfotransferase (HEC-GlcNAc6ST) in high endothelial
RT venules of lymph nodes and in high endothelial venule-like vessels within
RT ectopic lymphoid aggregates: relationship to the MECA-79 epitope.";
RL Am. J. Pathol. 164:1635-1644(2004).
RN [8]
RP FUNCTION.
RX PubMed=15319280; DOI=10.1182/blood-2004-05-1986;
RA Gauguet J.M., Rosen S.D., Marth J.D., von Andrian U.H.;
RT "Core 2 branching beta1,6-N-acetylglucosaminyltransferase and high
RT endothelial cell N-acetylglucosamine-6-sulfotransferase exert differential
RT control over B- and T-lymphocyte homing to peripheral lymph nodes.";
RL Blood 104:4104-4112(2004).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=14593101; DOI=10.1074/jbc.m311150200;
RA Hiraoka N., Kawashima H., Petryniak B., Nakayama J., Mitoma J., Marth J.D.,
RA Lowe J.B., Fukuda M.;
RT "Core 2 branching beta1,6-N-acetylglucosaminyltransferase and high
RT endothelial venule-restricted sulfotransferase collaboratively control
RT lymphocyte homing.";
RL J. Biol. Chem. 279:3058-3067(2004).
RN [10]
RP FUNCTION, CATALYTIC ACTIVITY, PATHWAY, DISRUPTION PHENOTYPE, AND TISSUE
RP SPECIFICITY.
RX PubMed=16227985; DOI=10.1038/ni1259;
RA Kawashima H., Petryniak B., Hiraoka N., Mitoma J., Huckaby V., Nakayama J.,
RA Uchimura K., Kadomatsu K., Muramatsu T., Lowe J.B., Fukuda M.;
RT "N-acetylglucosamine-6-O-sulfotransferases 1 and 2 cooperatively control
RT lymphocyte homing through L-selectin ligand biosynthesis in high
RT endothelial venules.";
RL Nat. Immunol. 6:1096-1104(2005).
RN [11]
RP FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=16227986; DOI=10.1038/ni1258;
RA Uchimura K., Gauguet J.M., Singer M.S., Tsay D., Kannagi R., Muramatsu T.,
RA von Andrian U.H., Rosen S.D.;
RT "A major class of L-selectin ligands is eliminated in mice deficient in two
RT sulfotransferases expressed in high endothelial venules.";
RL Nat. Immunol. 6:1105-1113(2005).
CC -!- FUNCTION: Sulfotransferase involved in SELL/L-selectin ligand
CC biosynthesis pathway. Catalyzes the transfer of the sulfate group from
CC 3'-phospho-5'-adenylyl sulfate (PAPS) onto the hydroxyl group at C-6
CC position of the non-reducing N-acetylglucosamine (GlcNAc) residue
CC within O-linked mucin-type glycans (PubMed:10435581, PubMed:16227985,
CC PubMed:15319280, PubMed:16227986, PubMed:14597732, PubMed:15111310).
CC Contributes to generate sialyl 6-sulfo Lewis X determinant (also known
CC as MECA-79 epitope) for SELL recognition, a prerequisite for continuous
CC lymphocyte homing into peripheral lymph nodes and antigen immune
CC surveillance. Transfers the sulfate group primarily on core 2
CC GlcNAcbeta1-6(Galbeta1-3)GalNAcalphaSer/Thr and extended core 1
CC GlcNAcbeta1-3Galbeta1-3GalNAcalphaSer/Thr based O-linked glycans on
CC CD34 and GLYCAM1 peripheral node addressins (PNAds) expressed on the
CC lumenal side of high endothelial venules (HEVs) (PubMed:10435581,
CC PubMed:16227985, PubMed:15319280, PubMed:16227986, PubMed:15111310,
CC PubMed:14593101). The recognition of PNAds by SELL initiates a
CC multistep process comprising tethering and rolling of blood lymphocytes
CC on HEVs against the blood flow, followed by chemokine signaling,
CC integrin-mediated lymphocyte adhesion onto endothelial cells and
CC lymphocyte transendothelial migration. Modulates rolling velocity and
CC differential T and B lymphocyte recruitment into peripheral lymph
CC nodes, with a major role in B lymphocyte homing (PubMed:16227985,
CC PubMed:15319280, PubMed:16227986, PubMed:14597732, PubMed:10435581).
CC Might be redundant in sulfation of MADCAM1 and lymphocyte trafficking
CC to mesenteric lymph nodes (PubMed:10435581, PubMed:11520459,
CC PubMed:16227986). Can also sulfonate core 3 GlcNAcbeta1-3GalNAc-R based
CC glycans as well as GlcNAcbeta1-3Galbeta1-Glc, GlcNAcbeta1-6ManOMe and
CC GlcNAcbeta1-2Man oligosaccharides, which might be ectopically expressed
CC during tumorigenesis (By similarity). {ECO:0000250|UniProtKB:Q8NCG5,
CC ECO:0000269|PubMed:10435581, ECO:0000269|PubMed:11520459,
CC ECO:0000269|PubMed:14593101, ECO:0000269|PubMed:14597732,
CC ECO:0000269|PubMed:15111310, ECO:0000269|PubMed:15319280,
CC ECO:0000269|PubMed:16227985, ECO:0000269|PubMed:16227986}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-threonyl-[protein] = 3-O-{6-O-sulfo-N-acetyl-beta-
CC D-glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-threonyl-[protein] + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67856, Rhea:RHEA-COMP:17368, Rhea:RHEA-
CC COMP:17369, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:176489, ChEBI:CHEBI:176492;
CC Evidence={ECO:0000269|PubMed:16227985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67857;
CC Evidence={ECO:0000305|PubMed:16227985};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-seryl-[protein] = 3-O-{6-O-sulfo-N-acetyl-beta-D-
CC glucosaminyl-(1->3)-beta-D-galactosyl-(1->3)-N-acetyl-alpha-D-
CC galactosaminyl}-L-seryl-[protein] + adenosine 3',5'-bisphosphate +
CC H(+); Xref=Rhea:RHEA:67860, Rhea:RHEA-COMP:17365, Rhea:RHEA-
CC COMP:17366, ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:176490, ChEBI:CHEBI:176491;
CC Evidence={ECO:0000269|PubMed:16227985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67861;
CC Evidence={ECO:0000305|PubMed:16227985};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-galactosyl-(1->3)-[N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-threonyl-[protein] = 3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-threonyl-[protein] + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:67864, Rhea:RHEA-COMP:14420, Rhea:RHEA-COMP:17370,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:139607, ChEBI:CHEBI:176493;
CC Evidence={ECO:0000269|PubMed:10435581, ECO:0000269|PubMed:16227985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67865;
CC Evidence={ECO:0000305|PubMed:10435581, ECO:0000305|PubMed:16227985};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3'-phosphoadenylyl sulfate + 3-O-{beta-D-galactosyl-(1->3)-[N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-seryl-[protein] = 3-O-{beta-D-galactosyl-(1->3)-[6-O-sulfo-N-
CC acetyl-beta-D-glucosaminyl-(1->6)]-N-acetyl-alpha-D-galactosaminyl}-
CC L-seryl-[protein] + adenosine 3',5'-bisphosphate + H(+);
CC Xref=Rhea:RHEA:67868, Rhea:RHEA-COMP:14419, Rhea:RHEA-COMP:17367,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343,
CC ChEBI:CHEBI:139605, ChEBI:CHEBI:176494;
CC Evidence={ECO:0000269|PubMed:10435581, ECO:0000269|PubMed:16227985};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67869;
CC Evidence={ECO:0000305|PubMed:10435581, ECO:0000305|PubMed:16227985};
CC -!- PATHWAY: Protein modification; carbohydrate sulfation.
CC {ECO:0000269|PubMed:10435581, ECO:0000269|PubMed:16227985}.
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q8NCG5}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:15111310}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:15111310}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in high endothelial venules
CC (HEV) of peripheral lymph nodes. {ECO:0000269|PubMed:10435581,
CC ECO:0000269|PubMed:16227985, ECO:0000269|PubMed:16227986}.
CC -!- DISRUPTION PHENOTYPE: Mice are impaired in lymphocyte homing and
CC exhibit faster lymphocyte rolling and reduced lymphocyte sticking in
CC HEV. The epitope of SELL ligands recognized by the MECA-79 antibody is
CC greatly reduced or abolished in the abluminal aspect of HEV.
CC Simultaneous knockdown of CHST4 and CHST2 results in lower contact
CC hypersensitivity response when compared to wild-type littermates.
CC {ECO:0000269|PubMed:11520459, ECO:0000269|PubMed:14593101,
CC ECO:0000269|PubMed:14597732, ECO:0000269|PubMed:15111310,
CC ECO:0000269|PubMed:16227985}.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
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DR EMBL; AF109155; AAD45579.1; -; mRNA.
DR EMBL; AF131236; AAD33016.1; -; Genomic_DNA.
DR EMBL; AK009113; BAB26078.1; -; mRNA.
DR EMBL; BC057886; AAH57886.1; -; mRNA.
DR CCDS; CCDS22659.1; -.
DR RefSeq; NP_036128.3; NM_011998.4.
DR RefSeq; XP_006531106.1; XM_006531043.3.
DR RefSeq; XP_006531107.1; XM_006531044.2.
DR RefSeq; XP_006531108.1; XM_006531045.3.
DR AlphaFoldDB; Q9R1I1; -.
DR STRING; 10090.ENSMUSP00000104845; -.
DR GlyGen; Q9R1I1; 3 sites.
DR PhosphoSitePlus; Q9R1I1; -.
DR PaxDb; Q9R1I1; -.
DR PRIDE; Q9R1I1; -.
DR ProteomicsDB; 283838; -.
DR DNASU; 26887; -.
DR GeneID; 26887; -.
DR KEGG; mmu:26887; -.
DR UCSC; uc009njt.2; mouse.
DR CTD; 10164; -.
DR MGI; MGI:1349479; Chst4.
DR eggNOG; ENOG502RGC5; Eukaryota.
DR InParanoid; Q9R1I1; -.
DR OrthoDB; 1246608at2759; -.
DR PhylomeDB; Q9R1I1; -.
DR TreeFam; TF342871; -.
DR Reactome; R-MMU-913709; O-linked glycosylation of mucins.
DR UniPathway; UPA00353; -.
DR BioGRID-ORCS; 26887; 0 hits in 71 CRISPR screens.
DR ChiTaRS; Chst4; mouse.
DR PRO; PR:Q9R1I1; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9R1I1; protein.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005802; C:trans-Golgi network; ISO:MGI.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0050901; P:leukocyte tethering or rolling; IMP:MGI.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; ISO:MGI.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; IMP:UniProtKB.
DR GO; GO:0006477; P:protein sulfation; IMP:MGI.
DR GO; GO:0006790; P:sulfur compound metabolic process; ISO:MGI.
DR Gene3D; 3.40.50.300; -; 1.
DR InterPro; IPR016469; Carbohydrate_sulfotransferase.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000863; Sulfotransferase_dom.
DR Pfam; PF00685; Sulfotransfer_1; 1.
DR PIRSF; PIRSF005883; Carbohydrate_sulfotransferase; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycoprotein; Golgi apparatus;
KW Inflammatory response; Membrane; Reference proteome; Signal-anchor;
KW Transferase; Transmembrane; Transmembrane helix.
FT CHAIN 1..388
FT /note="Carbohydrate sulfotransferase 4"
FT /id="PRO_0000085194"
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..388
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 50..56
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 204..212
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 307
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 328
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 369
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CONFLICT 221
FT /note="V -> M (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 306
FT /note="H -> Y (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 388 AA; 44636 MW; 6D5371AFB6884AEE CRC64;
MMLLKKGRLL MFLGSQVIVV ALFIHMSVHR HLSQREESRR PVHVLVLSSW RSGSSFVGQL
FGQHPDVFYL MEPAWHVWMT FTSSTAWKLH MAVRDLLRSV FLCDMSVFDA YMNPGPRKQS
SLFQWEQSRA LCSAPVCDFF PAHEISSPKH CKLLCGQQPF DMVEKACRSH GFVVLKEVRF
LSLQALYPLL TDPSLNLHVV HLVRDPRAVF RSREHTTIEL VVDSHIVLGQ HLETIKEEDQ
PYYAMKIICK SQVDIVKAIQ TLPEALQQRY LFLRYEDLVR APLAQTTRLY KFVGLDFLPH
LQTWVHNVTR GKGMGQHAFH TNARNALNVS QAWRWSLPYE KVSQLQDACG EAMDLLGYLQ
VRSQQEQGNL SLDLLSSSHI LGQVFREG
