CHST4_HUMAN
ID CHST4_HUMAN Reviewed; 386 AA.
AC Q8NCG5; Q8IV46; Q9Y5R3;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 2.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Carbohydrate sulfotransferase 4;
DE EC=2.8.2.- {ECO:0000269|PubMed:10330415, ECO:0000269|PubMed:11439191, ECO:0000269|PubMed:11726653, ECO:0000269|PubMed:12107080};
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;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND
RP TISSUE SPECIFICITY.
RC 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 [2]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=11439191; DOI=10.1016/s0092-8674(01)00394-4;
RA Yeh J.-C., Hiraoka N., Petryniak B., Nakayama J., Ellies L.G., Rabuka D.,
RA Hindsgaul O., Marth J.D., Lowe J.B., Fukuda M.;
RT "Novel sulfated lymphocyte homing receptors and their control by a Core1
RT extension beta 1,3-N-acetylglucosaminyltransferase.";
RL Cell 105:957-969(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Tonsil;
RX PubMed=11181564; DOI=10.1093/glycob/11.1.75;
RA Hemmerich S., Lee J.K., Bhakta S., Bistrup A., Ruddle N.R., Rosen S.D.;
RT "Chromosomal localization and genomic organization for the galactose/ N-
RT acetylgalactosamine/N-acetylglucosamine 6-O-sulfotransferase gene family.";
RL Glycobiology 11:75-87(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Teratocarcinoma;
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., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., 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., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA 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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
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 [6]
RP TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11310842;
RA Li X., Tu L., Murphy P.G., Kadono T., Steeber D.A., Tedder T.F.;
RT "CHST1 and CHST2 sulfotransferase expression by vascular endothelial cells
RT regulates shear-resistant leukocyte rolling via L-selectin.";
RL J. Leukoc. Biol. 69:565-574(2001).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND PATHWAY.
RX PubMed=12107080; DOI=10.1093/glycob/12.6.379;
RA Seko A., Nagata K., Yonezawa S., Yamashita K.;
RT "Ectopic expression of a GlcNAc 6-O-sulfotransferase, GlcNAc6ST-2, in
RT colonic mucinous adenocarcinoma.";
RL Glycobiology 12:379-388(2002).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND PATHWAY.
RX PubMed=11726653; DOI=10.1074/jbc.m106587200;
RA Uchimura K., El-Fasakhany F.M., Hori M., Hemmerich S., Blink S.E.,
RA Kansas G.S., Kanamori A., Kumamoto K., Kannagi R., Muramatsu T.;
RT "Specificities of N-acetylglucosamine-6-O-sulfotransferases in relation to
RT L-selectin ligand synthesis and tumor-associated enzyme expression.";
RL J. Biol. Chem. 277:3979-3984(2002).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=12855678; DOI=10.1074/jbc.m304928200;
RA de Graffenried C.L., Bertozzi C.R.;
RT "Golgi localization of carbohydrate sulfotransferases is a determinant of
RT L-selectin ligand biosynthesis.";
RL J. Biol. Chem. 278:40282-40295(2003).
RN [10]
RP SUBUNIT.
RX PubMed=15220337; DOI=10.1074/jbc.m405709200;
RA de Graffenried C.L., Bertozzi C.R.;
RT "The stem region of the sulfotransferase GlcNAc6ST-1 is a determinant of
RT substrate specificity.";
RL J. Biol. Chem. 279:40035-40043(2004).
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. Contributes to generate sialyl 6-
CC sulfo Lewis X determinant (also known as MECA-79 epitope) for SELL
CC recognition, a prerequisite for continuous lymphocyte homing into
CC peripheral lymph nodes and antigen immune surveillance
CC (PubMed:11439191, PubMed:12107080, PubMed:10330415, PubMed:11726653).
CC Transfers the sulfate group primarily on core 2 GlcNAcbeta1-6(Galbeta1-
CC 3)GalNAcalphaSer/Thr and extended core 1 GlcNAcbeta1-3Galbeta1-
CC 3GalNAcalphaSer/Thr based O-linked glycans on CD34 and GLYCAM1
CC peripheral node addressins (PNAds) expressed on the lumenal side of
CC high endothelial venules (HEVs) (PubMed:11439191). The recognition of
CC PNAds by SELL initiates a multistep process comprising tethering and
CC rolling of blood lymphocytes on HEVs against the blood flow, followed
CC by chemokine signaling, integrin-mediated lymphocyte adhesion onto
CC endothelial cells and lymphocyte transendothelial migration. Modulates
CC rolling velocity and differential T and B lymphocyte recruitment into
CC peripheral lymph nodes, with a major role in B lymphocyte homing. Might
CC be redundant in sulfation of MADCAM1 and lymphocyte trafficking to
CC mesenteric lymph nodes (By similarity). Can also sulfonate core 3
CC GlcNAcbeta1-3GalNAc-R based glycans as well as GlcNAcbeta1-3Galbeta1-
CC Glc, GlcNAcbeta1-6ManOMe and GlcNAcbeta1-2Man oligosaccharides, which
CC might be ectopically expressed during tumorigenesis (PubMed:12107080,
CC PubMed:11439191, PubMed:11726653). {ECO:0000250|UniProtKB:Q9R1I1,
CC ECO:0000269|PubMed:10330415, ECO:0000269|PubMed:11439191,
CC ECO:0000269|PubMed:11726653, ECO:0000269|PubMed:12107080}.
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:11439191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67857;
CC Evidence={ECO:0000305|PubMed:11439191};
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:11439191};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67861;
CC Evidence={ECO:0000305|PubMed:11439191};
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:10330415, ECO:0000269|PubMed:11439191,
CC ECO:0000269|PubMed:11726653, ECO:0000269|PubMed:12107080};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67865;
CC Evidence={ECO:0000305|PubMed:10330415, ECO:0000305|PubMed:11439191,
CC ECO:0000305|PubMed:11726653, ECO:0000305|PubMed:12107080};
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:10330415, ECO:0000269|PubMed:11439191,
CC ECO:0000269|PubMed:11726653, ECO:0000269|PubMed:12107080};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67869;
CC Evidence={ECO:0000305|PubMed:10330415, ECO:0000305|PubMed:11439191,
CC ECO:0000305|PubMed:11726653, ECO:0000305|PubMed:12107080};
CC -!- PATHWAY: Protein modification; carbohydrate sulfation.
CC {ECO:0000269|PubMed:10330415, ECO:0000269|PubMed:11439191,
CC ECO:0000269|PubMed:11726653, ECO:0000269|PubMed:12107080}.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15220337}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:12855678}; Single-pass type II membrane protein
CC {ECO:0000269|PubMed:12855678}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in HEV. Weakly expressed in
CC spleen. Not expressed in other tissues. Expressed in colonic mucinous
CC adenocarcinoma. {ECO:0000269|PubMed:10330415,
CC ECO:0000269|PubMed:11310842, ECO:0000269|PubMed:12107080}.
CC -!- INDUCTION: Upon cytokine activation, it is expressed at low level.
CC {ECO:0000269|PubMed:11310842}.
CC -!- MISCELLANEOUS: May serve as an anti-inflammatory target.
CC -!- SIMILARITY: Belongs to the sulfotransferase 1 family. Gal/GlcNAc/GalNAc
CC subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH35282.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF131235; AAD33015.1; -; mRNA.
DR EMBL; AF149783; AAK48417.1; -; mRNA.
DR EMBL; AF280088; AAG48246.1; -; mRNA.
DR EMBL; AK074746; BAC11177.1; -; mRNA.
DR EMBL; BC035282; AAH35282.1; ALT_INIT; mRNA.
DR CCDS; CCDS10902.1; -.
DR RefSeq; NP_001159867.1; NM_001166395.1.
DR RefSeq; NP_005760.1; NM_005769.2.
DR AlphaFoldDB; Q8NCG5; -.
DR BioGRID; 115466; 4.
DR IntAct; Q8NCG5; 2.
DR STRING; 9606.ENSP00000341206; -.
DR ChEMBL; CHEMBL2239; -.
DR GlyGen; Q8NCG5; 3 sites.
DR iPTMnet; Q8NCG5; -.
DR PhosphoSitePlus; Q8NCG5; -.
DR BioMuta; CHST4; -.
DR DMDM; 61211834; -.
DR EPD; Q8NCG5; -.
DR MassIVE; Q8NCG5; -.
DR PaxDb; Q8NCG5; -.
DR PeptideAtlas; Q8NCG5; -.
DR PRIDE; Q8NCG5; -.
DR ProteomicsDB; 72890; -.
DR Antibodypedia; 16600; 101 antibodies from 22 providers.
DR DNASU; 10164; -.
DR Ensembl; ENST00000338482.5; ENSP00000341206.5; ENSG00000140835.10.
DR Ensembl; ENST00000539698.4; ENSP00000441204.3; ENSG00000140835.10.
DR GeneID; 10164; -.
DR KEGG; hsa:10164; -.
DR MANE-Select; ENST00000539698.4; ENSP00000441204.3; NM_001166395.2; NP_001159867.1.
DR UCSC; uc002fan.4; human.
DR CTD; 10164; -.
DR DisGeNET; 10164; -.
DR GeneCards; CHST4; -.
DR HGNC; HGNC:1972; CHST4.
DR HPA; ENSG00000140835; Tissue enriched (gallbladder).
DR neXtProt; NX_Q8NCG5; -.
DR OpenTargets; ENSG00000140835; -.
DR PharmGKB; PA26504; -.
DR VEuPathDB; HostDB:ENSG00000140835; -.
DR eggNOG; ENOG502RGC5; Eukaryota.
DR GeneTree; ENSGT00940000162746; -.
DR HOGENOM; CLU_028381_3_1_1; -.
DR InParanoid; Q8NCG5; -.
DR OMA; WHVWMSF; -.
DR OrthoDB; 1246608at2759; -.
DR PhylomeDB; Q8NCG5; -.
DR TreeFam; TF342871; -.
DR PathwayCommons; Q8NCG5; -.
DR Reactome; R-HSA-913709; O-linked glycosylation of mucins.
DR SABIO-RK; Q8NCG5; -.
DR SignaLink; Q8NCG5; -.
DR UniPathway; UPA00353; -.
DR BioGRID-ORCS; 10164; 12 hits in 1064 CRISPR screens.
DR GeneWiki; CHST4; -.
DR GenomeRNAi; 10164; -.
DR Pharos; Q8NCG5; Tbio.
DR PRO; PR:Q8NCG5; -.
DR Proteomes; UP000005640; Chromosome 16.
DR RNAct; Q8NCG5; protein.
DR Bgee; ENSG00000140835; Expressed in gall bladder and 62 other tissues.
DR Genevisible; Q8NCG5; HS.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031228; C:intrinsic component of Golgi membrane; NAS:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0001517; F:N-acetylglucosamine 6-O-sulfotransferase activity; IDA:UniProtKB.
DR GO; GO:0008146; F:sulfotransferase activity; TAS:ProtInc.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR GO; GO:0006955; P:immune response; TAS:ProtInc.
DR GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
DR GO; GO:0006044; P:N-acetylglucosamine metabolic process; IDA:UniProtKB.
DR GO; GO:0016266; P:O-glycan processing; TAS:Reactome.
DR GO; GO:1903238; P:positive regulation of leukocyte tethering or rolling; ISS:UniProtKB.
DR GO; GO:0006477; P:protein sulfation; IBA:GO_Central.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:UniProtKB.
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..386
FT /note="Carbohydrate sulfotransferase 4"
FT /id="PRO_0000085193"
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..386
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT BINDING 51..57
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT BINDING 205..213
FT /ligand="3'-phosphoadenylyl sulfate"
FT /ligand_id="ChEBI:CHEBI:58339"
FT /evidence="ECO:0000250"
FT CARBOHYD 30
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 308
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VARIANT 361
FT /note="H -> Q (in dbSNP:rs3813744)"
FT /id="VAR_052528"
FT CONFLICT 225
FT /note="S -> N (in Ref. 4; BAC11177)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 386 AA; 45134 MW; 0C3BB4022417143A CRC64;
MLLPKKMKLL LFLVSQMAIL ALFFHMYSHN ISSLSMKAQP ERMHVLVLSS WRSGSSFVGQ
LFGQHPDVFY LMEPAWHVWM TFKQSTAWML HMAVRDLIRA VFLCDMSVFD AYMEPGPRRQ
SSLFQWENSR ALCSAPACDI IPQDEIIPRA HCRLLCSQQP FEVVEKACRS YSHVVLKEVR
FFNLQSLYPL LKDPSLNLHI VHLVRDPRAV FRSRERTKGD LMIDSRIVMG QHEQKLKKED
QPYYVMQVIC QSQLEIYKTI QSLPKALQER YLLVRYEDLA RAPVAQTSRM YEFVGLEFLP
HLQTWVHNIT RGKGMGDHAF HTNARDALNV SQAWRWSLPY EKVSRLQKAC GDAMNLLGYR
HVRSEQEQRN LLLDLLSTWT VPEQIH
