SIAT1_RAT
ID SIAT1_RAT Reviewed; 403 AA.
AC P13721; D4ABR2; G3V680;
DT 01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT 02-DEC-2020, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Beta-galactoside alpha-2,6-sialyltransferase 1;
DE Short=Alpha 2,6-ST 1;
DE EC=2.4.99.1 {ECO:0000269|PubMed:11278697, ECO:0000269|PubMed:24155237, ECO:0000269|PubMed:3121604};
DE AltName: Full=CMP-N-acetylneuraminate-beta-galactosamide-alpha-2,6-sialyltransferase 1;
DE AltName: Full=ST6Gal I;
DE Short=ST6GalI;
DE AltName: Full=Sialyltransferase 1;
GN Name=St6gal1; Synonyms=Siat1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RLA), PROTEIN SEQUENCE OF 64-79 AND
RP 329-357, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, SUBCELLULAR LOCATION,
RP GLYCOSYLATION, AND TISSUE SPECIFICITY.
RC TISSUE=Liver;
RX PubMed=3121604; DOI=10.1016/s0021-9258(18)45441-5;
RA Weinstein J., Lee E.U., McEntee K., Lai P.-H., Paulson J.C.;
RT "Primary structure of beta-galactoside alpha 2,6-sialyltransferase.
RT Conversion of membrane-bound enzyme to soluble forms by cleavage of the
RT NH2-terminal signal anchor.";
RL J. Biol. Chem. 262:17735-17743(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM RKA), IDENTIFICATION (ISOFORMS RLA AND
RP RKB), AND TISSUE SPECIFICITY.
RC TISSUE=Kidney;
RX PubMed=1733948; DOI=10.1016/s0021-9258(18)45909-1;
RA Wen D.X., Svensson E.C., Paulson J.C.;
RT "Tissue-specific alternative splicing of the beta-galactoside alpha 2,6-
RT sialyltransferase gene.";
RL J. Biol. Chem. 267:2512-2518(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-240 (ISOFORM RKA), IDENTIFICATION (ISOFORMS
RP RLA AND RKB), AND TISSUE SPECIFICITY.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney, and Liver;
RX PubMed=1983783; DOI=10.1093/glycob/1.1.25;
RA Wang X., O'Hanlon T.P., Young R.F., Lau J.T.Y.;
RT "Rat beta-galactoside alpha 2,6-sialyltransferase genomic organization:
RT alternate promoters direct the synthesis of liver and kidney transcripts.";
RL Glycobiology 1:25-31(1990).
RN [6]
RP PARTIAL NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY, AND MONOMER.
RC STRAIN=Sprague-Dawley; TISSUE=Kidney;
RX PubMed=2793863; DOI=10.1016/s0021-9258(18)71506-8;
RA O'Hanlon T.P., Lau K.M., Wang X., Lau J.T.Y.;
RT "Tissue-specific expression of beta-galactoside alpha-2,6-
RT sialyltransferase. Transcript heterogeneity predicts a divergent
RT polypeptide.";
RL J. Biol. Chem. 264:17389-17394(1989).
RN [7]
RP DISULFIDE BOND, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND MUTAGENESIS OF ARG-180; CYS-181; CYS-332 AND ASP-333.
RX PubMed=11278697; DOI=10.1074/jbc.m010542200;
RA Datta A.K., Chammas R., Paulson J.C.;
RT "Conserved cysteines in the sialyltransferase sialylmotifs form an
RT essential disulfide bond.";
RL J. Biol. Chem. 276:15200-15207(2001).
RN [8] {ECO:0007744|PDB:4MPS}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 95-403, GLYCOSYLATION AT ASN-146
RP AND ASN-158, DISULFIDE BONDS, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND MUTAGENESIS OF TYR-119; PHE-208; ASN-230; SER-231; GLN-232;
RP ASP-271; TYR-272; SER-319; CYS-350; GLN-354; LYS-355; CYS-361; TYR-366 AND
RP HIS-367.
RX PubMed=24155237; DOI=10.1074/jbc.m113.519041;
RA Meng L., Forouhar F., Thieker D., Gao Z., Ramiah A., Moniz H., Xiang Y.,
RA Seetharaman J., Milaninia S., Su M., Bridger R., Veillon L., Azadi P.,
RA Kornhaber G., Wells L., Montelione G.T., Woods R.J., Tong L., Moremen K.W.;
RT "Enzymatic basis for N-glycan sialylation: structure of rat alpha2,6-
RT sialyltransferase (ST6GAL1) reveals conserved and unique features for
RT glycan sialylation.";
RL J. Biol. Chem. 288:34680-34698(2013).
CC -!- FUNCTION: Transfers sialic acid from CMP-sialic acid to galactose-
CC containing acceptor substrates. {ECO:0000269|PubMed:11278697,
CC ECO:0000269|PubMed:24155237, ECO:0000269|PubMed:3121604}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a beta-D-galactoside + CMP-N-acetyl-beta-neuraminate = an N-
CC acetyl-alpha-neuraminyl-(2->6)-beta-D-galactosyl derivative + CMP +
CC H(+); Xref=Rhea:RHEA:52104, ChEBI:CHEBI:15378, ChEBI:CHEBI:28034,
CC ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, ChEBI:CHEBI:136398;
CC EC=2.4.99.1; Evidence={ECO:0000269|PubMed:11278697,
CC ECO:0000269|PubMed:24155237, ECO:0000269|PubMed:3121604};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=92 uM for donor CMP-Neu5Ac (at pH 6.5 and 37 degrees Celsius);
CC KM=1.8 mM for acceptor beta-Gal1,4-GlcNAc (at pH 6.5 and 37 degrees
CC Celsius);
CC Note=kcat is 35.6 min(-1) for the donor CMP-Neu5Ac (at pH 6.5 and 37
CC degrees Celsius). kcat is 40.3 min(-1) for the acceptor beta-Gal1,4-
CC GlcNAc (at pH 6.5 and 37 degrees Celsius).;
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:3121604}.
CC -!- SUBUNIT: Homodimer (By similarity). Monomer in its soluble form
CC (PubMed:11278697). {ECO:0000250|UniProtKB:P15907,
CC ECO:0000269|PubMed:11278697}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus, Golgi stack membrane
CC {ECO:0000269|PubMed:3121604}; Single-pass type II membrane protein
CC {ECO:0000305}. Secreted {ECO:0000269|PubMed:11278697,
CC ECO:0000269|PubMed:3121604}. Note=Membrane-bound form in trans
CC cisternae of Golgi. Secreted into the body fluid.
CC {ECO:0000269|PubMed:11278697, ECO:0000269|PubMed:3121604}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=RLA {ECO:0000303|PubMed:1983783};
CC IsoId=P13721-1; Sequence=Displayed;
CC Name=RKA {ECO:0000303|PubMed:1983783};
CC IsoId=P13721-2; Sequence=VSP_001782;
CC Name=RKB {ECO:0000303|PubMed:1983783};
CC IsoId=P13721-3; Sequence=VSP_001783;
CC -!- TISSUE SPECIFICITY: Expressed in hepatocytes (at protein level)
CC (PubMed:3121604, PubMed:11278697). Strongly expressed in liver, spleen,
CC lung, kidney and submaxillary gland and weakly in heart and brain
CC (PubMed:1733948, PubMed:2793863). {ECO:0000269|PubMed:11278697,
CC ECO:0000269|PubMed:1733948, ECO:0000269|PubMed:2793863,
CC ECO:0000269|PubMed:3121604}.
CC -!- TISSUE SPECIFICITY: [Isoform RLA]: Expressed in liver.
CC {ECO:0000269|PubMed:1983783}.
CC -!- TISSUE SPECIFICITY: [Isoform RKA]: Expressed in kidney, but not in
CC liver. {ECO:0000269|PubMed:1733948, ECO:0000269|PubMed:1983783}.
CC -!- TISSUE SPECIFICITY: [Isoform RKB]: Expressed in kidney, but not in
CC liver. {ECO:0000269|PubMed:1733948, ECO:0000269|PubMed:1983783}.
CC -!- PTM: The soluble form derives from the membrane form by proteolytic
CC processing. {ECO:0000269|PubMed:3121604}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:3121604}.
CC -!- MISCELLANEOUS: [Isoform RKA]: Produced by alternative promoter usage.
CC The alternative promoter is active in kidney.
CC {ECO:0000269|PubMed:1983783}.
CC -!- MISCELLANEOUS: [Isoform RKB]: Produced by alternative splicing of
CC isoform RKA. {ECO:0000269|PubMed:1983783}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family.
CC {ECO:0000305}.
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DR EMBL; M18769; AAA41196.1; -; mRNA.
DR EMBL; M73987; AAB06269.1; -; mRNA.
DR EMBL; M83143; AAB07233.1; -; mRNA.
DR EMBL; AABR07034602; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07034601; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07034600; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH473999; EDL78084.1; -; Genomic_DNA.
DR EMBL; CH473999; EDL78085.1; -; Genomic_DNA.
DR PIR; A28451; A28451.
DR PIR; C42327; C42327.
DR RefSeq; NP_001106815.1; NM_001113344.1. [P13721-1]
DR RefSeq; NP_671738.2; NM_147205.2.
DR RefSeq; XP_006248563.1; XM_006248501.1. [P13721-1]
DR RefSeq; XP_008767014.1; XM_008768792.2. [P13721-3]
DR PDB; 4MPS; X-ray; 2.40 A; A/B=95-403.
DR PDBsum; 4MPS; -.
DR AlphaFoldDB; P13721; -.
DR SMR; P13721; -.
DR IntAct; P13721; 1.
DR STRING; 10116.ENSRNOP00000002499; -.
DR ChEMBL; CHEMBL4276; -.
DR CAZy; GT29; Glycosyltransferase Family 29.
DR GlyGen; P13721; 2 sites.
DR iPTMnet; P13721; -.
DR PhosphoSitePlus; P13721; -.
DR PaxDb; P13721; -.
DR Ensembl; ENSRNOT00000002496; ENSRNOP00000002496; ENSRNOG00000001823. [P13721-1]
DR GeneID; 25197; -.
DR KEGG; rno:25197; -.
DR UCSC; RGD:3676; rat. [P13721-1]
DR CTD; 6480; -.
DR RGD; 3676; St6gal1.
DR eggNOG; KOG2692; Eukaryota.
DR GeneTree; ENSGT00940000157053; -.
DR HOGENOM; CLU_038334_0_0_1; -.
DR InParanoid; P13721; -.
DR OMA; ICVWKER; -.
DR OrthoDB; 494294at2759; -.
DR PhylomeDB; P13721; -.
DR TreeFam; TF323961; -.
DR BRENDA; 2.4.99.1; 5301.
DR Reactome; R-RNO-4085001; Sialic acid metabolism.
DR Reactome; R-RNO-975577; N-Glycan antennae elongation.
DR Reactome; R-RNO-977068; Termination of O-glycan biosynthesis.
DR SABIO-RK; P13721; -.
DR UniPathway; UPA00378; -.
DR PRO; PR:P13721; -.
DR Proteomes; UP000002494; Chromosome 11.
DR Proteomes; UP000234681; Chromosome 11.
DR Bgee; ENSRNOG00000001823; Expressed in liver and 20 other tissues.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:RGD.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IBA:GO_Central.
DR GO; GO:0032580; C:Golgi cisterna membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005797; C:Golgi medial cisterna; IDA:RGD.
DR GO; GO:0000139; C:Golgi membrane; ISO:RGD.
DR GO; GO:0000138; C:Golgi trans cisterna; IDA:RGD.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0003835; F:beta-galactoside alpha-2,6-sialyltransferase activity; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; ISO:RGD.
DR GO; GO:0008373; F:sialyltransferase activity; IDA:RGD.
DR GO; GO:0006054; P:N-acetylneuraminate metabolic process; ISS:UniProtKB.
DR GO; GO:0050922; P:negative regulation of chemotaxis; IDA:RGD.
DR GO; GO:2000110; P:negative regulation of macrophage apoptotic process; IDA:RGD.
DR GO; GO:0032946; P:positive regulation of mononuclear cell proliferation; IDA:RGD.
DR GO; GO:0006486; P:protein glycosylation; ISO:RGD.
DR GO; GO:0018279; P:protein N-linked glycosylation via asparagine; ISS:UniProtKB.
DR GO; GO:1990743; P:protein sialylation; IDA:RGD.
DR GO; GO:1900024; P:regulation of substrate adhesion-dependent cell spreading; IDA:RGD.
DR GO; GO:0045471; P:response to ethanol; IEP:RGD.
DR GO; GO:0097503; P:sialylation; ISS:UniProtKB.
DR Gene3D; 3.90.1480.20; -; 1.
DR InterPro; IPR001675; Glyco_trans_29.
DR InterPro; IPR038578; GT29-like_sf.
DR InterPro; IPR012163; Sialyl_trans.
DR Pfam; PF00777; Glyco_transf_29; 1.
DR PIRSF; PIRSF005557; Sialyl_trans; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative promoter usage; Alternative splicing;
KW Direct protein sequencing; Disulfide bond; Glycoprotein;
KW Glycosyltransferase; Golgi apparatus; Membrane; Phosphoprotein;
KW Reference proteome; Secreted; Signal-anchor; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..403
FT /note="Beta-galactoside alpha-2,6-sialyltransferase 1"
FT /id="PRO_0000149251"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT TRANSMEM 10..26
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 27..403
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 63..403
FT /note="Catalytic (soluble form)"
FT /evidence="ECO:0000305|PubMed:3121604"
FT BINDING 186
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 209
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 230
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 319..321
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 350
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 351
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 362
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT BINDING 366
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 373
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT MOD_RES 366
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT CARBOHYD 146
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24155237,
FT ECO:0007744|PDB:4MPS"
FT CARBOHYD 158
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:24155237,
FT ECO:0007744|PDB:4MPS"
FT DISULFID 139..403
FT /evidence="ECO:0000269|PubMed:24155237,
FT ECO:0007744|PDB:4MPS"
FT DISULFID 181..332
FT /evidence="ECO:0000269|PubMed:11278697,
FT ECO:0000269|PubMed:24155237, ECO:0007744|PDB:4MPS"
FT DISULFID 350..361
FT /evidence="ECO:0000250|UniProtKB:P15907"
FT VAR_SEQ 1..232
FT /note="MIHTNLKKKFSLFILVFLLFAVICVWKKGSDYEALTLQAKEFQMPKSQEKVA
FT MGSASQVVFSNSKQDPKEDIPILSYHRVTAKVKPQPSFQVWDKDSTYSKLNPRLLKIWR
FT NYLNMNKYKVSYKGPGPGVKFSVEALRCHLRDHVNVSMIEATDFPFNTTEWEGYLPKEN
FT FRTKVGPWQRCAVVSSAGSLKNSQLGREIDNHDAVLRFNGAPTDNFQQDVGSKTTIRLM
FT NSQ -> MRYLLFWYGLPHSYSQCVCHWTPASGIFENEPLLSLLLLVLGK (in
FT isoform RKA)"
FT /evidence="ECO:0000269|PubMed:1983783"
FT /id="VSP_001782"
FT VAR_SEQ 1..232
FT /note="MIHTNLKKKFSLFILVFLLFAVICVWKKGSDYEALTLQAKEFQMPKSQEKVA
FT MGSASQVVFSNSKQDPKEDIPILSYHRVTAKVKPQPSFQVWDKDSTYSKLNPRLLKIWR
FT NYLNMNKYKVSYKGPGPGVKFSVEALRCHLRDHVNVSMIEATDFPFNTTEWEGYLPKEN
FT FRTKVGPWQRCAVVSSAGSLKNSQLGREIDNHDAVLRFNGAPTDNFQQDVGSKTTIRLM
FT NSQ -> MRYLLFWYGLPHS (in isoform RKB)"
FT /evidence="ECO:0000269|PubMed:1983783"
FT /id="VSP_001783"
FT MUTAGEN 119
FT /note="Y->A: Protein destabilization."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 119
FT /note="Y->F: No effect on protein stability, nor on
FT catalytic activity."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 180
FT /note="R->A: Small decrease of sialyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11278697"
FT MUTAGEN 181
FT /note="C->A: Loss of sialyltransferase activity and
FT aberrant subcellular location."
FT /evidence="ECO:0000269|PubMed:11278697"
FT MUTAGEN 208
FT /note="F->A: Reduced KM/kcat values for CMP-Neu5Ac, no
FT effect on kinetic constants for beta-Gal1,4-GlcNAc."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 230
FT /note="N->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 231
FT /note="S->A: Protein destabilization."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 232
FT /note="Q->A: Decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 271
FT /note="D->A: Decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 272
FT /note="Y->A: Strongly decreased catalytic activity."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 319
FT /note="S->A: Protein destabilization."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 332
FT /note="C->A: Loss of sialyltransferase activity and
FT aberrant subcellular location."
FT /evidence="ECO:0000269|PubMed:11278697"
FT MUTAGEN 332
FT /note="C->S: Loss of sialyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11278697"
FT MUTAGEN 333
FT /note="D->A: Small decrease of sialyltransferase activity."
FT /evidence="ECO:0000269|PubMed:11278697"
FT MUTAGEN 350
FT /note="C->A: Loss of catalytic activity; when associated
FT with A-361."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 354
FT /note="Q->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 355
FT /note="K->A: No effect on catalytic activity."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 361
FT /note="C->A: Loss of catalytic activity; when associated
FT with A-350."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 366
FT /note="Y->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24155237"
FT MUTAGEN 367
FT /note="H->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:24155237"
FT CONFLICT 367
FT /note="H -> D (in Ref. 1; AAA41196)"
FT HELIX 107..115
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 134..144
FT /evidence="ECO:0007829|PDB:4MPS"
FT TURN 155..158
FT /evidence="ECO:0007829|PDB:4MPS"
FT TURN 160..165
FT /evidence="ECO:0007829|PDB:4MPS"
FT TURN 172..174
FT /evidence="ECO:0007829|PDB:4MPS"
FT STRAND 178..184
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 196..200
FT /evidence="ECO:0007829|PDB:4MPS"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:4MPS"
FT TURN 214..216
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:4MPS"
FT STRAND 225..230
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 231..236
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 238..241
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:4MPS"
FT STRAND 248..254
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 263..268
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 275..284
FT /evidence="ECO:0007829|PDB:4MPS"
FT STRAND 290..293
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 297..308
FT /evidence="ECO:0007829|PDB:4MPS"
FT STRAND 309..311
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 320..329
FT /evidence="ECO:0007829|PDB:4MPS"
FT STRAND 332..341
FT /evidence="ECO:0007829|PDB:4MPS"
FT STRAND 348..352
FT /evidence="ECO:0007829|PDB:4MPS"
FT STRAND 365..367
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 369..379
FT /evidence="ECO:0007829|PDB:4MPS"
FT HELIX 384..389
FT /evidence="ECO:0007829|PDB:4MPS"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:4MPS"
FT CONFLICT P13721-2:40
FT /note="V -> L (in Ref. 5; AAB06269)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 403 AA; 46754 MW; F40D7EA6B59355DA CRC64;
MIHTNLKKKF SLFILVFLLF AVICVWKKGS DYEALTLQAK EFQMPKSQEK VAMGSASQVV
FSNSKQDPKE DIPILSYHRV TAKVKPQPSF QVWDKDSTYS KLNPRLLKIW RNYLNMNKYK
VSYKGPGPGV KFSVEALRCH LRDHVNVSMI EATDFPFNTT EWEGYLPKEN FRTKVGPWQR
CAVVSSAGSL KNSQLGREID NHDAVLRFNG APTDNFQQDV GSKTTIRLMN SQLVTTEKRF
LKDSLYTEGI LIVWDPSVYH ADIPKWYQKP DYNFFETYKS YRRLNPSQPF YILKPQMPWE
LWDIIQEISA DLIQPNPPSS GMLGIIIMMT LCDQVDIYEF LPSKRKTDVC YYHQKFFDSA
CTMGAYHPLL FEKNMVKHLN EGTDEDIYLF GKATLSGFRN IRC
