ID SIA8D_HUMAN Reviewed; 359 AA. AC Q92187; A8KA07; G3V104; Q8N1F4; Q92693; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1997, sequence version 1. DT 27-MAR-2024, entry version 187. DE RecName: Full=CMP-N-acetylneuraminate-poly-alpha-2,8-sialyltransferase; DE EC=2.4.3.- {ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:11279095, ECO:0000269|PubMed:28810663, ECO:0000269|PubMed:9774483}; DE AltName: Full=Alpha-2,8-sialyltransferase 8D; DE AltName: Full=Polysialyltransferase {ECO:0000303|PubMed:7624364}; DE AltName: Full=Polysialyltransferase-1; DE AltName: Full=Sialyltransferase 8D; DE Short=SIAT8-D; DE AltName: Full=Sialyltransferase St8Sia IV; DE Short=ST8SiaIV; GN Name=ST8SIA4 {ECO:0000312|HGNC:HGNC:10871}; GN Synonyms=PST {ECO:0000303|PubMed:7624364}, PST1, SIAT8D; 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] (ISOFORM 1), FUNCTION, AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=7624364; DOI=10.1073/pnas.92.15.7031; RA Nakayama J., Fukuda M.N., Fredette B., Ranscht B., Fukuda M.; RT "Expression cloning of a human polysialyltransferase that forms the RT polysialylated neural cell adhesion molecule present in embryonic brain."; RL Proc. Natl. Acad. Sci. U.S.A. 92:7031-7035(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Trachea; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15372022; DOI=10.1038/nature02919; RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., RA Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., RA Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., RA Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., RA Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., RA Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., RA Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., RA Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., RA Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.; RT "The DNA sequence and comparative analysis of human chromosome 5."; RL Nature 431:268-274(2004). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT RP LYS-7. RC TISSUE=Brain, and Lung; 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 FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=9774483; DOI=10.1074/jbc.273.43.28524; RA Angata K., Suzuki M., Fukuda M.; RT "Differential and cooperative polysialylation of the neural cell adhesion RT molecule by two polysialyltransferases, PST and STX."; RL J. Biol. Chem. 273:28524-28532(1998). RN [7] RP SUBCELLULAR LOCATION, AND AUTOPOLYSIALYLATION. RX PubMed=9852130; DOI=10.1074/jbc.273.51.34586; RA Close B.E., Colley K.J.; RT "In vivo autopolysialylation and localization of the polysialyltransferases RT PST and STX."; RL J. Biol. Chem. 273:34586-34593(1998). RN [8] RP FUNCTION, CATALYTIC ACTIVITY, AND AUTOPOLYSIALYLATION. RC TISSUE=Fetal brain; RX PubMed=10766765; DOI=10.1074/jbc.m910204199; RA Angata K., Suzuki M., McAuliffe J., Ding Y., Hindsgaul O., Fukuda M.; RT "Differential biosynthesis of polysialic acid on neural cell adhesion RT molecule (NCAM) and oligosaccharide acceptors by three distinct alpha2,8- RT Sialyltransferases, ST8Sia IV (PST), ST8Sia II (STX), and ST8Sia III."; RL J. Biol. Chem. 275:18594-18601(2000). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, DISULFIDE BONDS, GLYCOSYLATION AT ASN-74, RP IDENTIFICATION BY MASS SPECTROMETRY, AND MUTAGENESIS OF CYS-142; CYS-156; RP CYS-169; CYS-292 AND CYS-356. RX PubMed=11279095; DOI=10.1074/jbc.m100576200; RA Angata K., Yen T.Y., El-Battari A., Macher B.A., Fukuda M.; RT "Unique disulfide bond structures found in ST8Sia IV polysialyltransferase RT are required for its activity."; RL J. Biol. Chem. 276:15369-15377(2001). RN [10] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=28810663; DOI=10.1093/glycob/cwx057; RA Mori A., Hane M., Niimi Y., Kitajima K., Sato C.; RT "Different properties of polysialic acids synthesized by the RT polysialyltransferases ST8SIA2 and ST8SIA4."; RL Glycobiology 27:834-846(2017). RN [11] {ECO:0007744|PDB:5Y22, ECO:0007744|PDB:5Y3U} RP STRUCTURE BY NMR OF 258-279. RA Lu B., Liao S.M., Chen D., Liu X.H., Zhou G.P., Huang R.B.; RT "NMR-Based Model of the 22 Amino Acid Peptide in Polysialyltransferase RT Domain (PSTD) of the Polysialyltransferase ST8Sia IV."; RL Submitted (JUL-2017) to the PDB data bank. RN [12] {ECO:0007744|PDB:6AHZ} RP STRUCTURE BY NMR OF 245-279. RX PubMed=30569872; DOI=10.2174/1573406415666181218101623; RA Peng L.X., Liu X.H., Lu B., Liao S.M., Zhou F., Huang J.M., Chen D., RA Troy F.A. II, Zhou G.P., Huang R.B.; RT "The Inhibition of Polysialyltranseferase ST8SiaIV Through Heparin Binding RT to Polysialyltransferase Domain (PSTD)."; RL Med. Chem. 15:486-495(2019). RN [13] RP VARIANT [LARGE SCALE ANALYSIS] GLY-92. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Catalyzes the transfer of a sialic acid from a CMP-linked CC sialic acid donor onto a terminal alpha-2,3-, alpha-2,6-, or alpha-2,8- CC linked sialic acid of an N-linked glycan protein acceptor through CC alpha-2,8-linkages (PubMed:10766765, PubMed:11279095, PubMed:9774483, CC PubMed:28810663). Therefore, participates in polysialic acid synthesis CC on various sialylated N-acetyllactosaminyl oligosaccharides, including CC NCAM1 N-glycans, FETUB N-glycans and AHSG (PubMed:10766765, CC PubMed:11279095, PubMed:9774483, PubMed:28810663). It is noteworthy CC that alpha-2,3-linked sialic acid is apparently a better acceptor than CC alpha-2,6-linked sialic acid (PubMed:9774483). CC {ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:11279095, CC ECO:0000269|PubMed:28810663, ECO:0000269|PubMed:9774483}. CC -!- CATALYTIC ACTIVITY: CC Reaction=[N-acetyl-alpha-D-neuraminosyl-(2->8)](n) + CMP-N-acetyl-beta- CC neuraminate = [N-acetyl-alpha-D-neuraminosyl-(2->8)](n+1) + CMP + CC H(+); Xref=Rhea:RHEA:77367, Rhea:RHEA-COMP:14315, Rhea:RHEA- CC COMP:18878, ChEBI:CHEBI:15378, ChEBI:CHEBI:57812, ChEBI:CHEBI:60377, CC ChEBI:CHEBI:139252; Evidence={ECO:0000269|PubMed:10766765, CC ECO:0000269|PubMed:11279095, ECO:0000269|PubMed:28810663, CC ECO:0000269|PubMed:9774483}; CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77368; CC Evidence={ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:11279095, CC ECO:0000269|PubMed:28810663, ECO:0000269|PubMed:9774483}; CC -!- PATHWAY: Protein modification; protein glycosylation. CC {ECO:0000269|PubMed:10766765, ECO:0000269|PubMed:11279095, CC ECO:0000269|PubMed:28810663, ECO:0000269|PubMed:9774483}. CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane CC {ECO:0000269|PubMed:9852130}; Single-pass type II membrane protein CC {ECO:0000305}. Secreted {ECO:0000269|PubMed:9852130}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q92187-1; Sequence=Displayed; CC Name=2; CC IsoId=Q92187-2; Sequence=VSP_044867; CC -!- TISSUE SPECIFICITY: Highly expressed in fetal brain, lung and kidney CC and in adult heart, spleen and thymus (PubMed:7624364). Present to a CC lesser extent in adult brain, placenta, lung, large and small intestine CC and peripheral blood leukocytes (PubMed:7624364). CC {ECO:0000269|PubMed:7624364}. CC -!- PTM: Autopolysialylated. {ECO:0000269|PubMed:10766765, CC ECO:0000269|PubMed:9852130}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 29 family. CC {ECO:0000305}. CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - GTase; Note=ST8Sia CC IV; CC URL="http://www.functionalglycomics.org/glycomics/molecule/jsp/glycoEnzyme/viewGlycoEnzyme.jsp?gbpId=gt_hum_639"; 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; L41680; AAC41775.1; -; mRNA. DR EMBL; AK292872; BAF85561.1; -; mRNA. DR EMBL; AC010411; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC117530; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471086; EAW49104.1; -; Genomic_DNA. DR EMBL; CH471086; EAW49105.1; -; Genomic_DNA. DR EMBL; BC027866; AAH27866.1; -; mRNA. DR EMBL; BC053657; AAH53657.1; -; mRNA. DR CCDS; CCDS4091.1; -. [Q92187-1] DR CCDS; CCDS47252.1; -. [Q92187-2] DR PIR; I59403; I59403. DR RefSeq; NP_005659.1; NM_005668.5. [Q92187-1] DR RefSeq; NP_778222.1; NM_175052.2. [Q92187-2] DR PDB; 5Y22; NMR; -; A=258-279. DR PDB; 5Y3U; NMR; -; A=258-279. DR PDB; 6AHZ; NMR; -; A=245-279. DR PDBsum; 5Y22; -. DR PDBsum; 5Y3U; -. DR PDBsum; 6AHZ; -. DR AlphaFoldDB; Q92187; -. DR SMR; Q92187; -. DR BioGRID; 113636; 84. DR IntAct; Q92187; 66. DR STRING; 9606.ENSP00000231461; -. DR CAZy; GT29; Glycosyltransferase Family 29. DR GlyCosmos; Q92187; 5 sites, No reported glycans. DR GlyGen; Q92187; 6 sites, 1 O-linked glycan (1 site). DR iPTMnet; Q92187; -. DR PhosphoSitePlus; Q92187; -. DR BioMuta; ST8SIA4; -. DR DMDM; 2494834; -. DR EPD; Q92187; -. DR MassIVE; Q92187; -. DR PaxDb; 9606-ENSP00000231461; -. DR PeptideAtlas; Q92187; -. DR ProteomicsDB; 32217; -. DR ProteomicsDB; 75254; -. [Q92187-1] DR Pumba; Q92187; -. DR ABCD; Q92187; 1 sequenced antibody. DR Antibodypedia; 25167; 204 antibodies from 24 providers. DR DNASU; 7903; -. DR Ensembl; ENST00000231461.10; ENSP00000231461.4; ENSG00000113532.13. [Q92187-1] DR Ensembl; ENST00000451528.2; ENSP00000428914.1; ENSG00000113532.13. [Q92187-2] DR GeneID; 7903; -. DR KEGG; hsa:7903; -. DR MANE-Select; ENST00000231461.10; ENSP00000231461.4; NM_005668.6; NP_005659.1. DR UCSC; uc003knk.5; human. [Q92187-1] DR AGR; HGNC:10871; -. DR CTD; 7903; -. DR DisGeNET; 7903; -. DR GeneCards; ST8SIA4; -. DR HGNC; HGNC:10871; ST8SIA4. DR HPA; ENSG00000113532; Tissue enhanced (lymphoid). DR MIM; 602547; gene. DR neXtProt; NX_Q92187; -. DR OpenTargets; ENSG00000113532; -. DR PharmGKB; PA35772; -. DR VEuPathDB; HostDB:ENSG00000113532; -. DR eggNOG; KOG2692; Eukaryota. DR GeneTree; ENSGT01030000234535; -. DR HOGENOM; CLU_048583_3_0_1; -. DR InParanoid; Q92187; -. DR OMA; HAAEGWK; -. DR OrthoDB; 5348004at2759; -. DR PhylomeDB; Q92187; -. DR TreeFam; TF352820; -. DR BRENDA; 2.4.99.8; 2681. DR PathwayCommons; Q92187; -. DR Reactome; R-HSA-4085001; Sialic acid metabolism. DR Reactome; R-HSA-419037; NCAM1 interactions. DR SignaLink; Q92187; -. DR UniPathway; UPA00378; -. DR BioGRID-ORCS; 7903; 9 hits in 1143 CRISPR screens. DR ChiTaRS; ST8SIA4; human. DR GeneWiki; ST8SIA4; -. DR GenomeRNAi; 7903; -. DR Pharos; Q92187; Tbio. DR PRO; PR:Q92187; -. DR Proteomes; UP000005640; Chromosome 5. DR RNAct; Q92187; Protein. DR Bgee; ENSG00000113532; Expressed in bronchial epithelial cell and 165 other cell types or tissues. DR ExpressionAtlas; Q92187; baseline and differential. DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB. DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome. DR GO; GO:0003828; F:alpha-N-acetylneuraminate alpha-2,8-sialyltransferase activity; IDA:UniProtKB. DR GO; GO:0033691; F:sialic acid binding; IC:BHF-UCL. DR GO; GO:0008373; F:sialyltransferase activity; IDA:UniProtKB. DR GO; GO:0001574; P:ganglioside biosynthetic process; IDA:BHF-UCL. DR GO; GO:0006491; P:N-glycan processing; IDA:BHF-UCL. DR GO; GO:0007399; P:nervous system development; TAS:ProtInc. DR GO; GO:0009311; P:oligosaccharide metabolic process; IDA:BHF-UCL. DR GO; GO:0006486; P:protein glycosylation; IDA:BHF-UCL. DR GO; GO:0036211; P:protein modification process; TAS:ProtInc. DR GO; GO:0097503; P:sialylation; IDA:UniProtKB. DR Gene3D; 3.90.1480.20; Glycosyl transferase family 29; 1. DR InterPro; IPR001675; Glyco_trans_29. DR InterPro; IPR038578; GT29-like_sf. DR InterPro; IPR012163; Sialyl_trans. DR PANTHER; PTHR11987; ALPHA-2,8-SIALYLTRANSFERASE; 1. DR PANTHER; PTHR11987:SF48; CMP-N-ACETYLNEURAMINATE-POLY-ALPHA-2,8-SIALYLTRANSFERASE; 1. DR Pfam; PF00777; Glyco_transf_29; 1. DR PIRSF; PIRSF005557; Sialyl_trans; 1. DR Genevisible; Q92187; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disulfide bond; Glycoprotein; KW Glycosyltransferase; Golgi apparatus; Membrane; Reference proteome; KW Secreted; Signal-anchor; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1..359 FT /note="CMP-N-acetylneuraminate-poly-alpha-2,8- FT sialyltransferase" FT /id="PRO_0000149293" FT TOPO_DOM 1..7 FT /note="Cytoplasmic" FT /evidence="ECO:0000255" FT TRANSMEM 8..20 FT /note="Helical; Signal-anchor for type II membrane protein" FT /evidence="ECO:0000255" FT TOPO_DOM 21..359 FT /note="Lumenal" FT /evidence="ECO:0000255" FT ACT_SITE 331 FT /note="Proton donor/acceptor" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 147 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 170 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 279 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 280 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 281 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT BINDING 301 FT /ligand="CMP-N-acetyl-beta-neuraminate" FT /ligand_id="ChEBI:CHEBI:57812" FT /evidence="ECO:0000250|UniProtKB:O43173" FT CARBOHYD 50 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 74 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000269|PubMed:11279095" FT CARBOHYD 119 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 204 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT CARBOHYD 219 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 142..292 FT /evidence="ECO:0000269|PubMed:11279095" FT DISULFID 156..356 FT /evidence="ECO:0000269|PubMed:11279095" FT VAR_SEQ 169..359 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_044867" FT VARIANT 7 FT /note="R -> K (in dbSNP:rs199768560)" FT /evidence="ECO:0000269|PubMed:15489334" FT /id="VAR_068976" FT VARIANT 92 FT /note="E -> G (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036169" FT MUTAGEN 142 FT /note="C->A: Loss of NCAM1 polysialylation activity. Loss FT of autopolysialylation. Loss of NCAM1 polysialylation FT activity; when associated with A-292. Loss of FT autopolysialylation; when associated with A-292." FT /evidence="ECO:0000269|PubMed:11279095" FT MUTAGEN 156 FT /note="C->A: Loss of NCAM1 polysialylation activity. Loss FT of autopolysialylation.Loss of NCAM1 polysialylation FT activity; when associated with A-356. Loss of FT autopolysialylation; when associated with A-356." FT /evidence="ECO:0000269|PubMed:11279095" FT MUTAGEN 169 FT /note="C->A: Reduces NCAM1 polysialylation activity. Loss FT of autopolysialylation." FT /evidence="ECO:0000269|PubMed:11279095" FT MUTAGEN 292 FT /note="C->A: Loss of NCAM1 polysialylation activity. Loss FT of autopolysialylation.Loss of NCAM1 polysialylation FT activity; when associated with A-142. Loss of FT autopolysialylation; when associated with A-142." FT /evidence="ECO:0000269|PubMed:11279095" FT MUTAGEN 356 FT /note="C->A: Loss of NCAM1 polysialylation activity. Loss FT of autopolysialylation.Loss of NCAM1 polysialylation FT activity; when associated with A-156. Loss of FT autopolysialylation; when associated with A-156." FT /evidence="ECO:0000269|PubMed:11279095" FT HELIX 247..253 FT /evidence="ECO:0007829|PDB:6AHZ" FT HELIX 260..269 FT /evidence="ECO:0007829|PDB:5Y22" FT STRAND 272..274 FT /evidence="ECO:0007829|PDB:6AHZ" SQ SEQUENCE 359 AA; 41295 MW; C53FFDF658926D61 CRC64; MRSIRKRWTI CTISLLLIFY KTKEIARTEE HQETQLIGDG ELSLSRSLVN SSDKIIRKAG SSIFQHNVEG WKINSSLVLE IRKNILRFLD AERDVSVVKS SFKPGDVIHY VLDRRRTLNI SHDLHSLLPE VSPMKNRRFK TCAVVGNSGI LLDSECGKEI DSHNFVIRCN LAPVVEFAAD VGTKSDFITM NPSVVQRAFG GFRNESDREK FVHRLSMLND SVLWIPAFMV KGGEKHVEWV NALILKNKLK VRTAYPSLRL IHAVRGYWLT NKVPIKRPST GLLMYTLATR FCDEIHLYGF WPFPKDLNGK AVKYHYYDDL KYRYFSNASP HRMPLEFKTL NVLHNRGALK LTTGKCVKQ //