GT253_HUMAN
ID GT253_HUMAN Reviewed; 595 AA.
AC Q5T4B2; A7MD00; C4AMA2; Q0VDF3; Q2VPJ4; Q4KMP2; Q5T4B1; Q8N107; Q96EZ5;
AC Q9P226; Q9UMW5;
DT 13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 03-AUG-2022, entry version 142.
DE RecName: Full=Inactive glycosyltransferase 25 family member 3;
DE AltName: Full=Cerebral endothelial cell adhesion molecule;
DE Flags: Precursor;
GN Name=CERCAM; Synonyms=CEECAM1, GLT25D3, KIAA1502;
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 2), FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=Brain capillary;
RX PubMed=10608765; DOI=10.1086/315163;
RA Starzyk R.M., Rosenow C., Frye J., Leismann M., Rodzinski E., Putney S.,
RA Tuomanen E.I.;
RT "Cerebral cell adhesion molecule: a novel leukocyte adhesion determinant on
RT blood-brain barrier capillary endothelium.";
RL J. Infect. Dis. 181:181-187(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 65-595 (ISOFORM 1).
RC TISSUE=Embryo;
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=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 321-595 (ISOFORMS 1/2).
RC TISSUE=Muscle, Ovary, and PNS;
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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-561 (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=10819331; DOI=10.1093/dnares/7.2.143;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVII. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:143-150(2000).
RN [7]
RP FUNCTION, LACK OF GALACTOSYLTRANSFERASE ACTIVITY, AND TISSUE SPECIFICITY.
RX PubMed=19075007; DOI=10.1128/mcb.02085-07;
RA Schegg B., Huelsmeier A.J., Rutschmann C., Maag C., Hennet T.;
RT "Core glycosylation of collagen is initiated by two beta(1-
RT O)galactosyltransferases.";
RL Mol. Cell. Biol. 29:943-952(2009).
RN [8]
RP LACK OF GALACTOSYLTRANSFERASE ACTIVITY, AND MUTAGENESIS OF SER-440;
RP GLN-450; VAL-451; ASN-452 AND PRO-453.
RX PubMed=22216269; DOI=10.1371/journal.pone.0029390;
RA Perrin-Tricaud C., Rutschmann C., Hennet T.;
RT "Identification of domains and amino acids essential to the collagen
RT galactosyltransferase activity of GLT25D1.";
RL PLoS ONE 6:E29390-E29390(2011).
CC -!- FUNCTION: Probable cell adhesion protein involved in leukocyte
CC transmigration across the blood-brain barrier. Does not express any
CC beta-galactosyltransferase activity in vitro.
CC {ECO:0000269|PubMed:10608765, ECO:0000269|PubMed:19075007}.
CC -!- INTERACTION:
CC Q5T4B2; Q8WTS1: ABHD5; NbExp=3; IntAct=EBI-12261896, EBI-2813554;
CC Q5T4B2; Q7Z3C6-3: ATG9A; NbExp=3; IntAct=EBI-12261896, EBI-12006308;
CC Q5T4B2; Q9UJX2: CDC23; NbExp=3; IntAct=EBI-12261896, EBI-396137;
CC Q5T4B2; Q5T4B2: CERCAM; NbExp=3; IntAct=EBI-12261896, EBI-12261896;
CC Q5T4B2; Q02930-3: CREB5; NbExp=3; IntAct=EBI-12261896, EBI-10192698;
CC Q5T4B2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-12261896, EBI-3867333;
CC Q5T4B2; Q9NW38: FANCL; NbExp=3; IntAct=EBI-12261896, EBI-2339898;
CC Q5T4B2; Q9Y680: FKBP7; NbExp=3; IntAct=EBI-12261896, EBI-3918971;
CC Q5T4B2; Q9BVV2: FNDC11; NbExp=3; IntAct=EBI-12261896, EBI-744935;
CC Q5T4B2; P57678: GEMIN4; NbExp=3; IntAct=EBI-12261896, EBI-356700;
CC Q5T4B2; O76003: GLRX3; NbExp=3; IntAct=EBI-12261896, EBI-374781;
CC Q5T4B2; P49639: HOXA1; NbExp=3; IntAct=EBI-12261896, EBI-740785;
CC Q5T4B2; Q2WGJ6: KLHL38; NbExp=3; IntAct=EBI-12261896, EBI-6426443;
CC Q5T4B2; Q3LI76: KRTAP15-1; NbExp=3; IntAct=EBI-12261896, EBI-11992140;
CC Q5T4B2; Q6PEX3: KRTAP26-1; NbExp=3; IntAct=EBI-12261896, EBI-3957672;
CC Q5T4B2; Q9BYR6: KRTAP3-3; NbExp=3; IntAct=EBI-12261896, EBI-3957694;
CC Q5T4B2; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-12261896, EBI-11962084;
CC Q5T4B2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-12261896, EBI-10261141;
CC Q5T4B2; Q9BYQ3: KRTAP9-3; NbExp=3; IntAct=EBI-12261896, EBI-1043191;
CC Q5T4B2; Q14847-2: LASP1; NbExp=3; IntAct=EBI-12261896, EBI-9088686;
CC Q5T4B2; Q9Y5V3: MAGED1; NbExp=3; IntAct=EBI-12261896, EBI-716006;
CC Q5T4B2; Q13064: MKRN3; NbExp=3; IntAct=EBI-12261896, EBI-2340269;
CC Q5T4B2; P32242: OTX1; NbExp=3; IntAct=EBI-12261896, EBI-740446;
CC Q5T4B2; Q7Z4N8: P4HA3; NbExp=3; IntAct=EBI-12261896, EBI-10181968;
CC Q5T4B2; Q7Z3K3: POGZ; NbExp=3; IntAct=EBI-12261896, EBI-1389308;
CC Q5T4B2; Q12837: POU4F2; NbExp=3; IntAct=EBI-12261896, EBI-17236143;
CC Q5T4B2; Q9BQY4: RHOXF2; NbExp=3; IntAct=EBI-12261896, EBI-372094;
CC Q5T4B2; Q8WV19: SFT2D1; NbExp=3; IntAct=EBI-12261896, EBI-2854842;
CC Q5T4B2; Q5JUK2: SOHLH1; NbExp=3; IntAct=EBI-12261896, EBI-12288855;
CC Q5T4B2; Q96A09: TENT5B; NbExp=3; IntAct=EBI-12261896, EBI-752030;
CC Q5T4B2; Q9BZL1: UBL5; NbExp=3; IntAct=EBI-12261896, EBI-607755;
CC Q5T4B2; O95231: VENTX; NbExp=3; IntAct=EBI-12261896, EBI-10191303;
CC Q5T4B2; A8MV65-2: VGLL3; NbExp=3; IntAct=EBI-12261896, EBI-11957216;
CC Q5T4B2; Q96MV8: ZDHHC15; NbExp=3; IntAct=EBI-12261896, EBI-12837904;
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum lumen {ECO:0000255|PROSITE-
CC ProRule:PRU10138}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5T4B2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5T4B2-2; Sequence=VSP_029234;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in secretory and
CC nervous tissues. {ECO:0000269|PubMed:10608765,
CC ECO:0000269|PubMed:19075007}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 25 family.
CC {ECO:0000305}.
CC -!- CAUTION: Has no glucosyltransferase activity. Concerning beta-
CC galactosyltransferase activity, the level of CERCAM could be too low to
CC detect any activity when tested in transfected insect cells.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH98432.2; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI19699.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAI19700.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAA96026.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC11040.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF177203; AAD51367.1; -; mRNA.
DR EMBL; AK074519; BAC11036.1; -; mRNA.
DR EMBL; AK074523; BAC11040.1; ALT_INIT; mRNA.
DR EMBL; AL359091; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471090; EAW87787.1; -; Genomic_DNA.
DR EMBL; CH471090; EAW87789.1; -; Genomic_DNA.
DR EMBL; BC011811; AAH11811.2; -; mRNA.
DR EMBL; BC098432; AAH98432.2; ALT_INIT; mRNA.
DR EMBL; BC108698; AAI08699.1; -; mRNA.
DR EMBL; BC119698; AAI19699.1; ALT_INIT; mRNA.
DR EMBL; BC119699; AAI19700.1; ALT_INIT; mRNA.
DR EMBL; AB040935; BAA96026.1; ALT_INIT; mRNA.
DR CCDS; CCDS6901.2; -. [Q5T4B2-1]
DR CCDS; CCDS69675.1; -. [Q5T4B2-2]
DR RefSeq; NP_001273689.1; NM_001286760.1. [Q5T4B2-2]
DR RefSeq; NP_057258.3; NM_016174.4. [Q5T4B2-1]
DR RefSeq; XP_005252092.1; XM_005252035.1. [Q5T4B2-1]
DR RefSeq; XP_011517064.1; XM_011518762.1. [Q5T4B2-1]
DR RefSeq; XP_011517065.1; XM_011518763.2. [Q5T4B2-2]
DR RefSeq; XP_016870283.1; XM_017014794.1. [Q5T4B2-1]
DR AlphaFoldDB; Q5T4B2; -.
DR SMR; Q5T4B2; -.
DR BioGRID; 119332; 165.
DR IntAct; Q5T4B2; 54.
DR STRING; 9606.ENSP00000361929; -.
DR CAZy; GT25; Glycosyltransferase Family 25.
DR GlyGen; Q5T4B2; 4 sites.
DR iPTMnet; Q5T4B2; -.
DR PhosphoSitePlus; Q5T4B2; -.
DR BioMuta; CERCAM; -.
DR EPD; Q5T4B2; -.
DR jPOST; Q5T4B2; -.
DR MassIVE; Q5T4B2; -.
DR MaxQB; Q5T4B2; -.
DR PaxDb; Q5T4B2; -.
DR PeptideAtlas; Q5T4B2; -.
DR PRIDE; Q5T4B2; -.
DR ProteomicsDB; 64440; -. [Q5T4B2-1]
DR ProteomicsDB; 64441; -. [Q5T4B2-2]
DR Antibodypedia; 17470; 114 antibodies from 23 providers.
DR DNASU; 51148; -.
DR Ensembl; ENST00000372838.9; ENSP00000361929.4; ENSG00000167123.20. [Q5T4B2-1]
DR Ensembl; ENST00000372842.5; ENSP00000361933.1; ENSG00000167123.20. [Q5T4B2-2]
DR GeneID; 51148; -.
DR KEGG; hsa:51148; -.
DR MANE-Select; ENST00000372838.9; ENSP00000361929.4; NM_016174.5; NP_057258.3.
DR UCSC; uc004buz.5; human. [Q5T4B2-1]
DR CTD; 51148; -.
DR GeneCards; CERCAM; -.
DR HGNC; HGNC:23723; CERCAM.
DR HPA; ENSG00000167123; Tissue enhanced (brain).
DR MIM; 616626; gene.
DR neXtProt; NX_Q5T4B2; -.
DR OpenTargets; ENSG00000167123; -.
DR PharmGKB; PA162382177; -.
DR VEuPathDB; HostDB:ENSG00000167123; -.
DR eggNOG; KOG4179; Eukaryota.
DR GeneTree; ENSGT01030000234558; -.
DR HOGENOM; CLU_024037_2_0_1; -.
DR InParanoid; Q5T4B2; -.
DR OMA; NRQRQGC; -.
DR OrthoDB; 931915at2759; -.
DR PhylomeDB; Q5T4B2; -.
DR TreeFam; TF313826; -.
DR PathwayCommons; Q5T4B2; -.
DR SignaLink; Q5T4B2; -.
DR BioGRID-ORCS; 51148; 21 hits in 1077 CRISPR screens.
DR ChiTaRS; CERCAM; human.
DR GenomeRNAi; 51148; -.
DR Pharos; Q5T4B2; Tdark.
DR PRO; PR:Q5T4B2; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q5T4B2; protein.
DR Bgee; ENSG00000167123; Expressed in C1 segment of cervical spinal cord and 143 other tissues.
DR ExpressionAtlas; Q5T4B2; baseline and differential.
DR Genevisible; Q5T4B2; HS.
DR GO; GO:0005788; C:endoplasmic reticulum lumen; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; NAS:ProtInc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0007155; P:cell adhesion; IDA:MGI.
DR GO; GO:0007159; P:leukocyte cell-cell adhesion; TAS:ProtInc.
DR CDD; cd06532; Glyco_transf_25; 1.
DR Gene3D; 3.90.550.10; -; 1.
DR InterPro; IPR002654; Glyco_trans_25.
DR InterPro; IPR029044; Nucleotide-diphossugar_trans.
DR Pfam; PF01755; Glyco_transf_25; 1.
DR SUPFAM; SSF53448; SSF53448; 1.
DR PROSITE; PS00014; ER_TARGET; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Endoplasmic reticulum; Glycoprotein;
KW Reference proteome; Signal.
FT SIGNAL 1..22
FT /evidence="ECO:0000255"
FT CHAIN 23..595
FT /note="Inactive glycosyltransferase 25 family member 3"
FT /id="PRO_0000309544"
FT REGION 548..595
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 592..595
FT /note="Prevents secretion from ER"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10138"
FT COMPBIAS 548..589
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 75
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 360
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10608765,
FT ECO:0000303|PubMed:10819331, ECO:0000303|PubMed:14702039"
FT /id="VSP_029234"
FT MUTAGEN 440
FT /note="S->D: No effect on lack of galactosyltransferase
FT activity in a chimeric construct with COLGALT1. Exhibits
FT some galactosyltransferase activity; when associated with
FT R-450; M-451; Q-452 and V-453 in a chimeric construct with
FT COLGALT1."
FT /evidence="ECO:0000269|PubMed:22216269"
FT MUTAGEN 450
FT /note="Q->R: Exhibits some galactosyltransferase activity;
FT when associated with D-440; M-451; Q-452 and V-453 in a
FT chimeric construct with COLGALT1."
FT /evidence="ECO:0000269|PubMed:22216269"
FT MUTAGEN 451
FT /note="V->M: Exhibits some galactosyltransferase activity;
FT when associated with D-440; R-450; Q-452 and V-453 in a
FT chimeric construct with COLGALT1."
FT /evidence="ECO:0000269|PubMed:22216269"
FT MUTAGEN 452
FT /note="N->Q: Exhibits some galactosyltransferase activity;
FT when associated with D-440; R-450; M-451 and V-453 in a
FT chimeric construct with COLGALT1."
FT /evidence="ECO:0000269|PubMed:22216269"
FT MUTAGEN 453
FT /note="P->V: Exhibits some galactosyltransferase activity;
FT when associated with D-440; R-450; M-451 and Q-452 in a
FT chimeric construct with COLGALT1."
FT /evidence="ECO:0000269|PubMed:22216269"
FT CONFLICT 209
FT /note="R -> H (in Ref. 5; AAI19700)"
FT /evidence="ECO:0000305"
FT CONFLICT 356..358
FT /note="GWM -> AGW (in Ref. 1; AAD51367)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 595 AA; 67592 MW; FC2157AD8C7AC558 CRC64;
MRAARAAPLL QLLLLLGPWL EAAGVAESPL PAVVLAILAR NAEHSLPHYL GALERLDYPR
ARMALWCATD HNVDNTTEML QEWLAAVGDD YAAVVWRPEG EPRFYPDEEG PKHWTKERHQ
FLMELKQEAL TFARNWGADY ILFADTDNIL TNNQTLRLLM GQGLPVVAPM LDSQTYYSNF
WCGITPQGYY RRTAEYFPTK NRQRRGCFRV PMVHSTFLAS LRAEGADQLA FYPPHPNYTW
PFDDIIVFAY ACQAAGVSVH VCNEHRYGYM NVPVKSHQGL EDERVNFIHL ILEALVDGPR
MQASAHVTRP SKRPSKIGFD EVFVISLARR PDRRERMLAS LWEMEISGRV VDAVDGWMLN
SSAIRNLGVD LLPGYQDPYS GRTLTKGEVG CFLSHYSIWE EVVARGLARV LVFEDDVRFE
SNFRGRLERL MEDVEAEKLS WDLIYLGRKQ VNPEKETAVE GLPGLVVAGY SYWTLAYALR
LAGARKLLAS QPLRRMLPVD EFLPIMFDQH PNEQYKAHFW PRDLVAFSAQ PLLAAPTHYA
GDAEWLSDTE TSSPWDDDSG RLISWSGSQK TLRSPRLDLT GSSGHSLQPQ PRDEL
