TTLL3_HUMAN
ID TTLL3_HUMAN Reviewed; 772 AA.
AC Q9Y4R7; Q4KMS8; Q6AWA3; Q6ZU95; Q8NDN8; Q96GG8; Q9H876; Q9UI99;
DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 162.
DE RecName: Full=Tubulin monoglycylase TTLL3 {ECO:0000250|UniProtKB:A4Q9E5};
DE EC=6.3.2.- {ECO:0000250|UniProtKB:A4Q9E5};
DE AltName: Full=HOTTL;
DE AltName: Full=Tubulin--tyrosine ligase-like protein 3;
GN Name=TTLL3 {ECO:0000312|HGNC:HGNC:24483}; ORFNames=PRO0207;
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 [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ARG-502.
RC TISSUE=Cervix, Testis, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP ARG-502.
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-744 (ISOFORM 1), AND VARIANT
RP ARG-502.
RC TISSUE=Thyroid;
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] (ISOFORM 4).
RC TISSUE=Fetal liver;
RA Yu Y., Zhang C., Luo L., Ouyang S., Zhang S., Li W., Wu J., Zhou S.,
RA Liu M., He F.;
RT "Functional prediction of the coding sequences of 50 new genes deduced by
RT analysis of cDNA clones from human fetal liver.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25180231; DOI=10.15252/embj.201488466;
RA Rocha C., Papon L., Cacheux W., Marques Sousa P., Lascano V., Tort O.,
RA Giordano T., Vacher S., Lemmers B., Mariani P., Meseure D., Medema J.P.,
RA Bieche I., Hahne M., Janke C.;
RT "Tubulin glycylases are required for primary cilia, control of cell
RT proliferation and tumor development in colon.";
RL EMBO J. 33:2247-2260(2014).
RN [7]
RP VARIANTS [LARGE SCALE ANALYSIS] SER-454 AND ILE-476.
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: Monoglycylase which modifies alpha- and beta-tubulin, adding
CC a single glycine on the gamma-carboxyl groups of specific glutamate
CC residues to generate monoglycine side chains within the C-terminal tail
CC of tubulin. Not involved in elongation step of the polyglycylation
CC reaction (By similarity). Preferentially glycylates a beta-tail peptide
CC over the alpha-tail, although shifts its preference toward alpha-tail
CC as beta-tail glutamylation increases (By similarity). Competes with
CC polyglutamylases for modification site on beta-tubulin substrate,
CC thereby creating an anticorrelation between glycylation and
CC glutamylation reactions (By similarity). Together with TTLL8, mediates
CC microtubule glycylation of primary and motile cilia, which is essential
CC for their stability and maintenance (By similarity). Involved in
CC microtubule glycylation of primary cilia in colon which controls cell
CC proliferation of epithelial cells and plays an essential role in colon
CC cancer development (PubMed:25180231). Together with TTLL8, glycylates
CC sperm flagella which regulates axonemal dynein motor activity, thereby
CC controlling flagellar beat, directional sperm swimming and male
CC fertility (By similarity). {ECO:0000250|UniProtKB:A4Q9E5,
CC ECO:0000250|UniProtKB:B2GUB3, ECO:0000269|PubMed:25180231}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + glycine + L-glutamyl-[protein] = ADP + glycyl-L-
CC glutamyl-[protein] + H(+) + phosphate; Xref=Rhea:RHEA:67180,
CC Rhea:RHEA-COMP:10208, Rhea:RHEA-COMP:17207, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29973, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:57305, ChEBI:CHEBI:167890, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E5};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67181;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E5};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:A4Q9E8};
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:25180231}. Cell projection, cilium
CC {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:A4Q9E5}. Cytoplasm, cytoskeleton, flagellum
CC axoneme {ECO:0000250|UniProtKB:A4Q9E5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9Y4R7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4R7-2; Sequence=VSP_032568, VSP_032572, VSP_032573;
CC Name=3;
CC IsoId=Q9Y4R7-5; Sequence=VSP_032568, VSP_032576, VSP_032577;
CC Name=4;
CC IsoId=Q9Y4R7-6; Sequence=VSP_032567, VSP_032572, VSP_032573;
CC -!- TISSUE SPECIFICITY: Expressed in brain, heart, kidney, testis, liver,
CC lung, muscle, spleen, trachea and colon. {ECO:0000269|PubMed:25180231}.
CC -!- DOMAIN: Two conserved structural elements specific among
CC monoglycylases, IS1 and IS2, are involved in glycyl chains initiation.
CC Two conserved structural interfaces likely constitute the binding
CC platforms for tubulin tail and microtubule.
CC {ECO:0000250|UniProtKB:B2GUB3}.
CC -!- DOMAIN: Arg-289 is the main determinant for regioselectivity, which
CC segregates between initiases and elongases in all tubulin--tyrosine
CC ligase family. A glutamine residue at this position is found in
CC elongases TTLL6, TTLL9, TTLL11, TTLL13, TTLL10 and favors glutamate-
CC chain elongation, whereas an arginine residue is found in initiases
CC TTLL2, TTLL4, TTLL5, TTLL3, TTLL8 and favors initiation.
CC {ECO:0000250|UniProtKB:A4Q9E8}.
CC -!- CAUTION: TTLL3 and TTLL8 monoglycylase-mediated glycylation of tubulin
CC was initially reported to play a role in ependymal motile ciliary
CC maintenance (By similarity). However, contradictory results were later
CC observed (By similarity). {ECO:0000250|UniProtKB:A4Q9E5}.
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DR EMBL; AL096725; CAB46375.1; -; mRNA.
DR EMBL; AL833939; CAD38794.1; -; mRNA.
DR EMBL; BX648175; CAH10554.1; -; mRNA.
DR EMBL; AC022382; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC098298; AAH98298.1; -; mRNA.
DR EMBL; BC098361; AAH98361.1; -; mRNA.
DR EMBL; BC099735; AAH99735.1; -; mRNA.
DR EMBL; BC105638; AAI05639.1; -; mRNA.
DR EMBL; AK023960; BAB14741.1; -; mRNA.
DR EMBL; AF078842; AAF23353.1; -; mRNA.
DR PIR; T12515; T12515.
DR RefSeq; NP_001021100.3; NM_001025930.3.
DR AlphaFoldDB; Q9Y4R7; -.
DR SMR; Q9Y4R7; -.
DR BioGRID; 117575; 15.
DR IntAct; Q9Y4R7; 9.
DR STRING; 9606.ENSP00000392549; -.
DR DrugBank; DB00277; Theophylline.
DR iPTMnet; Q9Y4R7; -.
DR PhosphoSitePlus; Q9Y4R7; -.
DR SwissPalm; Q9Y4R7; -.
DR BioMuta; TTLL3; -.
DR DMDM; 172046606; -.
DR MassIVE; Q9Y4R7; -.
DR MaxQB; Q9Y4R7; -.
DR PaxDb; Q9Y4R7; -.
DR PeptideAtlas; Q9Y4R7; -.
DR PRIDE; Q9Y4R7; -.
DR ProteomicsDB; 86244; -. [Q9Y4R7-1]
DR TopDownProteomics; Q9Y4R7-5; -. [Q9Y4R7-5]
DR Antibodypedia; 34894; 36 antibodies from 13 providers.
DR DNASU; 26140; -.
DR Ensembl; ENST00000383827.5; ENSP00000373338.1; ENSG00000214021.17. [Q9Y4R7-2]
DR Ensembl; ENST00000426895.10; ENSP00000392549.5; ENSG00000214021.17. [Q9Y4R7-1]
DR Ensembl; ENST00000430793.1; ENSP00000403874.1; ENSG00000214021.17. [Q9Y4R7-5]
DR Ensembl; ENST00000438141.5; ENSP00000409246.1; ENSG00000214021.17. [Q9Y4R7-2]
DR GeneID; 26140; -.
DR KEGG; hsa:26140; -.
DR UCSC; uc003bti.5; human. [Q9Y4R7-1]
DR CTD; 26140; -.
DR DisGeNET; 26140; -.
DR GeneCards; TTLL3; -.
DR HGNC; HGNC:24483; TTLL3.
DR HPA; ENSG00000214021; Low tissue specificity.
DR MIM; 619195; gene.
DR neXtProt; NX_Q9Y4R7; -.
DR OpenTargets; ENSG00000214021; -.
DR PharmGKB; PA134942870; -.
DR VEuPathDB; HostDB:ENSG00000214021; -.
DR eggNOG; KOG2157; Eukaryota.
DR GeneTree; ENSGT00940000154857; -.
DR HOGENOM; CLU_633064_0_0_1; -.
DR InParanoid; Q9Y4R7; -.
DR OrthoDB; 1137333at2759; -.
DR PhylomeDB; Q9Y4R7; -.
DR PathwayCommons; Q9Y4R7; -.
DR Reactome; R-HSA-8955332; Carboxyterminal post-translational modifications of tubulin.
DR SignaLink; Q9Y4R7; -.
DR BioGRID-ORCS; 26140; 12 hits in 1076 CRISPR screens.
DR ChiTaRS; TTLL3; human.
DR GeneWiki; TTLL3; -.
DR GenomeRNAi; 26140; -.
DR Pharos; Q9Y4R7; Tbio.
DR PRO; PR:Q9Y4R7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y4R7; protein.
DR Bgee; ENSG00000214021; Expressed in right uterine tube and 156 other tissues.
DR ExpressionAtlas; Q9Y4R7; baseline and differential.
DR Genevisible; Q9Y4R7; HS.
DR GO; GO:0005930; C:axoneme; ISS:UniProtKB.
DR GO; GO:0005929; C:cilium; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005874; C:microtubule; IEA:UniProtKB-KW.
DR GO; GO:0015630; C:microtubule cytoskeleton; ISS:UniProtKB.
DR GO; GO:0036126; C:sperm flagellum; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0070735; F:protein-glycine ligase activity; IDA:UniProtKB.
DR GO; GO:0070736; F:protein-glycine ligase activity, initiating; ISS:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR GO; GO:0060271; P:cilium assembly; ISS:UniProtKB.
DR GO; GO:0003341; P:cilium movement; IBA:GO_Central.
DR GO; GO:0030317; P:flagellated sperm motility; ISS:UniProtKB.
DR GO; GO:0018094; P:protein polyglycylation; TAS:Reactome.
DR InterPro; IPR004344; TTL/TTLL_fam.
DR InterPro; IPR027753; TTLL3.
DR PANTHER; PTHR45870:SF1; PTHR45870:SF1; 3.
DR Pfam; PF03133; TTL; 1.
DR PROSITE; PS51221; TTL; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Cell projection; Cilium; Cytoplasm;
KW Cytoskeleton; Flagellum; Ligase; Magnesium; Metal-binding; Microtubule;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..772
FT /note="Tubulin monoglycylase TTLL3"
FT /id="PRO_0000212441"
FT DOMAIN 151..510
FT /note="TTL"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00568"
FT REGION 50..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 65..81
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 289..290
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 289
FT /ligand="a protein"
FT /ligand_id="ChEBI:CHEBI:16541"
FT /ligand_part="L-glutamate residue"
FT /ligand_part_id="ChEBI:CHEBI:29973"
FT /ligand_part_note="L-glutamate acceptor residue in protein
FT target"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 321..324
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:B2GUB3"
FT BINDING 334..336
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 378..379
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 456
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 469
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250|UniProtKB:B2GUB3"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 469
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT BINDING 471
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT SITE 289
FT /note="Essential for specifying initiation versus
FT elongation step of the glycylase activity"
FT /evidence="ECO:0000250|UniProtKB:A4Q9E8"
FT VAR_SEQ 1..272
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_032567"
FT VAR_SEQ 1..212
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_032568"
FT VAR_SEQ 520..564
FT /note="AVEVPQYVGIRLLVEGFTIKKPMAMCHRRMGVRPAVPLLTQRGSG -> VTT
FT SPASTPRPSCLLPMYSDTRARSSDDSTASWWALRPCRPQARP (in isoform 2
FT and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.5"
FT /id="VSP_032572"
FT VAR_SEQ 565..772
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.5"
FT /id="VSP_032573"
FT VAR_SEQ 642..646
FT /note="APALL -> VGLDL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_032576"
FT VAR_SEQ 647..772
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005"
FT /id="VSP_032577"
FT VARIANT 174
FT /note="E -> K (in dbSNP:rs3806669)"
FT /id="VAR_052410"
FT VARIANT 418
FT /note="N -> H (in dbSNP:rs2290302)"
FT /id="VAR_052411"
FT VARIANT 454
FT /note="G -> S (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036054"
FT VARIANT 476
FT /note="M -> I (in a colorectal cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036055"
FT VARIANT 502
FT /note="M -> R (in dbSNP:rs2290305)"
FT /evidence="ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:17974005"
FT /id="VAR_020207"
FT VARIANT 689
FT /note="A -> T (in dbSNP:rs1057278)"
FT /id="VAR_052412"
FT CONFLICT 279
FT /note="I -> F (in Ref. 5; AAF23353)"
FT /evidence="ECO:0000305"
FT CONFLICT Q9Y4R7-2:317
FT /note="R -> G (in Ref. 1; CAH10554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 772 AA; 87414 MW; C89074C5E98E15C1 CRC64;
MNRLRNAKIY VERAVKQKKI FTIQGCYPVI RCLLRRRGWV EKKMVHRSGP TLLPPQKDLD
SSAMGDSDTT EDEDEDEDEE FQPSQLFDFD DLLKFDDLDG THALMVGLCL NLRNLPWFDE
VDANSFFPRC YCLGAEDDKK AFIEDFWLTA ARNVLKLVVK SEWKSYPIQA VEEEASGDKQ
PKKQEKNPVL VSPEFVDEAL CACEEYLSNL AHMDIDKDLE APLYLTPEGW SLFLQRYYQV
VHEGAELRHL DTQVQRCEDI LQQLQAVVPQ IDMEGDRNIW IVKPGAKSRG RGIMCMDHLE
EMLKLVNGNP VVMKDGKWVV QKYIERPLLI FGTKFDLRQW FLVTDWNPLT VWFYRDSYIR
FSTQPFSLKN LDNSVHLCNN SIQKHLENSC HRHPLLPPDN MWSSQRFQAH LQEMGAPNAW
STIIVPGMKD AVIHALQTSQ DTVQCRKASF ELYGADFVFG EDFQPWLIEI NASPTMAPST
AVTARLCAGV QADTLRVVID RMLDRNCDTG AFELIYKQPA VEVPQYVGIR LLVEGFTIKK
PMAMCHRRMG VRPAVPLLTQ RGSGEARHHF PSLHTKAQLP SPHVLRHQGQ VLRRQHSKLV
GTKALSTTGK ALRTLPTAKV FISLPPNLDF KVAPSILKPR KAPALLCLRG PQLEVPCCLC
PLKSEQFLAP VGRSRPKANS RPDCDKPRAE ACPMKRLSPL KPLPLVGTFQ RRRGLGDMKL
GKPLLRFPTA LVLDPTPNKK KQVKYLGLDS IAVGGSRVDG ARPCTPGSTA RA
