TMTC1_HUMAN
ID TMTC1_HUMAN Reviewed; 882 AA.
AC Q8IUR5; D0EP37; F5H8B5; Q6PIU4; Q6ZSM5; Q96N52; Q9BXM2;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 21-SEP-2011, sequence version 3.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Protein O-mannosyl-transferase TMTC1 {ECO:0000305};
DE EC=2.4.1.109 {ECO:0000269|PubMed:28973932};
DE AltName: Full=Transmembrane and TPR repeat-containing protein 1 {ECO:0000312|HGNC:HGNC:24099};
GN Name=TMTC1 {ECO:0000312|HGNC:HGNC:24099}; ORFNames=ARG99;
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 5).
RC TISSUE=Mammary gland;
RA Shen M.Q., Gu W.J., Fu H.L., Li J.M.;
RT "TMTC1A: A novel member of TPR motif family, as a potential chaperone of
RT HSP70 and HSP90.";
RL Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
RC TISSUE=Hippocampus;
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=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP LEU-814.
RC TISSUE=Pancreas, and Testis;
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 [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 704-882 (ISOFORMS 1/2/4/5).
RC TISSUE=Stomach cancer;
RA Yanqiu Z., Huazhang A., Fei L., Yongquan S., Xin W., Taidong Q., Baojun C.,
RA Kaichun W., Jie D., Daiming F.;
RT "Gene cloning of human adenocarcinoma cell line.";
RL Submitted (NOV-2000) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP INTERACTION WITH FAM168B.
RX PubMed=22771904; DOI=10.1016/j.febslet.2012.06.043;
RA Mishra M., Lee S., Lin M.K., Yamashita T., Heese K.;
RT "Characterizing the neurite outgrowth inhibitory effect of Mani.";
RL FEBS Lett. 586:3018-3023(2012).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=28973932; DOI=10.1073/pnas.1708319114;
RA Larsen I.S.B., Narimatsu Y., Joshi H.J., Siukstaite L., Harrison O.J.,
RA Brasch J., Goodman K.M., Hansen L., Shapiro L., Honig B., Vakhrushev S.Y.,
RA Clausen H., Halim A.;
RT "Discovery of an O-mannosylation pathway selectively serving cadherins and
RT protocadherins.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:11163-11168(2017).
CC -!- FUNCTION: Transfers mannosyl residues to the hydroxyl group of serine
CC or threonine residues. The 4 members of the TMTC family are O-mannosyl-
CC transferases dedicated primarily to the cadherin superfamily, each
CC member seems to have a distinct role in decorating the cadherin domains
CC with O-linked mannose glycans at specific regions. Also acts as O-
CC mannosyl-transferase on other proteins such as PDIA3.
CC {ECO:0000269|PubMed:28973932}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-seryl-[protein] = 3-
CC O-(alpha-D-mannosyl)-L-seryl-[protein] + a dolichyl phosphate + H(+);
CC Xref=Rhea:RHEA:17377, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:29999, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137321; EC=2.4.1.109;
CC Evidence={ECO:0000269|PubMed:28973932};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:17378;
CC Evidence={ECO:0000269|PubMed:28973932};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a dolichyl beta-D-mannosyl phosphate + L-threonyl-[protein] =
CC 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a dolichyl phosphate +
CC H(+); Xref=Rhea:RHEA:53396, Rhea:RHEA-COMP:9517, Rhea:RHEA-COMP:9527,
CC Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30013, ChEBI:CHEBI:57683, ChEBI:CHEBI:58211,
CC ChEBI:CHEBI:137323; EC=2.4.1.109;
CC Evidence={ECO:0000269|PubMed:28973932};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:53397;
CC Evidence={ECO:0000269|PubMed:28973932};
CC -!- PATHWAY: Protein modification; protein glycosylation.
CC {ECO:0000269|PubMed:28973932}.
CC -!- SUBUNIT: May interact with FAM168B. {ECO:0000269|PubMed:22771904}.
CC -!- INTERACTION:
CC Q8IUR5-4; Q86V38: ATN1; NbExp=3; IntAct=EBI-9089156, EBI-11954292;
CC Q8IUR5-4; Q9Y5Z0: BACE2; NbExp=3; IntAct=EBI-9089156, EBI-11282723;
CC Q8IUR5-4; P46379-2: BAG6; NbExp=3; IntAct=EBI-9089156, EBI-10988864;
CC Q8IUR5-4; P02489: CRYAA; NbExp=3; IntAct=EBI-9089156, EBI-6875961;
CC Q8IUR5-4; O14645: DNALI1; NbExp=3; IntAct=EBI-9089156, EBI-395638;
CC Q8IUR5-4; Q14204: DYNC1H1; NbExp=3; IntAct=EBI-9089156, EBI-356015;
CC Q8IUR5-4; O75460-2: ERN1; NbExp=3; IntAct=EBI-9089156, EBI-25852368;
CC Q8IUR5-4; P00488: F13A1; NbExp=3; IntAct=EBI-9089156, EBI-2565863;
CC Q8IUR5-4; P22607: FGFR3; NbExp=3; IntAct=EBI-9089156, EBI-348399;
CC Q8IUR5-4; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-9089156, EBI-10226858;
CC Q8IUR5-4; Q14957: GRIN2C; NbExp=3; IntAct=EBI-9089156, EBI-8285963;
CC Q8IUR5-4; P06396: GSN; NbExp=3; IntAct=EBI-9089156, EBI-351506;
CC Q8IUR5-4; P01112: HRAS; NbExp=3; IntAct=EBI-9089156, EBI-350145;
CC Q8IUR5-4; P04792: HSPB1; NbExp=3; IntAct=EBI-9089156, EBI-352682;
CC Q8IUR5-4; P42858: HTT; NbExp=6; IntAct=EBI-9089156, EBI-466029;
CC Q8IUR5-4; Q9Y2W7: KCNIP3; NbExp=3; IntAct=EBI-9089156, EBI-751501;
CC Q8IUR5-4; O60333-2: KIF1B; NbExp=3; IntAct=EBI-9089156, EBI-10975473;
CC Q8IUR5-4; O14901: KLF11; NbExp=3; IntAct=EBI-9089156, EBI-948266;
CC Q8IUR5-4; Q92876: KLK6; NbExp=3; IntAct=EBI-9089156, EBI-2432309;
CC Q8IUR5-4; Q9BVL2: NUP58; NbExp=3; IntAct=EBI-9089156, EBI-2811583;
CC Q8IUR5-4; D3DTS7: PMP22; NbExp=3; IntAct=EBI-9089156, EBI-25882629;
CC Q8IUR5-4; P60891: PRPS1; NbExp=3; IntAct=EBI-9089156, EBI-749195;
CC Q8IUR5-4; O76024: WFS1; NbExp=3; IntAct=EBI-9089156, EBI-720609;
CC Q8IUR5-4; Q9Y649; NbExp=3; IntAct=EBI-9089156, EBI-25900580;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}. Endoplasmic reticulum {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=5;
CC IsoId=Q8IUR5-5; Sequence=Displayed;
CC Name=1;
CC IsoId=Q8IUR5-1; Sequence=VSP_041823;
CC Name=2;
CC IsoId=Q8IUR5-2; Sequence=VSP_023612, VSP_023613;
CC Name=3;
CC IsoId=Q8IUR5-3; Sequence=VSP_041823, VSP_023614, VSP_023615,
CC VSP_023616;
CC Name=4;
CC IsoId=Q8IUR5-4; Sequence=VSP_023611, VSP_023617;
CC -!- SIMILARITY: Belongs to the TMTC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK32121.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; GQ865601; ACX30004.1; -; mRNA.
DR EMBL; AK055962; BAB71057.1; -; mRNA.
DR EMBL; AK127297; BAC86923.1; -; mRNA.
DR EMBL; AC009320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC009510; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC012151; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC022078; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC028716; AAH28716.1; -; mRNA.
DR EMBL; BC042083; AAH42083.1; -; mRNA.
DR EMBL; AF319520; AAK32121.1; ALT_INIT; mRNA.
DR CCDS; CCDS53772.1; -. [Q8IUR5-5]
DR CCDS; CCDS8718.1; -. [Q8IUR5-1]
DR RefSeq; NP_001180380.1; NM_001193451.1. [Q8IUR5-5]
DR RefSeq; NP_787057.2; NM_175861.3. [Q8IUR5-1]
DR AlphaFoldDB; Q8IUR5; -.
DR SMR; Q8IUR5; -.
DR BioGRID; 123773; 8.
DR IntAct; Q8IUR5; 27.
DR MINT; Q8IUR5; -.
DR STRING; 9606.ENSP00000442046; -.
DR GlyGen; Q8IUR5; 1 site.
DR iPTMnet; Q8IUR5; -.
DR PhosphoSitePlus; Q8IUR5; -.
DR BioMuta; TMTC1; -.
DR DMDM; 347595775; -.
DR EPD; Q8IUR5; -.
DR jPOST; Q8IUR5; -.
DR MassIVE; Q8IUR5; -.
DR MaxQB; Q8IUR5; -.
DR PaxDb; Q8IUR5; -.
DR PeptideAtlas; Q8IUR5; -.
DR PRIDE; Q8IUR5; -.
DR ProteomicsDB; 70599; -. [Q8IUR5-5]
DR ProteomicsDB; 70600; -. [Q8IUR5-1]
DR ProteomicsDB; 70601; -. [Q8IUR5-2]
DR ProteomicsDB; 70602; -. [Q8IUR5-3]
DR ProteomicsDB; 70603; -. [Q8IUR5-4]
DR Antibodypedia; 12772; 93 antibodies from 21 providers.
DR DNASU; 83857; -.
DR Ensembl; ENST00000256062.9; ENSP00000256062.5; ENSG00000133687.16. [Q8IUR5-1]
DR Ensembl; ENST00000539277.6; ENSP00000442046.1; ENSG00000133687.16. [Q8IUR5-5]
DR GeneID; 83857; -.
DR KEGG; hsa:83857; -.
DR MANE-Select; ENST00000539277.6; ENSP00000442046.1; NM_001193451.2; NP_001180380.1.
DR UCSC; uc001rjb.4; human. [Q8IUR5-5]
DR CTD; 83857; -.
DR DisGeNET; 83857; -.
DR GeneCards; TMTC1; -.
DR HGNC; HGNC:24099; TMTC1.
DR HPA; ENSG00000133687; Low tissue specificity.
DR MIM; 615855; gene.
DR neXtProt; NX_Q8IUR5; -.
DR OpenTargets; ENSG00000133687; -.
DR PharmGKB; PA142670718; -.
DR VEuPathDB; HostDB:ENSG00000133687; -.
DR eggNOG; KOG1124; Eukaryota.
DR GeneTree; ENSGT00940000158027; -.
DR HOGENOM; CLU_011615_1_1_1; -.
DR InParanoid; Q8IUR5; -.
DR OMA; YANFLMD; -.
DR PhylomeDB; Q8IUR5; -.
DR TreeFam; TF328339; -.
DR PathwayCommons; Q8IUR5; -.
DR SignaLink; Q8IUR5; -.
DR UniPathway; UPA00378; -.
DR BioGRID-ORCS; 83857; 8 hits in 1071 CRISPR screens.
DR ChiTaRS; TMTC1; human.
DR GenomeRNAi; 83857; -.
DR Pharos; Q8IUR5; Tbio.
DR PRO; PR:Q8IUR5; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8IUR5; protein.
DR Bgee; ENSG00000133687; Expressed in dorsal root ganglion and 186 other tissues.
DR ExpressionAtlas; Q8IUR5; baseline and differential.
DR Genevisible; Q8IUR5; HS.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000030; F:mannosyltransferase activity; IMP:UniProtKB.
DR GO; GO:0035269; P:protein O-linked mannosylation; IMP:UniProtKB.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR Gene3D; 1.25.40.10; -; 5.
DR InterPro; IPR003107; HAT.
DR InterPro; IPR013618; TMTC_DUF1736.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR013105; TPR_2.
DR InterPro; IPR019734; TPR_repeat.
DR Pfam; PF08409; DUF1736; 1.
DR Pfam; PF07719; TPR_2; 1.
DR Pfam; PF13181; TPR_8; 1.
DR SMART; SM00386; HAT; 3.
DR SMART; SM00028; TPR; 10.
DR SUPFAM; SSF48452; SSF48452; 2.
DR PROSITE; PS50005; TPR; 10.
DR PROSITE; PS50293; TPR_REGION; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Endoplasmic reticulum; Glycoprotein; Membrane;
KW Reference proteome; Repeat; TPR repeat; Transferase; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..882
FT /note="Protein O-mannosyl-transferase TMTC1"
FT /id="PRO_0000280288"
FT TRANSMEM 21..41
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 111..131
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 161..181
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 198..218
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 314..334
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 404..424
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 439..459
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REPEAT 483..516
FT /note="TPR 1"
FT REPEAT 518..547
FT /note="TPR 2"
FT REPEAT 548..581
FT /note="TPR 3"
FT REPEAT 583..615
FT /note="TPR 4"
FT REPEAT 616..649
FT /note="TPR 5"
FT REPEAT 650..683
FT /note="TPR 6"
FT REPEAT 684..716
FT /note="TPR 7"
FT REPEAT 751..784
FT /note="TPR 8"
FT REPEAT 789..822
FT /note="TPR 9"
FT REPEAT 823..856
FT /note="TPR 10"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 246..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 184
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..652
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023611"
FT VAR_SEQ 1..237
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023612"
FT VAR_SEQ 1..108
FT /note="Missing (in isoform 1 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_041823"
FT VAR_SEQ 238..312
FT /note="SNKQDKSSNGALCPRSPQQPGSPQPSSLPGHPHRENGKQQRFPHKGAWGGCH
FT SPLPPEPKSSGFPVSPRAVWSMM -> MTKQDSASKKKKKRYLRASSNRNFLLTMRPFL
FT KRAILVLSYVLVILYFRLWIMGGSMPLFSEQDNPASFSPYILT (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023613"
FT VAR_SEQ 312
FT /note="M -> MRYLRASSNRNFLLTMRPFLKRAILVLSYVLVILYFRLWIMGGSMPL
FT FSEQDNPASFSPYILT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023614"
FT VAR_SEQ 596..620
FT /note="ERFKEAEEIYQTGIKNCPDSSDLHN -> VIVSHSSFFQCYCYMYKLMLHRF
FT LY (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023615"
FT VAR_SEQ 621..882
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_023616"
FT VAR_SEQ 672..675
FT /note="WYKR -> C (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_023617"
FT VARIANT 814
FT /note="V -> L (in dbSNP:rs17854190)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_031112"
SQ SEQUENCE 882 AA; 98847 MW; 5E4E0B1453C8AAC0 CRC64;
MVVTTSARGG GGDRTPSRRR GCGLAPAGAA ALLAGASCLC YGRSLQGEFV HDDVWAIVNN
PDVRPGAPLR WGIFTNDFWG KGMAENTSHK SYRPLCVLTF KLNIFLTGMN PFYFHAVNII
LHCLVTLVLM YTCDKTVFKN RGLAFVTALL FAVHPIHTEA VAGIVGRADV LACLLFLLAF
LSYNRSLDQG CVGGSFPSTV SPFFLLLSLF LGTCAMLVKE TGITVFGVCL VYDLFSLSNK
QDKSSNGALC PRSPQQPGSP QPSSLPGHPH RENGKQQRFP HKGAWGGCHS PLPPEPKSSG
FPVSPRAVWS MMRFLTYSYL LAFNVWLLLA PVTLCYDWQV GSIPLVETIW DMRNLATIFL
AVVMALLSLH CLAAFKRLEH KEVLVGLLFL VFPFIPASNL FFRVGFVVAE RVLYMPSMGY
CILFVHGLSK LCTWLNRCGA TTLIVSTVLL LLLFSWKTVK QNEIWLSRES LFRSGVQTLP
HNAKVHYNYA NFLKDQGRNK EAIYHYRTAL KLYPRHASAL NNLGTLTRDT AEAKMYYQRA
LQLHPQHNRA LFNLGNLLKS QEKKEEAITL LKDSIKYGPE FADAYSSLAS LLAEQERFKE
AEEIYQTGIK NCPDSSDLHN NYGVFLVDTG LPEKAVAHYQ QAIKLSPSHH VAMVNLGRLY
RSLGENSMAE EWYKRALQVA HKAEILSPLG ALYYNTGRYE EALQIYQEAA ALQPSQRELR
LALAQVLAVM GQTKEAEKMT NHIVSEETGC LECYRLLSAI YSKQENHDKA LDAIDKALQL
KPKDPKVISE LFFTKGNQLR EQNLLDKAFE SYRVAVQLNP DQAQAWMNMG GIQHIKGKYV
SARAYYERAL QLVPDSKLLK ENLAKLDRLE KRLQEVREKD QT
