ID   TMTC3_HUMAN             Reviewed;         915 AA.
AC   Q6ZXV5; Q5CZ86; Q5H9T6; Q68DQ6; Q68DX0; Q7Z332; Q8NC50;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-MAR-2007, sequence version 2.
DT   09-APR-2025, entry version 161.
DE   RecName: Full=Protein O-mannosyl-transferase TMTC3 {ECO:0000305};
DE            EC=2.4.1.109 {ECO:0000269|PubMed:28973932};
DE   AltName: Full=Protein SMILE {ECO:0000303|PubMed:17974005};
DE   AltName: Full=Transmembrane O-mannosyltransferase targeting cadherins 3 {ECO:0000312|HGNC:HGNC:26899};
DE   AltName: Full=Transmembrane and tetratricopeptide repeat-containing 3 {ECO:0000312|HGNC:HGNC:26899};
GN   Name=TMTC3 {ECO:0000312|HGNC:HGNC:26899};
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).
RC   TISSUE=Tooth;
RA   Bleicher F., Heidet E., Carrouel F., Couble M.L., Magloire H.;
RT   "SMILE, a new gene expressed by human odontoblasts.";
RL   Submitted (APR-2004) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Amygdala, Endometrial tumor, Uterine endothelium, 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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Colon;
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 52-876 (ISOFORM 2).
RC   TISSUE=Teratocarcinoma;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-503, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=21603654; DOI=10.1371/journal.pone.0019321;
RA   Racape M., Duong Van Huyen J.P., Danger R., Giral M., Bleicher F.,
RA   Foucher Y., Pallier A., Pilet P., Tafelmeyer P., Ashton-Chess J.,
RA   Dugast E., Pettre S., Charreau B., Soulillou J.P., Brouard S.;
RT   "The involvement of SMILE/TMTC3 in endoplasmic reticulum stress response.";
RL   PLoS ONE 6:E19321-E19321(2011).
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).
RN   [8]
RP   INVOLVEMENT IN LIS8, AND VARIANTS LIS8 ASP-67 AND GLU-384.
RX   PubMed=27773428; DOI=10.1016/j.ajhg.2016.09.007;
RA   Jerber J., Zaki M.S., Al-Aama J.Y., Rosti R.O., Ben-Omran T., Dikoglu E.,
RA   Silhavy J.L., Caglar C., Musaev D., Albrecht B., Campbell K.P., Willer T.,
RA   Almuriekhi M., Caglayan A.O., Vajsar J., Bilguevar K., Ogur G.,
RA   Abou Jamra R., Guenel M., Gleeson J.G.;
RT   "Biallelic mutations in TMTC3, encoding a transmembrane and TPR-containing
RT   protein, lead to cobblestone lissencephaly.";
RL   Am. J. Hum. Genet. 99:1181-1189(2016).
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 (PubMed:28973932).
CC       Involved in the positive regulation of proteasomal protein degradation
CC       in the endoplasmic reticulum (ER), and the control of ER stress
CC       response. {ECO:0000269|PubMed:21603654, ECO:0000269|PubMed:28973932}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L-
CC         seryl-[protein] = 3-O-(alpha-D-mannosyl)-L-seryl-[protein] + a di-
CC         trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:17377,
CC         Rhea:RHEA-COMP:9863, Rhea:RHEA-COMP:13546, Rhea:RHEA-COMP:19498,
CC         Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137321;
CC         EC=2.4.1.109; 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 di-trans,poly-cis-dolichyl beta-D-mannosyl phosphate + L-
CC         threonyl-[protein] = 3-O-(alpha-D-mannosyl)-L-threonyl-[protein] + a
CC         di-trans,poly-cis-dolichyl phosphate + H(+); Xref=Rhea:RHEA:53396,
CC         Rhea:RHEA-COMP:11060, Rhea:RHEA-COMP:13547, Rhea:RHEA-COMP:19498,
CC         Rhea:RHEA-COMP:19501, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC         ChEBI:CHEBI:57683, ChEBI:CHEBI:58211, ChEBI:CHEBI:137323;
CC         EC=2.4.1.109; 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   -!- INTERACTION:
CC       Q6ZXV5; O75553: DAB1; NbExp=3; IntAct=EBI-10188441, EBI-7875264;
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000255}; Multi-pass membrane
CC       protein {ECO:0000255}. Endoplasmic reticulum
CC       {ECO:0000269|PubMed:21603654}. Note=In odontoblast cultures, it
CC       colocalizes with PDIA3 in the endoplasmic reticulum.
CC       {ECO:0000269|PubMed:21603654}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZXV5-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZXV5-2; Sequence=VSP_023619;
CC   -!- DISEASE: Lissencephaly 8 (LIS8) [MIM:617255]: A form of lissencephaly,
CC       a disorder of cortical development characterized by agyria or
CC       pachygyria and disorganization of the clear neuronal lamination of
CC       normal six-layered cortex. LIS8 patients manifest delayed psychomotor
CC       development, intellectual disability with poor or absent speech, early-
CC       onset refractory seizures, hypotonia, cortical gyral abnormalities, and
CC       hypoplasia of the corpus callosum, brainstem and cerebellum. LIS8
CC       inheritance is autosomal recessive. {ECO:0000269|PubMed:27773428}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
CC   -!- SIMILARITY: Belongs to the TMTC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAC11325.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AJ697717; CAG26973.1; -; mRNA.
DR   EMBL; BX538169; CAD98046.1; -; mRNA.
DR   EMBL; CR749244; CAH18100.1; -; mRNA.
DR   EMBL; CR749309; CAH18164.1; -; mRNA.
DR   EMBL; CR933632; CAI45938.1; -; mRNA.
DR   EMBL; CR936640; CAI56780.1; -; mRNA.
DR   EMBL; BC117175; AAI17176.1; -; mRNA.
DR   EMBL; BC117177; AAI17178.1; -; mRNA.
DR   EMBL; AK074973; BAC11325.1; ALT_INIT; mRNA.
DR   CCDS; CCDS9032.1; -. [Q6ZXV5-2]
DR   RefSeq; NP_861448.2; NM_181783.4. [Q6ZXV5-2]
DR   AlphaFoldDB; Q6ZXV5; -.
DR   SMR; Q6ZXV5; -.
DR   BioGRID; 127757; 135.
DR   IntAct; Q6ZXV5; 37.
DR   MINT; Q6ZXV5; -.
DR   STRING; 9606.ENSP00000266712; -.
DR   ChEMBL; CHEMBL5465323; -.
DR   TCDB; 8.A.95.1.1; the transmembrane and tpr repeat-containing protein 3 (tmtc3) family.
DR   GlyCosmos; Q6ZXV5; 5 sites, 3 glycans.
DR   GlyGen; Q6ZXV5; 6 sites, 14 N-linked glycans (2 sites), 2 O-linked glycans (3 sites).
DR   iPTMnet; Q6ZXV5; -.
DR   PhosphoSitePlus; Q6ZXV5; -.
DR   SwissPalm; Q6ZXV5; -.
DR   BioMuta; TMTC3; -.
DR   DMDM; 134035047; -.
DR   jPOST; Q6ZXV5; -.
DR   MassIVE; Q6ZXV5; -.
DR   PaxDb; 9606-ENSP00000266712; -.
DR   PeptideAtlas; Q6ZXV5; -.
DR   ProteomicsDB; 68498; -. [Q6ZXV5-1]
DR   ProteomicsDB; 68499; -. [Q6ZXV5-2]
DR   Pumba; Q6ZXV5; -.
DR   Antibodypedia; 52318; 34 antibodies from 12 providers.
DR   DNASU; 160418; -.
DR   Ensembl; ENST00000266712.11; ENSP00000266712.6; ENSG00000139324.12. [Q6ZXV5-2]
DR   GeneID; 160418; -.
DR   KEGG; hsa:160418; -.
DR   MANE-Select; ENST00000266712.11; ENSP00000266712.6; NM_181783.4; NP_861448.2. [Q6ZXV5-2]
DR   UCSC; uc001tau.3; human. [Q6ZXV5-1]
DR   AGR; HGNC:26899; -.
DR   CTD; 160418; -.
DR   DisGeNET; 160418; -.
DR   GeneCards; TMTC3; -.
DR   HGNC; HGNC:26899; TMTC3.
DR   HPA; ENSG00000139324; Low tissue specificity.
DR   MalaCards; TMTC3; -.
DR   MIM; 617218; gene.
DR   MIM; 617255; phenotype.
DR   neXtProt; NX_Q6ZXV5; -.
DR   OpenTargets; ENSG00000139324; -.
DR   Orphanet; 98892; Periventricular nodular heterotopia.
DR   PharmGKB; PA142670720; -.
DR   VEuPathDB; HostDB:ENSG00000139324; -.
DR   eggNOG; KOG1124; Eukaryota.
DR   GeneTree; ENSGT00940000157538; -.
DR   HOGENOM; CLU_011615_1_0_1; -.
DR   InParanoid; Q6ZXV5; -.
DR   OMA; AKACFTR; -.
DR   OrthoDB; 66906at2759; -.
DR   PhylomeDB; Q6ZXV5; -.
DR   TreeFam; TF328339; -.
DR   PathwayCommons; Q6ZXV5; -.
DR   SignaLink; Q6ZXV5; -.
DR   UniPathway; UPA00378; -.
DR   BioGRID-ORCS; 160418; 24 hits in 1156 CRISPR screens.
DR   ChiTaRS; TMTC3; human.
DR   GenomeRNAi; 160418; -.
DR   Pharos; Q6ZXV5; Tdark.
DR   PRO; PR:Q6ZXV5; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q6ZXV5; protein.
DR   Bgee; ENSG00000139324; Expressed in endothelial cell and 192 other cell types or tissues.
DR   ExpressionAtlas; Q6ZXV5; baseline and differential.
DR   GO; GO:0005783; C:endoplasmic reticulum; IDA:UniProtKB.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IMP:UniProtKB.
DR   GO; GO:0000030; F:mannosyltransferase activity; IBA:GO_Central.
DR   GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IMP:UniProtKB.
DR   GO; GO:0035269; P:protein O-linked mannosylation; IMP:UniProtKB.
DR   GO; GO:0034976; P:response to endoplasmic reticulum stress; IMP:UniProtKB.
DR   FunFam; 1.25.40.10:FF:000239; Transmembrane and TPR repeat-containing protein 3; 1.
DR   FunFam; 1.25.40.10:FF:000528; Transmembrane and TPR repeat-containing protein 3; 1.
DR   FunFam; 1.25.40.10:FF:000175; transmembrane and TPR repeat-containing protein 3; 1.
DR   Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 4.
DR   InterPro; IPR013618; TMTC_DUF1736.
DR   InterPro; IPR011990; TPR-like_helical_dom_sf.
DR   InterPro; IPR019734; TPR_rpt.
DR   PANTHER; PTHR44395; -; 1.
DR   PANTHER; PTHR44395:SF1; PROTEIN O-MANNOSYL-TRANSFERASE TMTC3; 1.
DR   Pfam; PF08409; TMTC_DUF1736; 1.
DR   Pfam; PF13431; TPR_17; 1.
DR   Pfam; PF13181; TPR_8; 4.
DR   SMART; SM00028; TPR; 9.
DR   SUPFAM; SSF48452; TPR-like; 2.
DR   PROSITE; PS50005; TPR; 9.
DR   PROSITE; PS50293; TPR_REGION; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Disease variant; Endoplasmic reticulum; Glycoprotein;
KW   Lissencephaly; Membrane; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Repeat; TPR repeat; Transferase; Transmembrane;
KW   Transmembrane helix.
FT   CHAIN           1..915
FT                   /note="Protein O-mannosyl-transferase TMTC3"
FT                   /id="PRO_0000280293"
FT   TOPO_DOM        1..8
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        9..29
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        30..93
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        115..120
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        121..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        140..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        159..166
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        188..193
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        194..214
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        215..231
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        232..252
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        253..317
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        318..338
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        339..353
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        354..374
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        375..376
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        377..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        398..404
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000305"
FT   TRANSMEM        405..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        424..915
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000305"
FT   REPEAT          446..479
FT                   /note="TPR 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REPEAT          480..513
FT                   /note="TPR 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REPEAT          529..562
FT                   /note="TPR 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REPEAT          563..596
FT                   /note="TPR 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REPEAT          597..631
FT                   /note="TPR 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REPEAT          669..702
FT                   /note="TPR 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REPEAT          703..736
FT                   /note="TPR 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REPEAT          738..771
FT                   /note="TPR 8"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REPEAT          772..805
FT                   /note="TPR 9"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00339"
FT   REGION          848..892
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        865..874
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        878..892
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         503
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   CARBOHYD        494
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        541
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   CARBOHYD        865
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT   VAR_SEQ         618
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT                   ECO:0000303|Ref.1"
FT                   /id="VSP_023619"
FT   VARIANT         67
FT                   /note="H -> D (in LIS8)"
FT                   /evidence="ECO:0000269|PubMed:27773428"
FT                   /id="VAR_077900"
FT   VARIANT         384
FT                   /note="G -> E (in LIS8)"
FT                   /evidence="ECO:0000269|PubMed:27773428"
FT                   /id="VAR_077901"
FT   CONFLICT        120
FT                   /note="S -> R (in Ref. 2; CAH18164)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        158
FT                   /note="S -> P (in Ref. 3; BAC11325)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        201
FT                   /note="Y -> C (in Ref. 3; BAC11325)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        348
FT                   /note="V -> G (in Ref. 2; CAD98046)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        489
FT                   /note="T -> A (in Ref. 2; CAH18100)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        538
FT                   /note="I -> V (in Ref. 2; CAI45938)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        639
FT                   /note="A -> V (in Ref. 2; CAD98046)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        864
FT                   /note="D -> N (in Ref. 2; CAD98046)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        883
FT                   /note="T -> A (in Ref. 2; CAD98046)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   915 AA;  104009 MW;  2B6787CE1B7CB83C CRC64;
     MANINLKEIT LIVGVVTACY WNSLFCGFVF DDVSAILDNK DLHPSTPLKT LFQNDFWGTP
     MSEERSHKSY RPLTVLTFRL NYLLSELKPM SYHLLNMIFH AVVSVIFLKV CKLFLDNKSS
     VIASLLFAVH PIHTEAVTGV VGRAELLSSI FFLAAFLSYT RSKGPDNSII WTPIALTVFL
     VAVATLCKEQ GITVVGICCV YEVFIAQGYT LPLLCTTAGQ FLRGKGSIPF SMLQTLVKLI
     VLMFSTLLLV VIRVQVIQSQ LPVFTRFDNP AAVSPTPTRQ LTFNYLLPVN AWLLLNPSEL
     CCDWTMGTIP LIESLLDIRN LATFTFFCFL GMLGVFSIRY SGDSSKTVLM ALCLMALPFI
     PASNLFFPVG FVVAERVLYV PSMGFCILVA HGWQKISTKS VFKKLSWICL SMVILTHSLK
     TFHRNWDWES EYTLFMSALK VNKNNAKLWN NVGHALENEK NFERALKYFL QATHVQPDDI
     GAHMNVGRTY KNLNRTKEAE ESYMMAKSLM PQIIPGKKYA ARIAPNHLNV YINLANLIRA
     NESRLEEADQ LYRQAISMRP DFKQAYISRG ELLLKMNKPL KAKEAYLKAL ELDRNNADLW
     YNLAIVHIEL KEPNEALKKN FNRALELNPK HKLALFNSAI VMQESGEVKL RPEARKRLLS
     YINEEPLDAN GYFNLGMLAM DDKKDNEAEI WMKKAIKLQA DFRSALFNLA LLYSQTAKEL
     KALPILEELL RYYPDHIKGL ILKGDILMNQ KKDILGAKKC FERILEMDPS NVQGKHNLCV
     VYFEEKDLLK AERCLLETLA LAPHEEYIQR HLNIVRDKIS SSSFIEPIFP TSKISSVEGK
     KIPTESVKEI RGESRQTQIV KTSDNKSQSK SNKQLGKNGD EETPHKTTKD IKEIEKKRVA
     ALKRLEEIER ILNGE
//