CADM3_HUMAN
ID CADM3_HUMAN Reviewed; 398 AA.
AC Q8N126; Q8IZQ9; Q9NVJ5; Q9UJP1;
DT 07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Cell adhesion molecule 3;
DE AltName: Full=Brain immunoglobulin receptor;
DE AltName: Full=Immunoglobulin superfamily member 4B;
DE Short=IgSF4B;
DE AltName: Full=Nectin-like protein 1;
DE Short=NECL-1;
DE AltName: Full=Synaptic cell adhesion molecule 3;
DE Short=SynCAM3;
DE AltName: Full=TSLC1-like protein 1;
DE Short=TSLL1;
DE Flags: Precursor;
GN Name=CADM3; Synonyms=IGSF4B, NECL1, SYNCAM3, TSLL1; ORFNames=UNQ225/PRO258;
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), TISSUE SPECIFICITY, AND INDUCTION.
RX PubMed=11536053; DOI=10.1038/sj.onc.1204696;
RA Fukuhara H., Kuramochi M., Nobukuni T., Fukami T., Saino M., Maruyama T.,
RA Nomura S., Sekiya T., Murakami Y.;
RT "Isolation of the TSLL1 and TSLL2 genes, members of the tumor suppressor
RT TSLC1 gene family encoding transmembrane proteins.";
RL Oncogene 20:5401-5407(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RX PubMed=15893517; DOI=10.1016/j.bbamem.2005.01.013;
RA Zhou Y., Du G., Hu X., Yu S., Liu Y., Xu Y., Huang X., Liu J., Yin B.,
RA Fan M., Peng X., Qiang B., Yuan J.;
RT "Nectin-like molecule 1 is a protein 4.1N associated protein and recruits
RT protein 4.1N from cytoplasm to the plasma membrane.";
RL Biochim. Biophys. Acta 1669:142-154(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Cunningham S.A., Tran T.M., Arrate M.P.;
RL Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-280 (ISOFORM 3).
RA Keryanov S.A., Gardner K.L.;
RT "Alternatively splicing forms of the human nectin V gene.";
RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PROTEIN SEQUENCE OF 25-39.
RX PubMed=15340161; DOI=10.1110/ps.04682504;
RA Zhang Z., Henzel W.J.;
RT "Signal peptide prediction based on analysis of experimentally verified
RT cleavage sites.";
RL Protein Sci. 13:2819-2824(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 155-398.
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 [9]
RP TISSUE SPECIFICITY, GLYCOSYLATION AT ASN-290, AND LACK OF GLYCOSYLATION AT
RP ASN-25.
RX PubMed=18420026; DOI=10.1016/j.bbamem.2008.03.013;
RA Gao J., Chen T., Hu G., Gong Y., Qiang B., Yuan J., Peng X.;
RT "Nectin-like molecule 1 is a glycoprotein with a single N-glycosylation
RT site at N290KS which influences its adhesion activity.";
RL Biochim. Biophys. Acta 1778:1429-1435(2008).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 25-135, SUBUNIT, AND DISULFIDE
RP BOND.
RX PubMed=16467305; DOI=10.1074/jbc.m513459200;
RA Dong X., Xu F., Gong Y., Gao J., Lin P., Chen T., Peng Y., Qiang B.,
RA Yuan J., Peng X., Rao Z.;
RT "Crystal structure of the V domain of human Nectin-like molecule-
RT 1/Syncam3/Tsll1/Igsf4b, a neural tissue-specific immunoglobulin-like cell-
RT cell adhesion molecule.";
RL J. Biol. Chem. 281:10610-10617(2006).
RN [11]
RP VARIANT CMT2FF CYS-138, INVOLVEMENT IN CMT2FF, AND CHARACTERIZATION OF
RP VARIANT CMT2FF CYS-138.
RX PubMed=33889941; DOI=10.1093/brain/awab019;
RA Rebelo A.P., Cortese A., Abraham A., Eshed-Eisenbach Y., Shner G.,
RA Vainshtein A., Buglo E., Camarena V., Gaidosh G., Shiekhattar R., Abreu L.,
RA Courel S., Burns D.K., Bai Y., Bacon C., Feely S.M.E., Castro D., Peles E.,
RA Reilly M.M., Shy M.E., Zuchner S.;
RT "A CADM3 variant causes Charcot-Marie-Tooth disease with marked upper limb
RT involvement.";
RL Brain 144:1197-1213(2021).
RN [12]
RP ERRATUM OF PUBMED:33889941.
RX PubMed=34037698; DOI=10.1093/brain/awab181;
RA Rebelo A.P., Cortese A., Abraham A., Eshed-Eisenbach Y., Shner G.,
RA Vainshtein A., Buglo E., Camarena V., Gaidosh G., Shiekhattar R., Abreu L.,
RA Courel S., Burns D.K., Bai Y., Bacon C., Feely S.M.E., Castro D., Peles E.,
RA Reilly M.M., Shy M.E., Zuchner S.;
RL Brain 144:e64-e64(2021).
CC -!- FUNCTION: Involved in the cell-cell adhesion. Has both calcium-
CC independent homophilic cell-cell adhesion activity and calcium-
CC independent heterophilic cell-cell adhesion activity with IGSF4,
CC NECTIN1 and NECTIN3. Interaction with EPB41L1 may regulate structure or
CC function of cell-cell junctions (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimer. Can form trans-heterodimers with NECTIN3. Interacts
CC with EPB41L1, DLG3, PALS2 and CASK (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC Q8N126; Q9BY50: SEC11C; NbExp=3; IntAct=EBI-18961338, EBI-2855401;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q99N28};
CC Single-pass type I membrane protein {ECO:0000250|UniProtKB:Q99N28}.
CC Cell junction {ECO:0000250|UniProtKB:Q99N28}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8N126-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N126-2; Sequence=VSP_017221;
CC Name=3;
CC IsoId=Q8N126-3; Sequence=VSP_022008;
CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed mainly in adult and fetal
CC brain. Isoform 2 is highly expressed in adult brain and weakly
CC expressed in placenta. In brain, Isoform 2 is highly expressed in
CC cerebellum. {ECO:0000269|PubMed:11536053, ECO:0000269|PubMed:15893517,
CC ECO:0000269|PubMed:18420026}.
CC -!- INDUCTION: Markedly in glioma cell lines and prostate cancer cell
CC lines. {ECO:0000269|PubMed:11536053}.
CC -!- DOMAIN: The cytoplasmic region mediates interaction with EPB41L1, DLG3,
CC PALS2 and CASK. {ECO:0000250}.
CC -!- DISEASE: Charcot-Marie-Tooth disease 2FF (CMT2FF) [MIM:619519]: A
CC dominant axonal form of Charcot-Marie-Tooth disease, a disorder of the
CC peripheral nervous system, characterized by progressive weakness and
CC atrophy, initially of the peroneal muscles and later of the distal
CC muscles of the arms. Charcot-Marie-Tooth disease is classified in two
CC main groups on the basis of electrophysiologic properties and
CC histopathology: primary peripheral demyelinating neuropathies
CC (designated CMT1 when they are dominantly inherited) and primary
CC peripheral axonal neuropathies (CMT2). Neuropathies of the CMT2 group
CC are characterized by signs of axonal degeneration in the absence of
CC obvious myelin alterations, normal or slightly reduced nerve conduction
CC velocities, and progressive distal muscle weakness and atrophy. CMT2FF
CC is characterized by early-childhood onset of difficulties walking or
CC running due to atrophy and weakness of the lower limbs. Some patients
CC lose independent ambulation. There is also prominent involvement of the
CC upper limbs. {ECO:0000269|PubMed:33889941}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the nectin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA91756.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AF363367; AAM60749.1; -; mRNA.
DR EMBL; AF062733; AAD17540.2; -; mRNA.
DR EMBL; AY046418; AAL02143.1; -; mRNA.
DR EMBL; AY358332; AAQ88698.1; -; mRNA.
DR EMBL; AL035403; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AF529206; AAN75603.1; -; mRNA.
DR EMBL; AK001560; BAA91756.1; ALT_INIT; mRNA.
DR CCDS; CCDS1182.1; -. [Q8N126-2]
DR CCDS; CCDS44251.1; -. [Q8N126-1]
DR RefSeq; NP_001120645.1; NM_001127173.2. [Q8N126-1]
DR RefSeq; NP_001333439.1; NM_001346510.1. [Q8N126-3]
DR RefSeq; NP_067012.1; NM_021189.4. [Q8N126-2]
DR PDB; 1Z9M; X-ray; 2.40 A; A/B=25-135.
DR PDBsum; 1Z9M; -.
DR AlphaFoldDB; Q8N126; -.
DR SMR; Q8N126; -.
DR BioGRID; 121793; 2.
DR IntAct; Q8N126; 1.
DR STRING; 9606.ENSP00000357106; -.
DR GlyGen; Q8N126; 2 sites, 1 O-linked glycan (1 site).
DR iPTMnet; Q8N126; -.
DR PhosphoSitePlus; Q8N126; -.
DR BioMuta; CADM3; -.
DR DMDM; 74759761; -.
DR EPD; Q8N126; -.
DR jPOST; Q8N126; -.
DR MassIVE; Q8N126; -.
DR MaxQB; Q8N126; -.
DR PeptideAtlas; Q8N126; -.
DR PRIDE; Q8N126; -.
DR ProteomicsDB; 71524; -. [Q8N126-1]
DR ProteomicsDB; 71525; -. [Q8N126-2]
DR ProteomicsDB; 71526; -. [Q8N126-3]
DR Antibodypedia; 669; 364 antibodies from 34 providers.
DR DNASU; 57863; -.
DR Ensembl; ENST00000368124.8; ENSP00000357106.4; ENSG00000162706.13. [Q8N126-2]
DR Ensembl; ENST00000368125.9; ENSP00000357107.4; ENSG00000162706.13. [Q8N126-1]
DR GeneID; 57863; -.
DR KEGG; hsa:57863; -.
DR MANE-Select; ENST00000368125.9; ENSP00000357107.4; NM_001127173.3; NP_001120645.1.
DR UCSC; uc001ftk.3; human. [Q8N126-1]
DR CTD; 57863; -.
DR DisGeNET; 57863; -.
DR GeneCards; CADM3; -.
DR HGNC; HGNC:17601; CADM3.
DR HPA; ENSG00000162706; Tissue enhanced (brain, placenta).
DR MIM; 609743; gene.
DR MIM; 619519; phenotype.
DR neXtProt; NX_Q8N126; -.
DR OpenTargets; ENSG00000162706; -.
DR PharmGKB; PA162380906; -.
DR VEuPathDB; HostDB:ENSG00000162706; -.
DR eggNOG; ENOG502QWJ8; Eukaryota.
DR GeneTree; ENSGT00940000159779; -.
DR HOGENOM; CLU_047574_1_0_1; -.
DR InParanoid; Q8N126; -.
DR OMA; MTQERAL; -.
DR OrthoDB; 716894at2759; -.
DR PhylomeDB; Q8N126; -.
DR TreeFam; TF326804; -.
DR PathwayCommons; Q8N126; -.
DR Reactome; R-HSA-418990; Adherens junctions interactions.
DR Reactome; R-HSA-420597; Nectin/Necl trans heterodimerization.
DR SignaLink; Q8N126; -.
DR BioGRID-ORCS; 57863; 9 hits in 1059 CRISPR screens.
DR ChiTaRS; CADM3; human.
DR EvolutionaryTrace; Q8N126; -.
DR GeneWiki; CADM3; -.
DR GenomeRNAi; 57863; -.
DR Pharos; Q8N126; Tbio.
DR PRO; PR:Q8N126; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q8N126; protein.
DR Bgee; ENSG00000162706; Expressed in cerebellar hemisphere and 156 other tissues.
DR ExpressionAtlas; Q8N126; baseline and differential.
DR Genevisible; Q8N126; HS.
DR GO; GO:0005911; C:cell-cell junction; ISS:HGNC-UCL.
DR GO; GO:0099056; C:integral component of presynaptic membrane; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0042803; F:protein homodimerization activity; ISS:HGNC-UCL.
DR GO; GO:0007157; P:heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; ISS:HGNC-UCL.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; ISS:HGNC-UCL.
DR Gene3D; 2.60.40.10; -; 3.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR013106; Ig_V-set.
DR InterPro; IPR003585; Neurexin-like.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00294; 4.1m; 1.
DR SMART; SM00409; IG; 3.
DR SMART; SM00408; IGc2; 3.
DR SUPFAM; SSF48726; SSF48726; 3.
DR PROSITE; PS50835; IG_LIKE; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell junction;
KW Cell membrane; Charcot-Marie-Tooth disease; Direct protein sequencing;
KW Disease variant; Disulfide bond; Glycoprotein; Immunoglobulin domain;
KW Membrane; Neurodegeneration; Neuropathy; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..24
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 25..398
FT /note="Cell adhesion molecule 3"
FT /id="PRO_0000046067"
FT TOPO_DOM 25..330
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 352..398
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 25..126
FT /note="Ig-like V-type"
FT DOMAIN 130..228
FT /note="Ig-like C2-type 1"
FT DOMAIN 233..315
FT /note="Ig-like C2-type 2"
FT REGION 367..398
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 25
FT /note="Not glycosylated"
FT /evidence="ECO:0000269|PubMed:18420026"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q99N28"
FT CARBOHYD 290
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:18420026"
FT DISULFID 50..110
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|PubMed:16467305"
FT DISULFID 152..209
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 254..299
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 29
FT /note="D -> DGYWQEQDLELGTLAPLDEAISSTVWSSPDMLASQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15893517"
FT /id="VSP_017221"
FT VAR_SEQ 185..231
FT /note="GKTFTVSSSVTFQVTREDDGASIVCSVNHESLKGADRSTSQRIEVLY -> D
FT (in isoform 3)"
FT /evidence="ECO:0000303|Ref.6"
FT /id="VSP_022008"
FT VARIANT 138
FT /note="Y -> C (in CMT2FF; results in misfolding due to the
FT creation of a non-native disulfide bond with C-152)"
FT /evidence="ECO:0000269|PubMed:33889941"
FT /id="VAR_086232"
FT VARIANT 162
FT /note="R -> W (in dbSNP:rs3026987)"
FT /id="VAR_059383"
FT STRAND 38..41
FT /evidence="ECO:0007829|PDB:1Z9M"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1Z9M"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:1Z9M"
FT STRAND 69..72
FT /evidence="ECO:0007829|PDB:1Z9M"
FT STRAND 83..88
FT /evidence="ECO:0007829|PDB:1Z9M"
FT STRAND 90..97
FT /evidence="ECO:0007829|PDB:1Z9M"
FT HELIX 102..104
FT /evidence="ECO:0007829|PDB:1Z9M"
FT STRAND 106..112
FT /evidence="ECO:0007829|PDB:1Z9M"
FT STRAND 114..116
FT /evidence="ECO:0007829|PDB:1Z9M"
FT STRAND 118..127
FT /evidence="ECO:0007829|PDB:1Z9M"
SQ SEQUENCE 398 AA; 43300 MW; 601B2FB5D512DB6C CRC64;
MGAPAASLLL LLLLFACCWA PGGANLSQDD SQPWTSDETV VAGGTVVLKC QVKDHEDSSL
QWSNPAQQTL YFGEKRALRD NRIQLVTSTP HELSISISNV ALADEGEYTC SIFTMPVRTA
KSLVTVLGIP QKPIITGYKS SLREKDTATL NCQSSGSKPA ARLTWRKGDQ ELHGEPTRIQ
EDPNGKTFTV SSSVTFQVTR EDDGASIVCS VNHESLKGAD RSTSQRIEVL YTPTAMIRPD
PPHPREGQKL LLHCEGRGNP VPQQYLWEKE GSVPPLKMTQ ESALIFPFLN KSDSGTYGCT
ATSNMGSYKA YYTLNVNDPS PVPSSSSTYH AIIGGIVAFI VFLLLIMLIF LGHYLIRHKG
TYLTHEAKGS DDAPDADTAI INAEGGQSGG DDKKEYFI
