CLPT1_HUMAN
ID CLPT1_HUMAN Reviewed; 669 AA.
AC O96005; B3KQH2; B4DDS3; B4E2X9; B7Z9X9; F5H8J3; Q53ET6; Q9BSS5;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Putative lipid scramblase CLPTM1 {ECO:0000305};
DE AltName: Full=Cleft lip and palate transmembrane protein 1;
GN Name=CLPTM1;
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 [GENOMIC DNA / MRNA] (ISOFORM 1), CHROMOSOMAL
RP TRANSLOCATION, TISSUE SPECIFICITY, AND POLYMORPHISM.
RC TISSUE=Craniofacial;
RX PubMed=9828125; DOI=10.1006/geno.1998.5577;
RA Yoshiura K., Machida J., Daack-Hirsch S., Patil S.R., Ashworth L.K.,
RA Hecht J.T., Murray J.C.;
RT "Characterization of a novel gene disrupted by a balanced chromosomal
RT translocation t(2;19)(q11.2;q13.3) in a family with cleft lip and palate.";
RL Genomics 54:231-240(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3), AND VARIANT
RP CYS-478.
RC TISSUE=Thalamus, and Uterus;
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 MRNA] (ISOFORM 1).
RX PubMed=16303743; DOI=10.1093/dnares/12.2.117;
RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J.,
RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S.,
RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y.,
RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S.,
RA Isogai T.;
RT "Signal sequence and keyword trap in silico for selection of full-length
RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA
RT libraries.";
RL DNA Res. 12:117-126(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Kidney;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.;
RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Choriocarcinoma, and Melanoma;
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 [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-656 (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-295.
RC TISSUE=Platelet;
RX PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT "Elucidation of N-glycosylation sites on human platelet proteins: a
RT glycoproteomic approach.";
RL Mol. Cell. Proteomics 5:226-233(2006).
RN [10]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-295.
RC TISSUE=Liver;
RX PubMed=19159218; DOI=10.1021/pr8008012;
RA Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT "Glycoproteomics analysis of human liver tissue by combination of multiple
RT enzyme digestion and hydrazide chemistry.";
RL J. Proteome Res. 8:651-661(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-601, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP ACETYLATION AT ALA-2, AND CLEAVAGE OF INITIATOR METHIONINE.
RX PubMed=25489052; DOI=10.1093/hmg/ddu611;
RA Myklebust L.M., Van Damme P., Stoeve S.I., Doerfel M.J., Abboud A.,
RA Kalvik T.V., Grauffel C., Jonckheere V., Wu Y., Swensen J., Kaasa H.,
RA Liszczak G., Marmorstein R., Reuter N., Lyon G.J., Gevaert K., Arnesen T.;
RT "Biochemical and cellular analysis of Ogden syndrome reveals downstream Nt-
RT acetylation defects.";
RL Hum. Mol. Genet. 24:1956-1976(2015).
RN [15]
RP FUNCTION.
RX PubMed=29255114; DOI=10.1083/jcb.201706135;
RA Liu Y.S., Guo X.Y., Hirata T., Rong Y., Motooka D., Kitajima T.,
RA Murakami Y., Gao X.D., Nakamura S., Kinoshita T., Fujita M.;
RT "N-Glycan-dependent protein folding and endoplasmic reticulum retention
RT regulate GPI-anchor processing.";
RL J. Cell Biol. 217:585-599(2018).
CC -!- FUNCTION: Involved in GABAergic but not glutamatergic transmission.
CC Binds and traps GABAA receptors in the endoplasmic reticulum (ER).
CC Modulates postsynaptic GABAergic transmission, and therefore inhibitory
CC neurotransmission, by reducing the plasma membrane expression of these
CC receptors. Altered GABAergic signaling is one among many causes of
CC cleft palate (By similarity). Might function as a lipid scramblase,
CC translocating lipids in membranes from one leaflet to the other one (By
CC similarity). Required for efficient glycosylphosphatidylinositol (GPI)
CC inositol deacylation in the ER, which is a crucial step to switch GPI-
CC anchored proteins (GPI-APs) from protein folding to transport states
CC (PubMed:29255114). May play a role in T-cell development (By
CC similarity). {ECO:0000250|UniProtKB:Q8VBZ3,
CC ECO:0000250|UniProtKB:Q96KA5, ECO:0000269|PubMed:29255114}.
CC -!- INTERACTION:
CC O96005; Q8VCW4: Unc93b1; Xeno; NbExp=2; IntAct=EBI-2873194, EBI-6116986;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O96005-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O96005-3; Sequence=VSP_055525;
CC Name=3;
CC IsoId=O96005-4; Sequence=VSP_055526;
CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:9828125}.
CC -!- POLYMORPHISM: A chromosomal translocation involving CLPTM1 is found in
CC a family with cleft lip and palate. However, no etiologic link with the
CC disease is characterized. Translocation t(2;19)(q11.2;q13.3).
CC {ECO:0000269|PubMed:9828125}.
CC -!- SIMILARITY: Belongs to the CLPTM1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH04865.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=AAP35926.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AF037338; AAC97420.1; -; Genomic_DNA.
DR EMBL; AF037339; AAC98151.1; -; mRNA.
DR EMBL; AK293314; BAG56834.1; -; mRNA.
DR EMBL; AK304480; BAG65291.1; -; mRNA.
DR EMBL; AK316094; BAH14465.1; -; mRNA.
DR EMBL; AK074935; BAG52034.1; -; mRNA.
DR EMBL; AK223553; BAD97273.1; -; mRNA.
DR EMBL; AC011481; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471126; EAW57314.1; -; Genomic_DNA.
DR EMBL; BC004865; AAH04865.1; ALT_SEQ; mRNA.
DR EMBL; BC012359; AAH12359.1; -; mRNA.
DR EMBL; BT007262; AAP35926.1; ALT_SEQ; mRNA.
DR CCDS; CCDS12651.1; -. [O96005-1]
DR CCDS; CCDS74394.1; -. [O96005-4]
DR CCDS; CCDS74395.1; -. [O96005-3]
DR RefSeq; NP_001269104.1; NM_001282175.1. [O96005-4]
DR RefSeq; NP_001269105.1; NM_001282176.1. [O96005-3]
DR RefSeq; NP_001285.1; NM_001294.3. [O96005-1]
DR AlphaFoldDB; O96005; -.
DR BioGRID; 107619; 156.
DR IntAct; O96005; 31.
DR MINT; O96005; -.
DR STRING; 9606.ENSP00000336994; -.
DR TCDB; 8.A.125.1.1; the cleft lip and palate transmembrane protein 1 (clptm1) family.
DR GlyConnect; 1116; 5 N-Linked glycans (1 site).
DR GlyGen; O96005; 7 sites, 5 N-linked glycans (1 site).
DR iPTMnet; O96005; -.
DR MetOSite; O96005; -.
DR PhosphoSitePlus; O96005; -.
DR SwissPalm; O96005; -.
DR BioMuta; CLPTM1; -.
DR EPD; O96005; -.
DR jPOST; O96005; -.
DR MassIVE; O96005; -.
DR MaxQB; O96005; -.
DR PaxDb; O96005; -.
DR PeptideAtlas; O96005; -.
DR PRIDE; O96005; -.
DR ProteomicsDB; 27801; -.
DR ProteomicsDB; 3887; -.
DR ProteomicsDB; 51184; -. [O96005-1]
DR TopDownProteomics; O96005-1; -. [O96005-1]
DR Antibodypedia; 31237; 165 antibodies from 29 providers.
DR DNASU; 1209; -.
DR Ensembl; ENST00000337392.10; ENSP00000336994.4; ENSG00000104853.16. [O96005-1]
DR Ensembl; ENST00000541297.6; ENSP00000442011.1; ENSG00000104853.16. [O96005-4]
DR Ensembl; ENST00000546079.5; ENSP00000443192.1; ENSG00000104853.16. [O96005-3]
DR GeneID; 1209; -.
DR KEGG; hsa:1209; -.
DR MANE-Select; ENST00000337392.10; ENSP00000336994.4; NM_001294.4; NP_001285.1.
DR UCSC; uc002pai.5; human. [O96005-1]
DR CTD; 1209; -.
DR DisGeNET; 1209; -.
DR GeneCards; CLPTM1; -.
DR HGNC; HGNC:2087; CLPTM1.
DR HPA; ENSG00000104853; Low tissue specificity.
DR MIM; 604783; gene.
DR neXtProt; NX_O96005; -.
DR OpenTargets; ENSG00000104853; -.
DR PharmGKB; PA26613; -.
DR VEuPathDB; HostDB:ENSG00000104853; -.
DR eggNOG; KOG2489; Eukaryota.
DR GeneTree; ENSGT00530000063461; -.
DR HOGENOM; CLU_019907_3_1_1; -.
DR InParanoid; O96005; -.
DR OMA; NMLYGYL; -.
DR PhylomeDB; O96005; -.
DR TreeFam; TF318501; -.
DR PathwayCommons; O96005; -.
DR SignaLink; O96005; -.
DR BioGRID-ORCS; 1209; 23 hits in 1076 CRISPR screens.
DR ChiTaRS; CLPTM1; human.
DR GeneWiki; Cleft_lip_and_palate_transmembrane_protein_1; -.
DR GenomeRNAi; 1209; -.
DR Pharos; O96005; Tbio.
DR PRO; PR:O96005; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O96005; protein.
DR Bgee; ENSG00000104853; Expressed in right adrenal gland cortex and 196 other tissues.
DR ExpressionAtlas; O96005; baseline and differential.
DR Genevisible; O96005; HS.
DR GO; GO:0009897; C:external side of plasma membrane; ISS:BHF-UCL.
DR GO; GO:0005887; C:integral component of plasma membrane; TAS:ProtInc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0050811; F:GABA receptor binding; IEA:Ensembl.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0033081; P:regulation of T cell differentiation in thymus; ISS:BHF-UCL.
DR InterPro; IPR008429; CLPTM1.
DR InterPro; IPR030434; CLPTM1L.
DR PANTHER; PTHR21347; PTHR21347; 1.
DR PANTHER; PTHR21347:SF0; PTHR21347:SF0; 1.
DR Pfam; PF05602; CLPTM1; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosomal rearrangement;
KW Developmental protein; Differentiation; Glycoprotein; Membrane;
KW Phosphoprotein; Reference proteome; Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..669
FT /note="Putative lipid scramblase CLPTM1"
FT /id="PRO_0000245096"
FT TOPO_DOM 2..354
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 355..375
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 376..390
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 412..416
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 417..437
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 438..477
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..502
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 503..523
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 524..669
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 1..50
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 614..669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..37
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 622..654
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000269|PubMed:25489052,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT CARBOHYD 28
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 161
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 241
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 295
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16263699,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 413
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..102
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055525"
FT VAR_SEQ 1..24
FT /note="MAAAQEADGARSAVVAAGGGSSGQ -> MSRKAHITEK (in isoform
FT 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055526"
FT VARIANT 478
FT /note="Y -> C (in dbSNP:rs140564801)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_071064"
FT CONFLICT 103
FT /note="M -> V (in Ref. 2; BAG65291)"
FT /evidence="ECO:0000305"
FT CONFLICT 175
FT /note="F -> S (in Ref. 2; BAG65291)"
FT /evidence="ECO:0000305"
FT CONFLICT 327
FT /note="W -> R (in Ref. 2; BAH14465)"
FT /evidence="ECO:0000305"
FT CONFLICT 494
FT /note="S -> G (in Ref. 3; BAG52034)"
FT /evidence="ECO:0000305"
FT CONFLICT 637
FT /note="A -> T (in Ref. 4; BAD97273)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 669 AA; 76097 MW; 769AB9D291917339 CRC64;
MAAAQEADGA RSAVVAAGGG SSGQVTSNGS IGRDPPAETQ PQNPPAQPAP NAWQVIKGVL
FRIFIIWAIS SWFRRGPAPQ DQAGPGGAPR VASRNLFPKD TLMNLHVYIS EHEHFTDFNA
TSALFWEQHD LVYGDWTSGE NSDGCYEHFA ELDIPQSVQQ NGSIYIHVYF TKSGFHPDPR
QKALYRRLAT VHMSRMINKY KRRRFQKTKN LLTGETEADP EMIKRAEDYG PVEVISHWHP
NITINIVDDH TPWVKGSVPP PLDQYVKFDA VSGDYYPIIY FNDYWNLQKD YYPINESLAS
LPLRVSFCPL SLWRWQLYAA QSTKSPWNFL GDELYEQSDE EQDSVKVALL ETNPYLLALT
IIVSIVHSVF EFLAFKNDIQ FWNSRQSLEG LSVRSVFFGV FQSFVVLLYI LDNETNFVVQ
VSVFIGVLID LWKITKVMDV RLDREHRVAG IFPRLSFKDK STYIESSTKV YDDMAFRYLS
WILFPLLGCY AVYSLLYLEH KGWYSWVLSM LYGFLLTFGF ITMTPQLFIN YKLKSVAHLP
WRMLTYKALN TFIDDLFAFV IKMPVMYRIG CLRDDVVFFI YLYQRWIYRV DPTRVNEFGM
SGEDPTAAAP VAEVPTAAGA LTPTPAPTTT TATREEASTS LPTKPTQGAS SASEPQEAPP
KPAEDKKKD
