ARAID_HUMAN
ID ARAID_HUMAN Reviewed; 229 AA.
AC Q6UW56; A8C1S2; A8K779; Q96FF6; Q96RT2; Q9Y2R7; Q9Y5L7;
DT 21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=All-trans retinoic acid-induced differentiation factor;
DE AltName: Full=Apoptosis-related protein 3;
DE Short=APR-3;
DE AltName: Full=p18;
DE Flags: Precursor;
GN Name=ATRAID; Synonyms=APR3, C2orf28; ORFNames=HSPC013, UNQ214/PRO240;
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), AND VARIANT SER-209.
RC TISSUE=Kidney;
RA Mori K., Ogawa Y., Tashiro K., Ozaki S., Mukoyama M., Tanaka I., Nakao K.;
RT "Molecular cloning of a novel protein with four putative transmembrane
RT domains.";
RL Submitted (NOV-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RX PubMed=10948432; DOI=10.2144/00292st06;
RA Zhu F., Yan W., Zhao Z.L., Chai Y.B., Lu F., Wang Q., Peng W.D., Yang A.G.,
RA Wang C.J.;
RT "Improved PCR-based subtractive hybridization strategy for cloning
RT differentially expressed genes.";
RL BioTechniques 29:310-313(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Yang Y.C., Chen S.Y., Chang M.S.;
RT "Cloning and characterization of p18.";
RL Submitted (JUN-2000) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
RC TISSUE=Umbilical cord blood;
RX PubMed=11042152; DOI=10.1101/gr.140200;
RA Zhang Q.-H., Ye M., Wu X.-Y., Ren S.-X., Zhao M., Zhao C.-J., Fu G.,
RA Shen Y., Fan H.-Y., Lu G., Zhong M., Xu X.-R., Han Z.-G., Zhang J.-W.,
RA Tao J., Huang Q.-H., Zhou J., Hu G.-X., Gu J., Chen S.-J., Chen Z.;
RT "Cloning and functional analysis of cDNAs with open reading frames for 300
RT previously undefined genes expressed in CD34+ hematopoietic stem/progenitor
RT cells.";
RL Genome Res. 10:1546-1560(2000).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Skeletal muscle;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (JUL-2004) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, Placenta, and Uterus;
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 [11]
RP PROTEIN SEQUENCE OF 31-45.
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 [12]
RP INDUCTION, SUBCELLULAR LOCATION, AND POSSIBLE FUNCTION.
RX PubMed=17524364; DOI=10.1016/j.bbrc.2007.05.049;
RA Yu F., Yang G., Zhao Z., Ji L., Cao Y., Bai L., Lu F., Fu H., Huang B.,
RA Li H., Zhang J., Yao L., Lu Z.;
RT "Apoptosis related protein 3, an ATRA-upregulated membrane protein arrests
RT the cell cycle at G1/S phase by decreasing the expression of cyclin D1.";
RL Biochem. Biophys. Res. Commun. 358:1041-1046(2007).
RN [13]
RP ALTERNATIVE PROMOTER USAGE.
RX PubMed=17387583; DOI=10.1007/s11010-007-9440-7;
RA Yang G., Yu F., Fu H., Lu F., Huang B., Bai L., Zhao Z., Yao L., Lu Z.;
RT "Identification of the distinct promoters for the two transcripts of
RT apoptosis related protein 3 and their transcriptional regulation by NFAT
RT and NFkappaB.";
RL Mol. Cell. Biochem. 302:187-194(2007).
RN [14]
RP FUNCTION IN OSTEOBLAST DIFFERENTIATION, INTERACTION WITH NELL1, AND
RP SUBCELLULAR LOCATION.
RX PubMed=21723284; DOI=10.1016/j.febslet.2011.06.024;
RA Zou X., Shen J., Chen F., Ting K., Zheng Z., Pang S., Zara J.N.,
RA Adams J.S., Soo C., Zhang X.;
RT "NELL-1 binds to APR3 affecting human osteoblast proliferation and
RT differentiation.";
RL FEBS Lett. 585:2410-2418(2011).
CC -!- FUNCTION: Promotes osteoblast cell differentiation and terminal
CC mineralization. Plays a role in inducing the cell cycle arrest via
CC inhibiting CCND1 expression in all-trans-retinoic acid (ATRA) signal
CC pathway. {ECO:0000269|PubMed:21723284}.
CC -!- SUBUNIT: Interacts with NELL1; the interaction promotes osteoblastic
CC differentiation and mineralization. {ECO:0000269|PubMed:21723284}.
CC -!- INTERACTION:
CC Q6UW56; Q92832: NELL1; NbExp=4; IntAct=EBI-723802, EBI-947754;
CC Q6UW56; Q9Y5X1: SNX9; NbExp=2; IntAct=EBI-723802, EBI-77848;
CC Q6UW56-2; Q00013: MPP1; NbExp=3; IntAct=EBI-12830308, EBI-711788;
CC -!- SUBCELLULAR LOCATION: Nucleus envelope {ECO:0000269|PubMed:21723284}.
CC Cell membrane {ECO:0000269|PubMed:17524364}; Single-pass membrane
CC protein {ECO:0000269|PubMed:17524364}. Note=Colocalizes with NELL1 on
CC the nuclear envelope and the perinuclear region (PubMed:21723284).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative promoter usage, Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6UW56-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UW56-2; Sequence=VSP_014108;
CC Name=3;
CC IsoId=Q6UW56-3; Sequence=VSP_037521;
CC -!- TISSUE SPECIFICITY: Weakly expressed in hematopoietic cell lines.
CC {ECO:0000269|PubMed:11042152}.
CC -!- INDUCTION: Up-regulated by all-trans-retinoic acid (ATRA) in several
CC tumor cell lines. {ECO:0000269|PubMed:17524364}.
CC -!- MISCELLANEOUS: [Isoform 2]: Produced by alternative splicing of isoform
CC 1. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: Produced by alternative promoter usage.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD27770.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAD31317.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAD31317.2; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAH02846.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH11006.3; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH35850.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAX93173.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AB009017; BAF80618.1; -; mRNA.
DR EMBL; AF144055; AAD31317.2; ALT_SEQ; mRNA.
DR EMBL; AF275744; AAK69412.1; -; mRNA.
DR EMBL; AF077037; AAD27770.1; ALT_FRAME; mRNA.
DR EMBL; AY358968; AAQ89327.1; -; mRNA.
DR EMBL; AK291894; BAF84583.1; -; mRNA.
DR EMBL; CR600041; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AC013403; AAX93173.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CH471053; EAX00617.1; -; Genomic_DNA.
DR EMBL; BC002846; AAH02846.2; ALT_INIT; mRNA.
DR EMBL; BC011006; AAH11006.3; ALT_INIT; mRNA.
DR EMBL; BC021237; AAH21237.1; -; mRNA.
DR EMBL; BC035850; AAH35850.1; ALT_INIT; mRNA.
DR CCDS; CCDS46243.1; -. [Q6UW56-2]
DR CCDS; CCDS62877.1; -. [Q6UW56-1]
DR RefSeq; NP_001164266.1; NM_001170795.1. [Q6UW56-1]
DR RefSeq; NP_057169.2; NM_016085.4. [Q6UW56-2]
DR RefSeq; NP_542159.3; NM_080592.3.
DR AlphaFoldDB; Q6UW56; -.
DR BioGRID; 119507; 10.
DR IntAct; Q6UW56; 8.
DR MINT; Q6UW56; -.
DR STRING; 9606.ENSP00000484228; -.
DR GlyConnect; 1000; 4 N-Linked glycans (2 sites).
DR GlyGen; Q6UW56; 4 sites, 4 N-linked glycans (2 sites).
DR iPTMnet; Q6UW56; -.
DR PhosphoSitePlus; Q6UW56; -.
DR BioMuta; ATRAID; -.
DR DMDM; 239938597; -.
DR EPD; Q6UW56; -.
DR jPOST; Q6UW56; -.
DR MassIVE; Q6UW56; -.
DR MaxQB; Q6UW56; -.
DR PaxDb; Q6UW56; -.
DR PeptideAtlas; Q6UW56; -.
DR PRIDE; Q6UW56; -.
DR ProteomicsDB; 67447; -. [Q6UW56-1]
DR ProteomicsDB; 67448; -. [Q6UW56-2]
DR ProteomicsDB; 67449; -. [Q6UW56-3]
DR Antibodypedia; 28263; 106 antibodies from 24 providers.
DR DNASU; 51374; -.
DR Ensembl; ENST00000380171.9; ENSP00000369518.4; ENSG00000138085.18. [Q6UW56-1]
DR Ensembl; ENST00000405489.7; ENSP00000384033.3; ENSG00000138085.18. [Q6UW56-2]
DR GeneID; 51374; -.
DR KEGG; hsa:51374; -.
DR MANE-Select; ENST00000380171.9; ENSP00000369518.4; NM_001170795.4; NP_001164266.1.
DR UCSC; uc002rjf.5; human. [Q6UW56-1]
DR CTD; 51374; -.
DR DisGeNET; 51374; -.
DR GeneCards; ATRAID; -.
DR HGNC; HGNC:24090; ATRAID.
DR HPA; ENSG00000138085; Low tissue specificity.
DR MIM; 619682; gene.
DR neXtProt; NX_Q6UW56; -.
DR OpenTargets; ENSG00000138085; -.
DR PharmGKB; PA134964154; -.
DR VEuPathDB; HostDB:ENSG00000138085; -.
DR eggNOG; ENOG502S1YR; Eukaryota.
DR GeneTree; ENSGT00390000017252; -.
DR HOGENOM; CLU_086391_0_0_1; -.
DR InParanoid; Q6UW56; -.
DR OMA; RCCLNQE; -.
DR OrthoDB; 1027431at2759; -.
DR PhylomeDB; Q6UW56; -.
DR TreeFam; TF335766; -.
DR PathwayCommons; Q6UW56; -.
DR SignaLink; Q6UW56; -.
DR BioGRID-ORCS; 51374; 9 hits in 1081 CRISPR screens.
DR ChiTaRS; ATRAID; human.
DR GeneWiki; C2orf28; -.
DR GenomeRNAi; 51374; -.
DR Pharos; Q6UW56; Tbio.
DR PRO; PR:Q6UW56; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q6UW56; protein.
DR Bgee; ENSG00000138085; Expressed in type B pancreatic cell and 199 other tissues.
DR ExpressionAtlas; Q6UW56; baseline and differential.
DR Genevisible; Q6UW56; HS.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central.
DR GO; GO:0005765; C:lysosomal membrane; IEA:Ensembl.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0033689; P:negative regulation of osteoblast proliferation; IDA:UniProtKB.
DR GO; GO:0042177; P:negative regulation of protein catabolic process; IDA:UniProtKB.
DR GO; GO:0030501; P:positive regulation of bone mineralization; IDA:UniProtKB.
DR GO; GO:0045669; P:positive regulation of osteoblast differentiation; IDA:UniProtKB.
DR GO; GO:0010468; P:regulation of gene expression; IDA:UniProtKB.
DR InterPro; IPR042350; ATRAID.
DR InterPro; IPR000742; EGF-like_dom.
DR PANTHER; PTHR15926; PTHR15926; 1.
DR PROSITE; PS00022; EGF_1; 1.
DR PROSITE; PS01186; EGF_2; 1.
DR PROSITE; PS50026; EGF_3; 1.
PE 1: Evidence at protein level;
KW Alternative promoter usage; Alternative splicing; Cell membrane;
KW Differentiation; Direct protein sequencing; Disulfide bond;
KW EGF-like domain; Glycoprotein; Membrane; Nucleus; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..30
FT /evidence="ECO:0000269|PubMed:15340161"
FT CHAIN 31..229
FT /note="All-trans retinoic acid-induced differentiation
FT factor"
FT /id="PRO_0000020752"
FT TOPO_DOM 31..199
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..229
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 152..193
FT /note="EGF-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT CARBOHYD 44
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 79
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 157
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 168
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 156..171
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 165..181
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT DISULFID 183..192
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00076"
FT VAR_SEQ 1..58
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10948432,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.3"
FT /id="VSP_014108"
FT VAR_SEQ 1
FT /note="M -> MKTSAELHEQEKPPSSPRATGPGRLGHARGRGPDALRGGAAGPGRAS
FT SGAPRERKM (in isoform 3)"
FT /evidence="ECO:0000303|Ref.7"
FT /id="VSP_037521"
FT VARIANT 209
FT /note="A -> S (in dbSNP:rs7437)"
FT /evidence="ECO:0000269|Ref.1"
FT /id="VAR_057991"
FT CONFLICT 5
FT /note="D -> G (in Ref. 1; BAF80618, 4; AAD27770, 5;
FT AAQ89327 and 10; AAH02846/AAH11006/AAH35850)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="E -> EP (in Ref. 3; AAK69412)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="W -> S (in Ref. 1; BAF80618)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="T -> A (in Ref. 3; AAK69412)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 229 AA; 24747 MW; CF051C5E886BCFF1 CRC64;
MAPHDPGSLT TLVPWAAALL LALGVERALA LPEICTQCPG SVQNLSKVAF YCKTTRELML
HARCCLNQKG TILGLDLQNC SLEDPGPNFH QAHTTVIIDL QANPLKGDLA NTFRGFTQLQ
TLILPQHVNC PGGINAWNTI TSYIDNQICQ GQKNLCNNTG DPEMCPENGS CVPDGPGLLQ
CVCADGFHGY KCMRQGSFSL LMFFGILGAT TLSVSILLWA TQRRKAKTS
