GenomeNet

Database: UniProt
Entry: Q6UW56
LinkDB: Q6UW56
Original site: Q6UW56 
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   10-APR-2019, entry version 126.
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;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; 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.,
RA   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;
RA   Zhu F., Yan W., Zhao Z.L., Chai Y.B., Lu F., Wang Q., Peng W.D.,
RA   Yang A.G., 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
RP   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
RT   300 previously undefined genes expressed in CD34+ hematopoietic
RT   stem/progenitor 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.,
RA   Huang A., Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J.,
RA   Lewis L., Liao D., Mark M.R., Robbie E., Sanchez C., Schoenfeld J.,
RA   Seshagiri S., Simmons L., Singh J., Smith V., Stinson J., Vagts A.,
RA   Vandlen R.L., Watanabe C., Wieand D., Woods K., Xie M.-H.,
RA   Yansura D.G., Yi S., Yu G., Yuan J., Zhang M., Zhang Z., Goddard A.D.,
RA   Wood W.I., Godowski P.J., Gray A.M.;
RT   "The secreted protein discovery initiative (SPDI), a large-scale
RT   effort to identify novel human secreted and transmembrane proteins: a
RT   bioinformatics 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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   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.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   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.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 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.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   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
RT   project: 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
RT   verified 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.,
RA   Huang B., Li H., Zhang J., Yao L., Lu Z.;
RT   "Apoptosis related protein 3, an ATRA-upregulated membrane protein
RT   arrests the cell cycle at G1/S phase by decreasing the expression of
RT   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.,
RA   Lu Z.;
RT   "Identification of the distinct promoters for the two transcripts of
RT   apoptosis related protein 3 and their transcriptional regulation by
RT   NFAT 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)
CC       signal pathway. {ECO:0000269|PubMed:21723284}.
CC   -!- SUBUNIT: Interacts with NELL1; the interaction promotes
CC       osteoblastic differentiation and mineralization.
CC       {ECO:0000269|PubMed:21723284}.
CC   -!- INTERACTION:
CC       Q92832:NELL1; NbExp=4; IntAct=EBI-723802, EBI-947754;
CC       Q9Y5X1:SNX9; NbExp=2; IntAct=EBI-723802, EBI-77848;
CC   -!- SUBCELLULAR LOCATION: Nucleus envelope
CC       {ECO:0000269|PubMed:21723284}. Cell membrane
CC       {ECO:0000269|PubMed:17524364}; Single-pass membrane protein
CC       {ECO:0000269|PubMed:17524364}. Note=Colocalizes with NELL1 on the
CC       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         Note=Produced by alternative splicing of isoform 1. No
CC         experimental confirmation available.;
CC       Name=3;
CC         IsoId=Q6UW56-3; Sequence=VSP_037521;
CC         Note=Produced by alternative promoter usage.;
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
CC       several tumor cell lines. {ECO:0000269|PubMed:17524364}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD27770.1; Type=Frameshift; Positions=19; Evidence={ECO:0000305};
CC       Sequence=AAD31317.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAD31317.2; Type=Frameshift; Positions=189; Evidence={ECO:0000305};
CC       Sequence=AAH02846.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAH11006.3; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
CC       Sequence=AAH35850.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
CC       Sequence=AAX93173.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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; CCDS1741.1; -. [Q6UW56-3]
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. [Q6UW56-3]
DR   UniGene; Hs.9527; -.
DR   ProteinModelPortal; Q6UW56; -.
DR   BioGrid; 119507; 4.
DR   IntAct; Q6UW56; 5.
DR   MINT; Q6UW56; -.
DR   STRING; 9606.ENSP00000484228; -.
DR   GlyConnect; 1000; -.
DR   iPTMnet; Q6UW56; -.
DR   PhosphoSitePlus; Q6UW56; -.
DR   BioMuta; ATRAID; -.
DR   DMDM; 239938597; -.
DR   jPOST; Q6UW56; -.
DR   MaxQB; Q6UW56; -.
DR   PaxDb; Q6UW56; -.
DR   PeptideAtlas; Q6UW56; -.
DR   PRIDE; Q6UW56; -.
DR   ProteomicsDB; 67447; -.
DR   ProteomicsDB; 67448; -. [Q6UW56-2]
DR   ProteomicsDB; 67449; -. [Q6UW56-3]
DR   Ensembl; ENST00000380171; ENSP00000369518; ENSG00000138085. [Q6UW56-3]
DR   Ensembl; ENST00000405489; ENSP00000384033; ENSG00000138085. [Q6UW56-2]
DR   Ensembl; ENST00000606999; ENSP00000476080; ENSG00000138085. [Q6UW56-1]
DR   Ensembl; ENST00000611786; ENSP00000484228; ENSG00000138085. [Q6UW56-3]
DR   GeneID; 51374; -.
DR   KEGG; hsa:51374; -.
DR   UCSC; uc002rjf.5; human. [Q6UW56-1]
DR   CTD; 51374; -.
DR   DisGeNET; 51374; -.
DR   EuPathDB; HostDB:ENSG00000138085.16; -.
DR   GeneCards; ATRAID; -.
DR   HGNC; HGNC:24090; ATRAID.
DR   HPA; HPA051353; -.
DR   neXtProt; NX_Q6UW56; -.
DR   OpenTargets; ENSG00000138085; -.
DR   PharmGKB; PA134964154; -.
DR   eggNOG; ENOG410IYNU; Eukaryota.
DR   eggNOG; ENOG4111PJW; LUCA.
DR   GeneTree; ENSGT00390000017252; -.
DR   HOVERGEN; HBG054041; -.
DR   InParanoid; Q6UW56; -.
DR   OMA; PGGINAW; -.
DR   OrthoDB; 1027431at2759; -.
DR   PhylomeDB; Q6UW56; -.
DR   TreeFam; TF335766; -.
DR   ChiTaRS; ATRAID; human.
DR   GeneWiki; C2orf28; -.
DR   GenomeRNAi; 51374; -.
DR   PRO; PR:Q6UW56; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000138085; Expressed in 225 organ(s), highest expression level in testis.
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: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:1903363; P:negative regulation of cellular protein catabolic process; IDA:UniProtKB.
DR   GO; GO:0033689; P:negative regulation of osteoblast proliferation; 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; IPR013032; EGF-like_CS.
DR   InterPro; IPR000742; EGF-like_dom.
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   Complete proteome; Differentiation; Direct protein sequencing;
KW   Disulfide bond; EGF-like domain; Glycoprotein; Membrane; Nucleus;
KW   Polymorphism; Reference proteome; Signal; Transmembrane;
KW   Transmembrane helix.
FT   SIGNAL        1     30       {ECO:0000269|PubMed:15340161}.
FT   CHAIN        31    229       All-trans retinoic acid-induced
FT                                differentiation factor.
FT                                /FTId=PRO_0000020752.
FT   TOPO_DOM     31    199       Extracellular. {ECO:0000255}.
FT   TRANSMEM    200    220       Helical. {ECO:0000255}.
FT   TOPO_DOM    221    229       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      152    193       EGF-like. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00076}.
FT   CARBOHYD     44     44       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD     79     79       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    157    157       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   CARBOHYD    168    168       N-linked (GlcNAc...) asparagine.
FT                                {ECO:0000255}.
FT   DISULFID    156    171       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    165    181       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   DISULFID    183    192       {ECO:0000255|PROSITE-ProRule:PRU00076}.
FT   VAR_SEQ       1     58       Missing (in isoform 2).
FT                                {ECO:0000303|PubMed:10948432,
FT                                ECO:0000303|PubMed:14702039,
FT                                ECO:0000303|PubMed:15489334,
FT                                ECO:0000303|Ref.3}.
FT                                /FTId=VSP_014108.
FT   VAR_SEQ       1      1       M -> MKTSAELHEQEKPPSSPRATGPGRLGHARGRGPDAL
FT                                RGGAAGPGRASSGAPRERKM (in isoform 3).
FT                                {ECO:0000303|Ref.7}.
FT                                /FTId=VSP_037521.
FT   VARIANT     209    209       A -> S (in dbSNP:rs7437).
FT                                {ECO:0000269|Ref.1}.
FT                                /FTId=VAR_057991.
FT   CONFLICT      5      5       D -> G (in Ref. 1; BAF80618, 4; AAD27770,
FT                                5; AAQ89327 and 10; AAH02846/AAH11006/
FT                                AAH35850). {ECO:0000305}.
FT   CONFLICT     33     33       E -> EP (in Ref. 3; AAK69412).
FT                                {ECO:0000305}.
FT   CONFLICT    219    219       W -> S (in Ref. 1; BAF80618).
FT                                {ECO:0000305}.
FT   CONFLICT    221    221       T -> A (in Ref. 3; AAK69412).
FT                                {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
//
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