DIP2A_HUMAN
ID DIP2A_HUMAN Reviewed; 1571 AA.
AC Q14689; A6P4T3; B4E0F0; E7EMA5; Q8IVA3; Q8N4S2; Q8TD89; Q96ML9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2003, sequence version 2.
DT 03-AUG-2022, entry version 174.
DE RecName: Full=Disco-interacting protein 2 homolog A;
DE Short=DIP2 homolog A;
DE EC=6.2.1.1 {ECO:0000250|UniProtKB:Q8BWT5};
GN Name=DIP2A; Synonyms=C21orf106, DIP2, KIAA0184;
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 6).
RX PubMed=12036298; DOI=10.1006/geno.2002.6782;
RA Gardiner K., Slavov D., Bechtel L., Davisson M.;
RT "Annotation of human chromosome 21 for relevance to Down syndrome: gene
RT structure and expression analysis.";
RL Genomics 79:833-843(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INTERACTION WITH FSTL1.
RX PubMed=20860622; DOI=10.1111/j.1742-4658.2010.07816.x;
RA Tanaka M., Murakami K., Ozaki S., Imura Y., Tong X.P., Watanabe T.,
RA Sawaki T., Kawanami T., Kawabata D., Fujii T., Usui T., Masaki Y.,
RA Fukushima T., Jin Z.X., Umehara H., Mimori T.;
RT "DIP2 disco-interacting protein 2 homolog A (Drosophila) is a candidate
RT receptor for follistatin-related protein/follistatin-like 1--analysis of
RT their binding with TGF-beta superfamily proteins.";
RL FEBS J. 277:4278-4289(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 5).
RC TISSUE=Placenta, and Thymus;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10830953; DOI=10.1038/35012518;
RA Hattori M., Fujiyama A., Taylor T.D., Watanabe H., Yada T., Park H.-S.,
RA Toyoda A., Ishii K., Totoki Y., Choi D.-K., Groner Y., Soeda E., Ohki M.,
RA Takagi T., Sakaki Y., Taudien S., Blechschmidt K., Polley A., Menzel U.,
RA Delabar J., Kumpf K., Lehmann R., Patterson D., Reichwald K., Rump A.,
RA Schillhabel M., Schudy A., Zimmermann W., Rosenthal A., Kudoh J.,
RA Shibuya K., Kawasaki K., Asakawa S., Shintani A., Sasaki T., Nagamine K.,
RA Mitsuyama S., Antonarakis S.E., Minoshima S., Shimizu N., Nordsiek G.,
RA Hornischer K., Brandt P., Scharfe M., Schoen O., Desario A., Reichelt J.,
RA Kauer G., Bloecker H., Ramser J., Beck A., Klages S., Hennig S.,
RA Riesselmann L., Dagand E., Wehrmeyer S., Borzym K., Gardiner K.,
RA Nizetic D., Francis F., Lehrach H., Reinhardt R., Yaspo M.-L.;
RT "The DNA sequence of human chromosome 21.";
RL Nature 405:311-319(2000).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 4).
RC TISSUE=Blood, and Mammary carcinoma;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 705-1567 (ISOFORM 1).
RC TISSUE=Bone marrow;
RX PubMed=8724849; DOI=10.1093/dnares/3.1.17;
RA Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.;
RT "Prediction of the coding sequences of unidentified human genes. V. The
RT coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of
RT cDNA clones from human cell line KG-1.";
RL DNA Res. 3:17-24(1996).
RN [7]
RP FUNCTION, INTERACTION WITH FSTL1, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=20054002; DOI=10.1074/jbc.m109.069468;
RA Ouchi N., Asaumi Y., Ohashi K., Higuchi A., Sono-Romanelli S., Oshima Y.,
RA Walsh K.;
RT "DIP2A functions as a FSTL1 receptor.";
RL J. Biol. Chem. 285:7127-7134(2010).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-94 AND THR-155, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
CC -!- FUNCTION: Catalyzes the de novo synthesis of acetyl-CoA in vitro (By
CC similarity). Promotes acetylation of CTTN, possibly by providing the
CC acetyl donor, ensuring correct dendritic spine morphology and synaptic
CC transmission (By similarity). Binds to follistatin-related protein
CC FSTL1 and may act as a cell surface receptor for FSTL1, contributing to
CC AKT activation and subsequent FSTL1-induced survival and function of
CC endothelial cells and cardiac myocytes (PubMed:20054002).
CC {ECO:0000250|UniProtKB:Q8BWT5, ECO:0000269|PubMed:20054002}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetate + ATP + CoA = acetyl-CoA + AMP + diphosphate;
CC Xref=Rhea:RHEA:23176, ChEBI:CHEBI:30089, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:57287, ChEBI:CHEBI:57288,
CC ChEBI:CHEBI:456215; EC=6.2.1.1;
CC Evidence={ECO:0000250|UniProtKB:Q8BWT5};
CC -!- SUBUNIT: Interacts with FSTL1; DIP2A may act as a cell surface receptor
CC for FSTL1 (PubMed:20860622, PubMed:20054002). Interacts (via N-
CC terminus) with CTTN (via SH3 domain); the interaction promotes
CC acetylation of CTTN and is required for proper synaptic transmission
CC (By similarity). Interacts with SHANK3 (By similarity).
CC {ECO:0000250|UniProtKB:Q8BWT5, ECO:0000269|PubMed:20054002,
CC ECO:0000269|PubMed:20860622}.
CC -!- INTERACTION:
CC Q14689; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-2564275, EBI-744115;
CC Q14689; Q7L5A3: FAM214B; NbExp=3; IntAct=EBI-2564275, EBI-745689;
CC Q14689; P19883: FST; NbExp=2; IntAct=EBI-2564275, EBI-1571188;
CC Q14689; Q12841: FSTL1; NbExp=4; IntAct=EBI-2564275, EBI-2349801;
CC Q14689; Q9NWQ4: GPATCH2L; NbExp=3; IntAct=EBI-2564275, EBI-5666657;
CC Q14689; P01137: TGFB1; NbExp=2; IntAct=EBI-2564275, EBI-779636;
CC Q14689; Q15645: TRIP13; NbExp=3; IntAct=EBI-2564275, EBI-358993;
CC Q14689; Q62356: Fstl1; Xeno; NbExp=3; IntAct=EBI-2564275, EBI-2564326;
CC Q14689-3; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-25858204, EBI-702390;
CC Q14689-3; P14136: GFAP; NbExp=3; IntAct=EBI-25858204, EBI-744302;
CC Q14689-4; Q8NA54: IQUB; NbExp=3; IntAct=EBI-12019962, EBI-10220600;
CC Q14689-6; Q6UY14-3: ADAMTSL4; NbExp=3; IntAct=EBI-10233719, EBI-10173507;
CC Q14689-6; Q9NS73-5: MBIP; NbExp=3; IntAct=EBI-10233719, EBI-10182361;
CC Q14689-6; P61289: PSME3; NbExp=3; IntAct=EBI-10233719, EBI-355546;
CC Q14689-6; P26045: PTPN3; NbExp=3; IntAct=EBI-10233719, EBI-1047946;
CC Q14689-6; O60504: SORBS3; NbExp=3; IntAct=EBI-10233719, EBI-741237;
CC Q14689-6; Q96MF2: STAC3; NbExp=3; IntAct=EBI-10233719, EBI-745680;
CC Q14689-6; Q08117: TLE5; NbExp=3; IntAct=EBI-10233719, EBI-717810;
CC Q14689-6; Q9HCM9: TRIM39; NbExp=3; IntAct=EBI-10233719, EBI-739510;
CC Q14689-6; Q15645: TRIP13; NbExp=3; IntAct=EBI-10233719, EBI-358993;
CC Q14689-6; O43298: ZBTB43; NbExp=3; IntAct=EBI-10233719, EBI-740718;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:20054002};
CC Peripheral membrane protein {ECO:0000305}. Mitochondrion
CC {ECO:0000250|UniProtKB:Q8BWT5}. Cell projection, dendritic spine
CC {ECO:0000250|UniProtKB:Q8BWT5}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q14689-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14689-2; Sequence=VSP_007749;
CC Name=3;
CC IsoId=Q14689-3; Sequence=VSP_007748, VSP_007749;
CC Name=4;
CC IsoId=Q14689-4; Sequence=VSP_007750, VSP_007751;
CC Name=5;
CC IsoId=Q14689-5; Sequence=VSP_045408, VSP_045409, VSP_045410;
CC Name=6;
CC IsoId=Q14689-6; Sequence=VSP_047246;
CC -!- TISSUE SPECIFICITY: Low expression in all tissues tested.
CC -!- SIMILARITY: Belongs to the DIP2 family. {ECO:0000305}.
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DR EMBL; AF490768; AAM18046.1; -; mRNA.
DR EMBL; AB273729; BAF69070.1; -; mRNA.
DR EMBL; AK056738; BAB71268.1; -; mRNA.
DR EMBL; AK303351; BAG64412.1; -; mRNA.
DR EMBL; AP000337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AP000338; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC033718; AAH33718.1; -; mRNA.
DR EMBL; BC038443; AAH38443.1; -; mRNA.
DR EMBL; D80006; BAA11501.1; -; mRNA.
DR CCDS; CCDS46655.1; -. [Q14689-1]
DR CCDS; CCDS46656.1; -. [Q14689-4]
DR CCDS; CCDS46657.1; -. [Q14689-2]
DR CCDS; CCDS54490.1; -. [Q14689-6]
DR CCDS; CCDS54491.1; -. [Q14689-3]
DR RefSeq; NP_001139587.1; NM_001146115.1. [Q14689-3]
DR RefSeq; NP_001139588.1; NM_001146116.1. [Q14689-6]
DR RefSeq; NP_055966.2; NM_015151.3. [Q14689-1]
DR RefSeq; NP_996772.1; NM_206889.2. [Q14689-4]
DR RefSeq; NP_996773.1; NM_206890.2. [Q14689-2]
DR RefSeq; NP_996774.1; NM_206891.2.
DR RefSeq; XP_016883784.1; XM_017028295.1. [Q14689-1]
DR RefSeq; XP_016883785.1; XM_017028296.1.
DR AlphaFoldDB; Q14689; -.
DR SMR; Q14689; -.
DR BioGRID; 116793; 99.
DR IntAct; Q14689; 40.
DR MINT; Q14689; -.
DR STRING; 9606.ENSP00000392066; -.
DR GlyGen; Q14689; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; Q14689; -.
DR PhosphoSitePlus; Q14689; -.
DR BioMuta; DIP2A; -.
DR DMDM; 32700084; -.
DR EPD; Q14689; -.
DR jPOST; Q14689; -.
DR MassIVE; Q14689; -.
DR MaxQB; Q14689; -.
DR PaxDb; Q14689; -.
DR PeptideAtlas; Q14689; -.
DR PRIDE; Q14689; -.
DR ProteomicsDB; 16898; -.
DR ProteomicsDB; 60124; -. [Q14689-1]
DR ProteomicsDB; 60125; -. [Q14689-2]
DR ProteomicsDB; 60126; -. [Q14689-3]
DR ProteomicsDB; 60127; -. [Q14689-4]
DR Antibodypedia; 24717; 152 antibodies from 20 providers.
DR DNASU; 23181; -.
DR Ensembl; ENST00000400274.5; ENSP00000383133.1; ENSG00000160305.18. [Q14689-6]
DR Ensembl; ENST00000417564.3; ENSP00000392066.2; ENSG00000160305.18. [Q14689-1]
DR Ensembl; ENST00000435722.7; ENSP00000415089.3; ENSG00000160305.18. [Q14689-2]
DR Ensembl; ENST00000457905.7; ENSP00000393434.3; ENSG00000160305.18. [Q14689-4]
DR Ensembl; ENST00000466639.5; ENSP00000430249.1; ENSG00000160305.18. [Q14689-3]
DR GeneID; 23181; -.
DR KEGG; hsa:23181; -.
DR MANE-Select; ENST00000417564.3; ENSP00000392066.2; NM_015151.4; NP_055966.2.
DR UCSC; uc002zjm.4; human. [Q14689-1]
DR CTD; 23181; -.
DR DisGeNET; 23181; -.
DR GeneCards; DIP2A; -.
DR HGNC; HGNC:17217; DIP2A.
DR HPA; ENSG00000160305; Low tissue specificity.
DR MIM; 607711; gene.
DR neXtProt; NX_Q14689; -.
DR OpenTargets; ENSG00000160305; -.
DR PharmGKB; PA134888233; -.
DR VEuPathDB; HostDB:ENSG00000160305; -.
DR eggNOG; KOG3628; Eukaryota.
DR GeneTree; ENSGT00950000182997; -.
DR HOGENOM; CLU_001345_0_0_1; -.
DR InParanoid; Q14689; -.
DR OMA; HTQIENH; -.
DR OrthoDB; 539697at2759; -.
DR PhylomeDB; Q14689; -.
DR TreeFam; TF312871; -.
DR PathwayCommons; Q14689; -.
DR SignaLink; Q14689; -.
DR SIGNOR; Q14689; -.
DR BioGRID-ORCS; 23181; 9 hits in 1083 CRISPR screens.
DR ChiTaRS; DIP2A; human.
DR GeneWiki; DIP2A; -.
DR GenomeRNAi; 23181; -.
DR Pharos; Q14689; Tbio.
DR PRO; PR:Q14689; -.
DR Proteomes; UP000005640; Chromosome 21.
DR RNAct; Q14689; protein.
DR Bgee; ENSG00000160305; Expressed in visceral pleura and 204 other tissues.
DR ExpressionAtlas; Q14689; baseline and differential.
DR Genevisible; Q14689; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0043197; C:dendritic spine; ISS:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003987; F:acetate-CoA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0006085; P:acetyl-CoA biosynthetic process; ISS:UniProtKB.
DR GO; GO:0060997; P:dendritic spine morphogenesis; ISS:UniProtKB.
DR GO; GO:0010629; P:negative regulation of gene expression; IDA:UniProtKB.
DR GO; GO:2000758; P:positive regulation of peptidyl-lysine acetylation; ISS:UniProtKB.
DR CDD; cd05905; Dip2; 2.
DR Gene3D; 3.30.300.30; -; 2.
DR Gene3D; 3.40.50.12780; -; 2.
DR InterPro; IPR045851; AMP-bd_C_sf.
DR InterPro; IPR000873; AMP-dep_Synth/Lig.
DR InterPro; IPR042099; ANL_N_sf.
DR InterPro; IPR037337; Dip2-like_dom.
DR InterPro; IPR010506; DMAP1-bd.
DR Pfam; PF00501; AMP-binding; 2.
DR Pfam; PF06464; DMAP_binding; 1.
DR SMART; SM01137; DMAP_binding; 1.
DR PROSITE; PS51912; DMAP1_BIND; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection;
KW Developmental protein; Ligase; Membrane; Mitochondrion; Neurogenesis;
KW Phosphoprotein; Reference proteome; Synapse.
FT CHAIN 1..1571
FT /note="Disco-interacting protein 2 homolog A"
FT /id="PRO_0000079906"
FT DOMAIN 9..127
FT /note="DMAP1-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01260"
FT REGION 60..203
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 283..286
FT /note="PXXP motif; required for interaction with CTTN"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT5"
FT MOTIF 307..310
FT /note="PXXP motif; required for interaction with CTTN"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT5"
FT COMPBIAS 64..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..140
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 168..191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 94
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 132
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8BWT5"
FT MOD_RES 155
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 31..94
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045408"
FT VAR_SEQ 219..261
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007748"
FT VAR_SEQ 302..305
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:12036298"
FT /id="VSP_047246"
FT VAR_SEQ 842..1571
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_007749"
FT VAR_SEQ 880..889
FT /note="AIDSIHQVGV -> VGAPARPMVR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007750"
FT VAR_SEQ 890..1571
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_007751"
FT VAR_SEQ 1167..1174
FT /note="MSHAATSA -> AGRGGSRL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045409"
FT VAR_SEQ 1175..1571
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045410"
FT VARIANT 191
FT /note="P -> A (in dbSNP:rs7283507)"
FT /id="VAR_047372"
FT VARIANT 372
FT /note="S -> N (in dbSNP:rs16979312)"
FT /id="VAR_047373"
FT CONFLICT 702
FT /note="V -> F (in Ref. 3; BAG64412)"
FT /evidence="ECO:0000305"
FT CONFLICT 1541
FT /note="P -> L (in Ref. 2; BAF69070)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1571 AA; 170369 MW; 40652BEFA5E9DD7C CRC64;
MADRGCPLEA APLPAEVRES LAELELELSE GDITQKGYEK KRAKLLARYI PLIQGIDPSL
QAENRIPGPS QTTAAAPKQQ KSRPTASRDE RFRSDVHTEA VQAALAKYKE RKMPMPSKRR
SVLVHSSVET YTPPDTSSAS EDEGSLRRPG RLTSTPLQSH SSVEPWLDRV IQGSSTSSSA
SSTSSHPGGR PTTAPSAAAT PGAAATTALA GLEAHTHIDL HSAPPDVTTG LVEHSYFERP
QVASVRSVPR GCSGSMLETA DGVPVNSRVS SKIQQLLNTL KRPKRPPLKE FFVDDFEELL
EVQQPDPNQP KPEGSETSVL RGEPLTAGVP RPPSLLATLQ RWGTTQPKSP CLTALDTTGK
AVYTLTYGKL WSRSLKLAYT LLNKLTSKNE PLLKPGDRVA LVFPNSDPVM FMVAFYGCLL
AELVPVPIEV PLTRKDAGSQ QVGFLLGSCG VFLALTTDAC QKGLPKAQTG EVAAFKGWPP
LSWLVIDGKH LAKPPKDWHP LAQDTGTGTA YIEYKTSKEG STVGVTVSHA SLLAQCRALT
QACGYSEAET LTNVLDFKRD AGLWHGVLTS VMNRMHVVSV PYALMKANPL SWIQKVCFYK
ARAALVKSRD MHWSLLAQRG QRDVSLSSLR MLIVADGANP WSISSCDAFL NVFQSRGLRP
EVICPCASSP EALTVAIRRP PDLGGPPPRK AVLSMNGLSY GVIRVDTEEK LSVLTVQDVG
QVMPGANVCV VKLEGTPYLC KTDEVGEICV SSSATGTAYY GLLGITKNVF EAVPVTTGGA
PIFDRPFTRT GLLGFIGPDN LVFIVGKLDG LMVTGVRRHN ADDVVATALA VEPMKFVYRG
RIAVFSVTVL HDDRIVLVAE QRPDASEEDS FQWMSRVLQA IDSIHQVGVY CLALVPANTL
PKAPLGGIHI SETKQRFLEG TLHPCNVLMC PHTCVTNLPK PRQKQPEVGP ASMIVGNLVA
GKRIAQASGR ELAHLEDSDQ ARKFLFLADV LQWRAHTTPD HPLFLLLNAK GTVTSTATCV
QLHKRAERVA AALMEKGRLS VGDHVALVYP PGVDLIAAFY GCLYCGCVPV TVRPPHPQNL
GTTLPTVKMI VEVSKSACVL TTQAVTRLLR SKEAAAAVDI RTWPTILDTD DIPKKKIASV
FRPPSPDVLA YLDFSVSTTG ILAGVKMSHA ATSALCRSIK LQCELYPSRQ IAICLDPYCG
LGFALWCLCS VYSGHQSVLV PPLELESNVS LWLSAVSQYK ARVTFCSYSV MEMCTKGLGA
QTGVLRMKGV NLSCVRTCMV VAEERPRIAL TQSFSKLFKD LGLPARAVST TFGCRVNVAI
CLQGTAGPDP TTVYVDMRAL RHDRVRLVER GSPHSLPLME SGKILPGVKV IIAHTETKGP
LGDSHLGEIW VSSPHNATGY YTVYGEEALH ADHFSARLSF GDTQTIWART GYLGFLRRTE
LTDASGGRHD ALYVVGSLDE TLELRGMRYH PIDIETSVIR AHRSIAECAV FTWTNLLVVV
VELDGLEQDA LDLVALVTNV VLEEHYLVVG VVVIVDPGVI PINSRGEKQR MHLRDGFLAD
QLDPIYVAYN M
