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   27-MAR-2024, entry version 183.
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; Q7L5A3: ATOSB; NbExp=3; IntAct=EBI-2564275, EBI-745689;
CC       Q14689; Q9C0F1: CEP44; NbExp=3; IntAct=EBI-2564275, EBI-744115;
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.
DR   RefSeq; XP_016883785.1; XM_017028296.1.
DR   AlphaFoldDB; Q14689; -.
DR   SMR; Q14689; -.
DR   BioGRID; 116793; 111.
DR   IntAct; Q14689; 47.
DR   MINT; Q14689; -.
DR   STRING; 9606.ENSP00000392066; -.
DR   GlyCosmos; Q14689; 2 sites, 1 glycan.
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; 9606-ENSP00000392066; -.
DR   PeptideAtlas; 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   Pumba; Q14689; -.
DR   Antibodypedia; 24717; 176 antibodies from 21 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   AGR; HGNC:17217; -.
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; CERPQVA; -.
DR   OrthoDB; 3994129at2759; -.
DR   PhylomeDB; Q14689; -.
DR   TreeFam; TF312871; -.
DR   PathwayCommons; Q14689; -.
DR   SignaLink; Q14689; -.
DR   SIGNOR; Q14689; -.
DR   BioGRID-ORCS; 23181; 9 hits in 1161 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 206 other cell types or tissues.
DR   ExpressionAtlas; Q14689; baseline and differential.
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; N-terminal domain of ligase-like; 2.
DR   InterPro; IPR045851; AMP-bd_C_sf.
DR   InterPro; IPR000873; AMP-dep_Synth/Lig_com.
DR   InterPro; IPR042099; ANL_N_sf.
DR   InterPro; IPR037337; Dip2-like_dom.
DR   InterPro; IPR010506; DMAP1-bd.
DR   PANTHER; PTHR22754; DISCO-INTERACTING PROTEIN 2 DIP2 -RELATED; 1.
DR   PANTHER; PTHR22754:SF34; DISCO-INTERACTING PROTEIN 2 HOMOLOG A; 1.
DR   Pfam; PF00501; AMP-binding; 2.
DR   Pfam; PF06464; DMAP_binding; 1.
DR   SMART; SM01137; DMAP_binding; 1.
DR   SUPFAM; SSF56801; Acetyl-CoA synthetase-like; 2.
DR   PROSITE; PS51912; DMAP1_BIND; 1.
DR   Genevisible; Q14689; HS.
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
//