PLXD1_HUMAN
ID PLXD1_HUMAN Reviewed; 1925 AA.
AC Q9Y4D7; A7E2C6; C9JPZ6; Q6PJS9; Q8IZJ2; Q9BTQ2;
DT 31-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 177.
DE RecName: Full=Plexin-D1;
DE Flags: Precursor;
GN Name=PLXND1; Synonyms=KIAA0620;
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 [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANTS ARG-894
RP AND ASN-1542.
RC TISSUE=Brain;
RX PubMed=9734811; DOI=10.1093/dnares/5.3.169;
RA Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H.,
RA Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. X. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:169-176(1998).
RN [2]
RP SEQUENCE REVISION.
RA Ohara O., Suyama M., Nagase T., Ishikawa K.;
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, AND VARIANTS
RP VARIANT ARG-894 AND ASN-1542.
RX PubMed=12412018; DOI=10.1002/dvdy.10159;
RA van der Zwaag B., Hellemons A.J.C.G.M., Leenders W.P.J., Burbach J.P.H.,
RA Brunner H.G., Padberg G.W., Van Bokhoven H.;
RT "PLEXIN-D1, a novel plexin family member, is expressed in vascular
RT endothelium and the central nervous system during mouse embryogenesis.";
RL Dev. Dyn. 225:336-343(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16641997; DOI=10.1038/nature04728;
RA Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT "The DNA sequence, annotation and analysis of human chromosome 3.";
RL Nature 440:1194-1198(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1386-1925 (ISOFORMS 1 AND 2), AND
RP VARIANT ASN-1542.
RC TISSUE=Muscle, 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 [6]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-500.
RC TISSUE=Plasma;
RX PubMed=16335952; DOI=10.1021/pr0502065;
RA Liu T., Qian W.-J., Gritsenko M.A., Camp D.G. II, Monroe M.E., Moore R.J.,
RA Smith R.D.;
RT "Human plasma N-glycoproteome analysis by immunoaffinity subtraction,
RT hydrazide chemistry, and mass spectrometry.";
RL J. Proteome Res. 4:2070-2080(2005).
RN [7]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-500.
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 [8]
RP FUNCTION.
RX PubMed=20385769; DOI=10.1128/mcb.01652-09;
RA Sakurai A., Gavard J., Annas-Linhares Y., Basile J.R., Amornphimoltham P.,
RA Palmby T.R., Yagi H., Zhang F., Randazzo P.A., Li X., Weigert R.,
RA Gutkind J.S.;
RT "Semaphorin 3E initiates antiangiogenic signaling through plexin D1 by
RT regulating Arf6 and R-Ras.";
RL Mol. Cell. Biol. 30:3086-3098(2010).
RN [9]
RP INTERACTION WITH SH3BP1, AND SUBCELLULAR LOCATION.
RX PubMed=24841563; DOI=10.1083/jcb.201309004;
RA Tata A., Stoppel D.C., Hong S., Ben-Zvi A., Xie T., Gu C.;
RT "An image-based RNAi screen identifies SH3BP1 as a key effector of
RT Semaphorin 3E-PlexinD1 signaling.";
RL J. Cell Biol. 205:573-590(2014).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 1553-1678.
RG Structural genomics consortium (SGC);
RT "Crystal structure of the ubiquitin-like domain of plexin D1.";
RL Submitted (MAY-2009) to the PDB data bank.
CC -!- FUNCTION: Cell surface receptor for SEMA4A and for class 3 semaphorins,
CC such as SEMA3A, SEMA3C and SEMA3E. Plays an important role in cell-cell
CC signaling, and in regulating the migration of a wide spectrum of cell
CC types. Regulates the migration of thymocytes in the medulla. Regulates
CC endothelial cell migration. Plays an important role in ensuring the
CC specificity of synapse formation. Required for normal development of
CC the heart and vasculature (By similarity). Mediates anti-angiogenic
CC signaling in response to SEMA3E. {ECO:0000250,
CC ECO:0000269|PubMed:20385769}.
CC -!- SUBUNIT: Interacts with NRP1 and SEMA4A (By similarity). Interacts with
CC SH3BP1; they dissociate upon SEMA3E binding to PLXND1 allowing SH3BP1
CC to transduce downstream signal through RAC1 inactivation
CC (PubMed:24841563). {ECO:0000250|UniProtKB:Q3UH93,
CC ECO:0000269|PubMed:24841563}.
CC -!- INTERACTION:
CC Q9Y4D7; P09067: HOXB5; NbExp=3; IntAct=EBI-310731, EBI-3893317;
CC Q9Y4D7; P22736: NR4A1; NbExp=2; IntAct=EBI-310731, EBI-721550;
CC Q9Y4D7; O15041: SEMA3E; NbExp=2; IntAct=EBI-310731, EBI-7283693;
CC Q9Y4D7; Q9H3S1: SEMA4A; NbExp=2; IntAct=EBI-310731, EBI-3924922;
CC Q9Y4D7; P70275: Sema3e; Xeno; NbExp=2; IntAct=EBI-310731, EBI-8876322;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q3UH93};
CC Single-pass membrane protein {ECO:0000250|UniProtKB:Q3UH93}. Cell
CC projection, lamellipodium membrane {ECO:0000269|PubMed:24841563}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y4D7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y4D7-2; Sequence=VSP_011516;
CC -!- TISSUE SPECIFICITY: Detected at low levels in heart, placenta, lung,
CC skeletal muscle, kidney, thymus and liver. Detected at very low levels
CC in brain, colon, spleen, small intestine and peripheral blood
CC leukocytes. {ECO:0000269|PubMed:12412018}.
CC -!- SIMILARITY: Belongs to the plexin family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA31595.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB014520; BAA31595.2; ALT_INIT; mRNA.
DR EMBL; AY116661; AAM49063.1; -; mRNA.
DR EMBL; AC023162; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC080007; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003526; AAH03526.1; -; mRNA.
DR EMBL; BC011848; AAH11848.1; -; mRNA.
DR EMBL; BC150280; AAI50281.1; -; mRNA.
DR CCDS; CCDS33854.1; -. [Q9Y4D7-1]
DR RefSeq; NP_055918.2; NM_015103.2. [Q9Y4D7-1]
DR PDB; 3H6N; X-ray; 2.00 A; A=1553-1678.
DR PDBsum; 3H6N; -.
DR AlphaFoldDB; Q9Y4D7; -.
DR SMR; Q9Y4D7; -.
DR BioGRID; 116747; 23.
DR CORUM; Q9Y4D7; -.
DR IntAct; Q9Y4D7; 12.
DR MINT; Q9Y4D7; -.
DR STRING; 9606.ENSP00000317128; -.
DR GlyConnect; 1615; 4 N-Linked glycans (2 sites).
DR GlyGen; Q9Y4D7; 20 sites, 4 N-linked glycans (2 sites), 1 O-linked glycan (1 site).
DR iPTMnet; Q9Y4D7; -.
DR PhosphoSitePlus; Q9Y4D7; -.
DR BioMuta; PLXND1; -.
DR DMDM; 296452982; -.
DR EPD; Q9Y4D7; -.
DR jPOST; Q9Y4D7; -.
DR MassIVE; Q9Y4D7; -.
DR MaxQB; Q9Y4D7; -.
DR PaxDb; Q9Y4D7; -.
DR PeptideAtlas; Q9Y4D7; -.
DR PRIDE; Q9Y4D7; -.
DR ProteomicsDB; 86168; -. [Q9Y4D7-1]
DR ProteomicsDB; 86169; -. [Q9Y4D7-2]
DR Antibodypedia; 33285; 256 antibodies from 34 providers.
DR DNASU; 23129; -.
DR Ensembl; ENST00000324093.9; ENSP00000317128.4; ENSG00000004399.13. [Q9Y4D7-1]
DR GeneID; 23129; -.
DR KEGG; hsa:23129; -.
DR MANE-Select; ENST00000324093.9; ENSP00000317128.4; NM_015103.3; NP_055918.3.
DR UCSC; uc003emx.3; human. [Q9Y4D7-1]
DR CTD; 23129; -.
DR DisGeNET; 23129; -.
DR GeneCards; PLXND1; -.
DR HGNC; HGNC:9107; PLXND1.
DR HPA; ENSG00000004399; Low tissue specificity.
DR MalaCards; PLXND1; -.
DR MIM; 604282; gene.
DR neXtProt; NX_Q9Y4D7; -.
DR OpenTargets; ENSG00000004399; -.
DR Orphanet; 570; Moebius syndrome.
DR Orphanet; 3384; Truncus arteriosus.
DR PharmGKB; PA128394602; -.
DR VEuPathDB; HostDB:ENSG00000004399; -.
DR eggNOG; KOG3610; Eukaryota.
DR GeneTree; ENSGT01020000230394; -.
DR HOGENOM; CLU_001436_1_1_1; -.
DR InParanoid; Q9Y4D7; -.
DR OMA; NESVVRC; -.
DR OrthoDB; 90434at2759; -.
DR PhylomeDB; Q9Y4D7; -.
DR TreeFam; TF312962; -.
DR PathwayCommons; Q9Y4D7; -.
DR Reactome; R-HSA-416700; Other semaphorin interactions.
DR Reactome; R-HSA-9013508; NOTCH3 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-9696270; RND2 GTPase cycle.
DR SignaLink; Q9Y4D7; -.
DR BioGRID-ORCS; 23129; 18 hits in 1084 CRISPR screens.
DR ChiTaRS; PLXND1; human.
DR EvolutionaryTrace; Q9Y4D7; -.
DR GeneWiki; PLXND1; -.
DR GenomeRNAi; 23129; -.
DR Pharos; Q9Y4D7; Tbio.
DR PRO; PR:Q9Y4D7; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q9Y4D7; protein.
DR Bgee; ENSG00000004399; Expressed in upper lobe of left lung and 194 other tissues.
DR ExpressionAtlas; Q9Y4D7; baseline and differential.
DR Genevisible; Q9Y4D7; HS.
DR GO; GO:0030424; C:axon; IEA:Ensembl.
DR GO; GO:0044297; C:cell body; IEA:Ensembl.
DR GO; GO:0005887; C:integral component of plasma membrane; ISS:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IDA:UniProtKB.
DR GO; GO:0031258; C:lamellipodium membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0002116; C:semaphorin receptor complex; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0017154; F:semaphorin receptor activity; ISS:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; ISS:UniProtKB.
DR GO; GO:0035904; P:aorta development; IEA:Ensembl.
DR GO; GO:0001569; P:branching involved in blood vessel morphogenesis; IEA:Ensembl.
DR GO; GO:0003279; P:cardiac septum development; IEA:Ensembl.
DR GO; GO:0060976; P:coronary vasculature development; IEA:Ensembl.
DR GO; GO:0060666; P:dichotomous subdivision of terminal units involved in salivary gland branching; IEA:Ensembl.
DR GO; GO:0043542; P:endothelial cell migration; ISS:UniProtKB.
DR GO; GO:0001822; P:kidney development; IEA:Ensembl.
DR GO; GO:0007162; P:negative regulation of cell adhesion; IBA:GO_Central.
DR GO; GO:0043524; P:negative regulation of neuron apoptotic process; IEA:Ensembl.
DR GO; GO:0003151; P:outflow tract morphogenesis; IEA:Ensembl.
DR GO; GO:0050772; P:positive regulation of axonogenesis; IBA:GO_Central.
DR GO; GO:0032092; P:positive regulation of protein binding; IEA:Ensembl.
DR GO; GO:0045765; P:regulation of angiogenesis; ISS:UniProtKB.
DR GO; GO:0030334; P:regulation of cell migration; ISS:UniProtKB.
DR GO; GO:0008360; P:regulation of cell shape; IBA:GO_Central.
DR GO; GO:0043087; P:regulation of GTPase activity; IBA:GO_Central.
DR GO; GO:0071526; P:semaphorin-plexin signaling pathway; ISS:UniProtKB.
DR GO; GO:1902287; P:semaphorin-plexin signaling pathway involved in axon guidance; IBA:GO_Central.
DR GO; GO:0007416; P:synapse assembly; ISS:UniProtKB.
DR CDD; cd11247; Sema_plexin_D1; 1.
DR Gene3D; 1.10.506.10; -; 2.
DR Gene3D; 2.130.10.10; -; 1.
DR Gene3D; 2.60.40.10; -; 5.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR002909; IPT_dom.
DR InterPro; IPR031148; Plexin.
DR InterPro; IPR042719; Plexin-D1_Sema.
DR InterPro; IPR013548; Plexin_cytoplasmic_RasGAP_dom.
DR InterPro; IPR002165; Plexin_repeat.
DR InterPro; IPR016201; PSI.
DR InterPro; IPR008936; Rho_GTPase_activation_prot.
DR InterPro; IPR001627; Semap_dom.
DR InterPro; IPR036352; Semap_dom_sf.
DR InterPro; IPR041019; TIG1_plexin.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR PANTHER; PTHR22625; PTHR22625; 1.
DR Pfam; PF08337; Plexin_cytopl; 2.
DR Pfam; PF01437; PSI; 2.
DR Pfam; PF01403; Sema; 1.
DR Pfam; PF01833; TIG; 3.
DR Pfam; PF17960; TIG_plexin; 1.
DR SMART; SM00429; IPT; 3.
DR SMART; SM00423; PSI; 3.
DR SMART; SM00630; Sema; 1.
DR SUPFAM; SSF101912; SSF101912; 1.
DR SUPFAM; SSF48350; SSF48350; 1.
DR SUPFAM; SSF81296; SSF81296; 3.
DR PROSITE; PS51004; SEMA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Angiogenesis; Cell membrane;
KW Cell projection; Developmental protein; Disulfide bond; Glycoprotein;
KW Membrane; Receptor; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..46
FT /evidence="ECO:0000255"
FT CHAIN 47..1925
FT /note="Plexin-D1"
FT /id="PRO_0000024676"
FT TOPO_DOM 47..1271
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1272..1292
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1293..1925
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 47..546
FT /note="Sema"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DOMAIN 891..979
FT /note="IPT/TIG 1"
FT DOMAIN 981..1066
FT /note="IPT/TIG 2"
FT DOMAIN 1069..1160
FT /note="IPT/TIG 3"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 86
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 155
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 188
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 224
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 481
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 500
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:16335952,
FT ECO:0000269|PubMed:19159218"
FT CARBOHYD 583
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 696
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 736
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 802
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 965
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1017
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1060
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1099
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1118
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1132
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1237
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 104..114
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 140..148
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 322..445
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 345..389
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 549..566
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 555..600
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 558..575
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 569..581
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT DISULFID 637..661
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00352"
FT VAR_SEQ 1766..1925
FT /note="SLPLRFWVNILKNPQFVFDIDKTDHIDACLSVIAQAFIDACSISDLQLGKDS
FT PTNKLLYAKEIPEYRKIVQRYYKQIQDMTPLSEQEMNAHLAEESRKYQNEFNTNVAMAE
FT IYKYAKRYRPQIMAALEANPTARRTQLQHKFEQVVALMEDNIYECYSEA -> RWRPSS
FT PVLGEHPEEPPVCL (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_011516"
FT VARIANT 617
FT /note="P -> S (in dbSNP:rs2285372)"
FT /id="VAR_056723"
FT VARIANT 870
FT /note="M -> V (in dbSNP:rs2255703)"
FT /id="VAR_022144"
FT VARIANT 894
FT /note="H -> R (in dbSNP:rs2625962)"
FT /evidence="ECO:0000269|PubMed:12412018,
FT ECO:0000269|PubMed:9734811"
FT /id="VAR_059558"
FT VARIANT 1412
FT /note="L -> V (in dbSNP:rs2625973)"
FT /id="VAR_056724"
FT VARIANT 1542
FT /note="S -> N (in dbSNP:rs2713625)"
FT /evidence="ECO:0000269|PubMed:12412018,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9734811"
FT /id="VAR_061539"
FT CONFLICT 531
FT /note="G -> V (in Ref. 1; BAA31595 and 3; AAM49063)"
FT /evidence="ECO:0000305"
FT STRAND 1555..1563
FT /evidence="ECO:0007829|PDB:3H6N"
FT STRAND 1570..1575
FT /evidence="ECO:0007829|PDB:3H6N"
FT HELIX 1580..1591
FT /evidence="ECO:0007829|PDB:3H6N"
FT HELIX 1597..1599
FT /evidence="ECO:0007829|PDB:3H6N"
FT HELIX 1603..1605
FT /evidence="ECO:0007829|PDB:3H6N"
FT STRAND 1606..1611
FT /evidence="ECO:0007829|PDB:3H6N"
FT STRAND 1613..1615
FT /evidence="ECO:0007829|PDB:3H6N"
FT STRAND 1617..1619
FT /evidence="ECO:0007829|PDB:3H6N"
FT STRAND 1622..1624
FT /evidence="ECO:0007829|PDB:3H6N"
FT TURN 1639..1643
FT /evidence="ECO:0007829|PDB:3H6N"
FT STRAND 1649..1654
FT /evidence="ECO:0007829|PDB:3H6N"
SQ SEQUENCE 1925 AA; 212007 MW; 28967933B2D17CE1 CRC64;
MAPRAAGGAP LSARAAAASP PPFQTPPRCP VPLLLLLLLG AARAGALEIQ RRFPSPTPTN
NFALDGAAGT VYLAAVNRLY QLSGANLSLE AEAAVGPVPD SPLCHAPQLP QASCEHPRRL
TDNYNKILQL DPGQGLVVVC GSIYQGFCQL RRRGNISAVA VRFPPAAPPA EPVTVFPSML
NVAANHPNAS TVGLVLPPAA GAGGSRLLVG ATYTGYGSSF FPRNRSLEDH RFENTPEIAI
RSLDTRGDLA KLFTFDLNPS DDNILKIKQG AKEQHKLGFV SAFLHPSDPP PGAQSYAYLA
LNSEARAGDK ESQARSLLAR ICLPHGAGGD AKKLTESYIQ LGLQCAGGAG RGDLYSRLVS
VFPARERLFA VFERPQGSPA ARAAPAALCA FRFADVRAAI RAARTACFVE PAPDVVAVLD
SVVQGTGPAC ERKLNIQLQP EQLDCGAAHL QHPLSILQPL KATPVFRAPG LTSVAVASVN
NYTAVFLGTV NGRLLKINLN ESMQVVSRRV VTVAYGEPVH HVMQFDPADS GYLYLMTSHQ
MARVKVAACN VHSTCGDCVG AADAYCGWCA LETRCTLQQD CTNSSQQHFW TSASEGPSRC
PAMTVLPSEI DVRQEYPGMI LQISGSLPSL SGMEMACDYG NNIRTVARVP GPAFGHQIAY
CNLLPRDQFP PFPPNQDHVT VEMSVRVNGR NIVKANFTIY DCSRTAQVYP HTACTSCLSA
QWPCFWCSQQ HSCVSNQSRC EASPNPTSPQ DCPRTLLSPL APVPTGGSQN ILVPLANTAF
FQGAALECSF GLEEIFEAVW VNESVVRCDQ VVLHTTRKSQ VFPLSLQLKG RPARFLDSPE
PMTVMVYNCA MGSPDCSQCL GREDLGHLCM WSDGCRLRGP LQPMAGTCPA PEIHAIEPLS
GPLDGGTLLT IRGRNLGRRL SDVAHGVWIG GVACEPLPDR YTVSEEIVCV TGPAPGPLSG
VVTVNASKEG KSRDRFSYVL PLVHSLEPTM GPKAGGTRIT IHGNDLHVGS ELQVLVNDTD
PCTELMRTDT SIACTMPEGA LPAPVPVCVR FERRGCVHGN LTFWYMQNPV ITAISPRRSP
VSGGRTITVA GERFHMVQNV SMAVHHIGRE PTLCKVLNST LITCPSPGAL SNASAPVDFF
INGRAYADEV AVAEELLDPE EAQRGSRFRL DYLPNPQFST AKREKWIKHH PGEPLTLVIH
KEQDSLGLQS HEYRVKIGQV SCDIQIVSDR IIHCSVNESL GAAVGQLPIT IQVGNFNQTI
ATLQLGGSET AIIVSIVICS VLLLLSVVAL FVFCTKSRRA ERYWQKTLLQ MEEMESQIRE
EIRKGFAELQ TDMTDLTKEL NRSQGIPFLE YKHFVTRTFF PKCSSLYEER YVLPSQTLNS
QGSSQAQETH PLLGEWKIPE SCRPNMEEGI SLFSSLLNNK HFLIVFVHAL EQQKDFAVRD
RCSLASLLTI ALHGKLEYYT SIMKELLVDL IDASAAKNPK LMLRRTESVV EKMLTNWMSI
CMYSCLRETV GEPFFLLLCA IKQQINKGSI DAITGKARYT LSEEWLLREN IEAKPRNLNV
SFQGCGMDSL SVRAMDTDTL TQVKEKILEA FCKNVPYSQW PRAEDVDLEW FASSTQSYIL
RDLDDTSVVE DGRKKLNTLA HYKIPEGASL AMSLIDKKDN TLGRVKDLDT EKYFHLVLPT
DELAEPKKSH RQSHRKKVLP EIYLTRLLST KGTLQKFLDD LFKAILSIRE DKPPLAVKYF
FDFLEEQAEK RGISDPDTLH IWKTNSLPLR FWVNILKNPQ FVFDIDKTDH IDACLSVIAQ
AFIDACSISD LQLGKDSPTN KLLYAKEIPE YRKIVQRYYK QIQDMTPLSE QEMNAHLAEE
SRKYQNEFNT NVAMAEIYKY AKRYRPQIMA ALEANPTARR TQLQHKFEQV VALMEDNIYE
CYSEA
