TNPO2_HUMAN
ID TNPO2_HUMAN Reviewed; 897 AA.
AC O14787; O14655; Q6IN77;
DT 15-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 24-NOV-2009, sequence version 3.
DT 03-AUG-2022, entry version 172.
DE RecName: Full=Transportin-2;
DE AltName: Full=Karyopherin beta-2b;
GN Name=TNPO2;
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).
RX PubMed=9298975; DOI=10.1083/jcb.138.6.1181;
RA Siomi M.C., Eder P.S., Kataoka N., Wan L., Liu Q., Dreyfuss G.;
RT "Transportin-mediated nuclear import of heterogeneous nuclear RNP
RT proteins.";
RL J. Cell Biol. 138:1181-1192(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT IDDHISD ARG-32.
RA Bonifaci N., Radu A., Blobel G.;
RT "Human karyopherin beta2b: an homolog of human karyopherin beta2.";
RL Submitted (JUN-1997) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15057824; DOI=10.1038/nature02399;
RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E.,
RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A.,
RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S.,
RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A.,
RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J.,
RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M.,
RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W.,
RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V.,
RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D.,
RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I.,
RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L.,
RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A.,
RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J.,
RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
RA Rubin E.M., Lucas S.M.;
RT "The DNA sequence and biology of human chromosome 19.";
RL Nature 428:529-535(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=PNS;
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 ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-862, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [8]
RP VARIANT IDDHISD CYS-370.
RX PubMed=23033978; DOI=10.1056/nejmoa1206524;
RA de Ligt J., Willemsen M.H., van Bon B.W., Kleefstra T., Yntema H.G.,
RA Kroes T., Vulto-van Silfhout A.T., Koolen D.A., de Vries P., Gilissen C.,
RA del Rosario M., Hoischen A., Scheffer H., de Vries B.B., Brunner H.G.,
RA Veltman J.A., Vissers L.E.;
RT "Diagnostic exome sequencing in persons with severe intellectual
RT disability.";
RL N. Engl. J. Med. 367:1921-1929(2012).
RN [9]
RP VARIANTS IDDHISD ARG-28; ARG-32; ARG-61; ASN-118; ASN-156; ARG-370;
RP CYS-370; 491-LYS-ARG-492 DELINS GLN-TRP; LEU-514; VAL-546; PHE-548;
RP 649-ALA--LEU-652 DEL AND CYS-727, AND INVOLVEMENT IN IDDHISD.
RX PubMed=34314705; DOI=10.1016/j.ajhg.2021.06.019;
RG Undiagnosed Diseases Network;
RA Goodman L.D., Cope H., Nil Z., Ravenscroft T.A., Charng W.L., Lu S.,
RA Tien A.C., Pfundt R., Koolen D.A., Haaxma C.A., Veenstra-Knol H.E.,
RA Wassink-Ruiter J.S.K., Wevers M.R., Jones M., Walsh L.E., Klee V.H.,
RA Theunis M., Legius E., Steel D., Barwick K.E.S., Kurian M.A.,
RA Mohammad S.S., Dale R.C., Terhal P.A., van Binsbergen E., Kirmse B.,
RA Robinette B., Cogne B., Isidor B., Grebe T.A., Kulch P., Hainline B.E.,
RA Sapp K., Morava E., Klee E.W., Macke E.L., Trapane P., Spencer C., Si Y.,
RA Begtrup A., Moulton M.J., Dutta D., Kanca O., Wangler M.F., Yamamoto S.,
RA Bellen H.J., Tan Q.K.;
RT "TNPO2 variants associate with human developmental delays, neurologic
RT deficits, and dysmorphic features and alter TNPO2 activity in Drosophila.";
RL Am. J. Hum. Genet. 108:1669-1691(2021).
CC -!- FUNCTION: Probably functions in nuclear protein import as nuclear
CC transport receptor. Serves as receptor for nuclear localization signals
CC (NLS) in cargo substrates. Is thought to mediate docking of the
CC importin/substrate complex to the nuclear pore complex (NPC) through
CC binding to nucleoporin and the complex is subsequently translocated
CC through the pore by an energy requiring, Ran-dependent mechanism. At
CC the nucleoplasmic side of the NPC, Ran binds to the importin, the
CC importin/substrate complex dissociates and importin is re-exported from
CC the nucleus to the cytoplasm where GTP hydrolysis releases Ran. The
CC directionality of nuclear import is thought to be conferred by an
CC asymmetric distribution of the GTP- and GDP-bound forms of Ran between
CC the cytoplasm and nucleus (By similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC O14787; Q96GX9: APIP; NbExp=4; IntAct=EBI-431907, EBI-359248;
CC O14787; Q6P1W5: C1orf94; NbExp=3; IntAct=EBI-431907, EBI-946029;
CC O14787; Q13557: CAMK2D; NbExp=4; IntAct=EBI-431907, EBI-351018;
CC O14787; O00471: EXOC5; NbExp=4; IntAct=EBI-431907, EBI-949824;
CC O14787; V9HW27: HEL-S-101; NbExp=3; IntAct=EBI-431907, EBI-10178933;
CC O14787; O95198: KLHL2; NbExp=4; IntAct=EBI-431907, EBI-746999;
CC O14787; P15531: NME1; NbExp=3; IntAct=EBI-431907, EBI-741141;
CC O14787; Q96PV4: PNMA5; NbExp=3; IntAct=EBI-431907, EBI-10171633;
CC O14787; P54274: TERF1; NbExp=2; IntAct=EBI-431907, EBI-710997;
CC O14787-2; Q8N7W2-2: BEND7; NbExp=3; IntAct=EBI-12076664, EBI-10181188;
CC O14787-2; Q96CA5: BIRC7; NbExp=3; IntAct=EBI-12076664, EBI-517623;
CC O14787-2; Q13867: BLMH; NbExp=3; IntAct=EBI-12076664, EBI-718504;
CC O14787-2; Q86WS4: C12orf40; NbExp=3; IntAct=EBI-12076664, EBI-10286004;
CC O14787-2; Q13554-3: CAMK2B; NbExp=3; IntAct=EBI-12076664, EBI-11523526;
CC O14787-2; Q13555-5: CAMK2G; NbExp=3; IntAct=EBI-12076664, EBI-12020154;
CC O14787-2; P78358: CTAG1B; NbExp=3; IntAct=EBI-12076664, EBI-1188472;
CC O14787-2; P07954: FH; NbExp=3; IntAct=EBI-12076664, EBI-1050358;
CC O14787-2; Q9C0B1-2: FTO; NbExp=3; IntAct=EBI-12076664, EBI-18138793;
CC O14787-2; Q9BTY2: FUCA2; NbExp=3; IntAct=EBI-12076664, EBI-9050116;
CC O14787-2; P30793: GCH1; NbExp=3; IntAct=EBI-12076664, EBI-958183;
CC O14787-2; O15499: GSC2; NbExp=3; IntAct=EBI-12076664, EBI-19954058;
CC O14787-2; Q9BS75: KLHL20; NbExp=3; IntAct=EBI-12076664, EBI-10693436;
CC O14787-2; Q9UH77: KLHL3; NbExp=3; IntAct=EBI-12076664, EBI-8524663;
CC O14787-2; Q92876: KLK6; NbExp=3; IntAct=EBI-12076664, EBI-2432309;
CC O14787-2; O95678: KRT75; NbExp=3; IntAct=EBI-12076664, EBI-2949715;
CC O14787-2; Q8IUC2: KRTAP8-1; NbExp=3; IntAct=EBI-12076664, EBI-10261141;
CC O14787-2; P32243-2: OTX2; NbExp=3; IntAct=EBI-12076664, EBI-9087860;
CC O14787-2; Q9UKS6: PACSIN3; NbExp=3; IntAct=EBI-12076664, EBI-77926;
CC O14787-2; Q9NR12: PDLIM7; NbExp=3; IntAct=EBI-12076664, EBI-350517;
CC O14787-2; Q96BK5: PINX1; NbExp=3; IntAct=EBI-12076664, EBI-721782;
CC O14787-2; P78424: POU6F2; NbExp=3; IntAct=EBI-12076664, EBI-12029004;
CC O14787-2; Q9NR22: PRMT8; NbExp=3; IntAct=EBI-12076664, EBI-745545;
CC O14787-2; P32322: PYCR1; NbExp=3; IntAct=EBI-12076664, EBI-848624;
CC O14787-2; P62826: RAN; NbExp=3; IntAct=EBI-12076664, EBI-286642;
CC O14787-2; Q8IUH3-3: RBM45; NbExp=3; IntAct=EBI-12076664, EBI-10964453;
CC O14787-2; Q9NQG5: RPRD1B; NbExp=3; IntAct=EBI-12076664, EBI-747925;
CC O14787-2; Q9UJW9: SERTAD3; NbExp=3; IntAct=EBI-12076664, EBI-748621;
CC O14787-2; Q15637-4: SF1; NbExp=3; IntAct=EBI-12076664, EBI-12223157;
CC O14787-2; Q13207: TBX2; NbExp=3; IntAct=EBI-12076664, EBI-2853051;
CC O14787-2; Q8TBB0: THAP6; NbExp=3; IntAct=EBI-12076664, EBI-3925505;
CC O14787-2; Q9BZR9: TRIM8; NbExp=3; IntAct=EBI-12076664, EBI-2340370;
CC O14787-2; A0A0C4DGF1: ZBTB32; NbExp=3; IntAct=EBI-12076664, EBI-10188476;
CC O14787-2; Q53FD0-2: ZC2HC1C; NbExp=3; IntAct=EBI-12076664, EBI-14104088;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O14787-1; Sequence=Displayed;
CC Name=2; Synonyms=beta2b;
CC IsoId=O14787-2; Sequence=VSP_009657;
CC -!- DISEASE: Intellectual developmental disorder with hypotonia, impaired
CC speech, and dysmorphic facies (IDDHISD) [MIM:619556]: An autosomal
CC dominant disorder characterized by global developmental delay, impaired
CC intellectual development, poor or absent speech, hypotonia,
CC ophthalmologic abnormalities, and non-specific dysmorphic features.
CC Some affected individuals have seizures, and a few have involvement of
CC other organ systems. {ECO:0000269|PubMed:23033978,
CC ECO:0000269|PubMed:34314705, ECO:0000269|Ref.2}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the importin beta family. Importin beta-2
CC subfamily. {ECO:0000305}.
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DR EMBL; AF019039; AAB83973.1; -; mRNA.
DR EMBL; AF007748; AAB71349.1; -; mRNA.
DR EMBL; AC018761; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471106; EAW84300.1; -; Genomic_DNA.
DR EMBL; BC072420; AAH72420.1; -; mRNA.
DR CCDS; CCDS45991.1; -. [O14787-1]
DR CCDS; CCDS45992.1; -. [O14787-2]
DR RefSeq; NP_001129667.1; NM_001136195.1. [O14787-2]
DR RefSeq; NP_001129668.1; NM_001136196.1. [O14787-1]
DR RefSeq; NP_038461.2; NM_013433.4. [O14787-2]
DR AlphaFoldDB; O14787; -.
DR SMR; O14787; -.
DR BioGRID; 119024; 195.
DR CORUM; O14787; -.
DR IntAct; O14787; 54.
DR MINT; O14787; -.
DR STRING; 9606.ENSP00000407182; -.
DR TCDB; 1.I.1.1.3; the nuclear pore complex (npc) family.
DR GlyGen; O14787; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O14787; -.
DR PhosphoSitePlus; O14787; -.
DR BioMuta; TNPO2; -.
DR EPD; O14787; -.
DR jPOST; O14787; -.
DR MassIVE; O14787; -.
DR MaxQB; O14787; -.
DR PaxDb; O14787; -.
DR PeptideAtlas; O14787; -.
DR PRIDE; O14787; -.
DR ProteomicsDB; 48235; -. [O14787-1]
DR ProteomicsDB; 48236; -. [O14787-2]
DR Antibodypedia; 26113; 95 antibodies from 20 providers.
DR DNASU; 30000; -.
DR Ensembl; ENST00000356861.9; ENSP00000349321.4; ENSG00000105576.16. [O14787-2]
DR Ensembl; ENST00000425528.6; ENSP00000407182.1; ENSG00000105576.16. [O14787-1]
DR Ensembl; ENST00000450764.6; ENSP00000397379.2; ENSG00000105576.16. [O14787-2]
DR Ensembl; ENST00000588216.5; ENSP00000465625.1; ENSG00000105576.16. [O14787-2]
DR Ensembl; ENST00000592287.5; ENSP00000468434.1; ENSG00000105576.16. [O14787-1]
DR GeneID; 30000; -.
DR KEGG; hsa:30000; -.
DR MANE-Select; ENST00000425528.6; ENSP00000407182.1; NM_001382241.1; NP_001369170.1.
DR UCSC; uc002muo.4; human. [O14787-1]
DR CTD; 30000; -.
DR DisGeNET; 30000; -.
DR GeneCards; TNPO2; -.
DR HGNC; HGNC:19998; TNPO2.
DR HPA; ENSG00000105576; Low tissue specificity.
DR MIM; 603002; gene.
DR MIM; 619556; phenotype.
DR neXtProt; NX_O14787; -.
DR OpenTargets; ENSG00000105576; -.
DR PharmGKB; PA134921349; -.
DR VEuPathDB; HostDB:ENSG00000105576; -.
DR eggNOG; KOG2023; Eukaryota.
DR GeneTree; ENSGT00940000156708; -.
DR HOGENOM; CLU_008136_1_0_1; -.
DR InParanoid; O14787; -.
DR OMA; AMMYSQH; -.
DR PhylomeDB; O14787; -.
DR TreeFam; TF300825; -.
DR PathwayCommons; O14787; -.
DR SignaLink; O14787; -.
DR BioGRID-ORCS; 30000; 16 hits in 1083 CRISPR screens.
DR ChiTaRS; TNPO2; human.
DR GeneWiki; TNPO2; -.
DR GenomeRNAi; 30000; -.
DR Pharos; O14787; Tbio.
DR PRO; PR:O14787; -.
DR Proteomes; UP000005640; Chromosome 19.
DR RNAct; O14787; protein.
DR Bgee; ENSG00000105576; Expressed in cortical plate and 207 other tissues.
DR ExpressionAtlas; O14787; baseline and differential.
DR Genevisible; O14787; HS.
DR GO; GO:0005737; C:cytoplasm; TAS:ProtInc.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0061608; F:nuclear import signal receptor activity; IBA:GO_Central.
DR GO; GO:0008139; F:nuclear localization sequence binding; IBA:GO_Central.
DR GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR GO; GO:0006606; P:protein import into nucleus; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 2.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR001494; Importin-beta_N.
DR InterPro; IPR040122; Importin_beta.
DR PANTHER; PTHR10527; PTHR10527; 1.
DR Pfam; PF03810; IBN_N; 1.
DR SMART; SM00913; IBN_N; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Disease variant;
KW Intellectual disability; Nucleus; Protein transport; Reference proteome;
KW Repeat; Transport.
FT CHAIN 1..897
FT /note="Transportin-2"
FT /id="PRO_0000120767"
FT REPEAT 9..36
FT /note="HEAT 1"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT DOMAIN 31..99
FT /note="Importin N-terminal"
FT REPEAT 41..79
FT /note="HEAT 2"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 88..121
FT /note="HEAT 3"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 127..164
FT /note="HEAT 4"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 171..201
FT /note="HEAT 5"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 214..241
FT /note="HEAT 6"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 253..280
FT /note="HEAT 7"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 296..386
FT /note="HEAT 8"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 394..422
FT /note="HEAT 9"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 434..461
FT /note="HEAT 10"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 475..508
FT /note="HEAT 11"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 516..549
FT /note="HEAT 12"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 557..595
FT /note="HEAT 13"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 603..654
FT /note="HEAT 14"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 665..696
FT /note="HEAT 15"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 704..737
FT /note="HEAT 16"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 745..790
FT /note="HEAT 17"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 798..831
FT /note="HEAT 18"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 840..871
FT /note="HEAT 19"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REPEAT 874..894
FT /note="HEAT 20"
FT /evidence="ECO:0000250|UniProtKB:Q92973"
FT REGION 325..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 329..353
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 862
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 769..778
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.2"
FT /id="VSP_009657"
FT VARIANT 28
FT /note="Q -> R (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705"
FT /id="VAR_086356"
FT VARIANT 32
FT /note="Q -> R (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705, ECO:0000269|Ref.2"
FT /id="VAR_086357"
FT VARIANT 61
FT /note="P -> R (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705"
FT /id="VAR_086358"
FT VARIANT 118
FT /note="K -> N (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705"
FT /id="VAR_086359"
FT VARIANT 156
FT /note="D -> N (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705"
FT /id="VAR_086360"
FT VARIANT 370
FT /note="W -> C (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:23033978,
FT ECO:0000269|PubMed:34314705"
FT /id="VAR_069373"
FT VARIANT 370
FT /note="W -> R (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705"
FT /id="VAR_086361"
FT VARIANT 491..492
FT /note="KR -> QW (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705"
FT /id="VAR_086362"
FT VARIANT 514
FT /note="P -> L (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705"
FT /id="VAR_086363"
FT VARIANT 546
FT /note="A -> V (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705"
FT /id="VAR_086364"
FT VARIANT 548
FT /note="S -> F (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705"
FT /id="VAR_086365"
FT VARIANT 649..652
FT /note="Missing (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705"
FT /id="VAR_086366"
FT VARIANT 727
FT /note="W -> C (in IDDHISD)"
FT /evidence="ECO:0000269|PubMed:34314705"
FT /id="VAR_086367"
FT CONFLICT 28
FT /note="Q -> H (in Ref. 2; AAB71349)"
FT /evidence="ECO:0000305"
FT CONFLICT 194
FT /note="A -> G (in Ref. 2; AAB71349)"
FT /evidence="ECO:0000305"
FT CONFLICT 398..401
FT /note="LLKG -> YQS (in Ref. 1; AAB83973)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="R -> K (in Ref. 2; AAB71349)"
FT /evidence="ECO:0000305"
FT CONFLICT 499
FT /note="S -> I (in Ref. 2; AAB71349)"
FT /evidence="ECO:0000305"
FT CONFLICT 507
FT /note="E -> K (in Ref. 2; AAB71349)"
FT /evidence="ECO:0000305"
FT CONFLICT 608
FT /note="R -> C (in Ref. 2; AAB71349)"
FT /evidence="ECO:0000305"
FT CONFLICT 645
FT /note="L -> F (in Ref. 2; AAB71349)"
FT /evidence="ECO:0000305"
FT CONFLICT 646
FT /note="S -> T (in Ref. 1; AAB83973)"
FT /evidence="ECO:0000305"
FT CONFLICT 656
FT /note="V -> L (in Ref. 1; AAB83973)"
FT /evidence="ECO:0000305"
FT CONFLICT 687
FT /note="L -> F (in Ref. 2; AAB71349)"
FT /evidence="ECO:0000305"
FT CONFLICT 691
FT /note="L -> F (in Ref. 2; AAB71349)"
FT /evidence="ECO:0000305"
FT CONFLICT 696..697
FT /note="FI -> SS (in Ref. 2; AAB71349)"
FT /evidence="ECO:0000305"
FT CONFLICT 717
FT /note="E -> K (in Ref. 1; AAB83973)"
FT /evidence="ECO:0000305"
FT CONFLICT 812
FT /note="R -> Q (in Ref. 1; AAB83973)"
FT /evidence="ECO:0000305"
FT CONFLICT 841
FT /note="F -> L (in Ref. 2; AAB71349)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 897 AA; 101388 MW; 26FE455583D7D35F CRC64;
MDWQPDEQGL QQVLQLLKDS QSPNTATQRI VQDKLKQLNQ FPDFNNYLIF VLTRLKSEDE
PTRSLSGLIL KNNVKAHYQS FPPPVADFIK QECLNNIGDA SSLIRATIGI LITTIASKGE
LQMWPELLPQ LCNLLNSEDY NTCEGAFGAL QKICEDSSEL LDSDALNRPL NIMIPKFLQF
FKHCSPKIRS HAIACVNQFI MDRAQALMDN IDTFIEHLFA LAVDDDPEVR KNVCRALVML
LEVRIDRLIP HMHSIIQYML QRTQDHDENV ALEACEFWLT LAEQPICKEV LASHLVQLIP
ILVNGMKYSE IDIILLKGDV EEDEAVPDSE QDIKPRFHKS RTVTLPHEAE RPDGSEDAED
DDDDDALSDW NLRKCSAAAL DVLANVFREE LLPHLLPLLK GLLFHPEWVV KESGILVLGA
IAEGCMQGMV PYLPELIPHL IQCLSDKKAL VRSIACWTLS RYAHWVVSQP PDMHLKPLMT
ELLKRILDGN KRVQEAACSA FATLEEEACT ELVPYLSYIL DTLVFAFGKY QHKNLLILYD
AIGTLADSVG HHLNQPEYIQ KLMPPLIQKW NELKDEDKDL FPLLECLSSV ATALQSGFLP
YCEPVYQRCV TLVQKTLAQA MMYTQHPEQY EAPDKDFMIV ALDLLSGLAE GLGGHVEQLV
ARSNIMTLLF QCMQDSMPEV RQSSFALLGD LTKACFIHVK PCIAEFMPIL GTNLNPEFIS
VCNNATWAIG EICMQMGAEM QPYVQMVLNN LVEIINRPNT PKTLLENTGR LTSPSAIPAI
TIGRLGYVCP QEVAPMLQQF IRPWCTSLRN IRDNEEKDSA FRGICMMIGV NPGGVVQDFI
FFCDAVASWV SPKDDLRDMF YKILHGFKDQ VGEDNWQQFS EQFPPLLKER LAAFYGV
