ID NOSTN_HUMAN Reviewed; 506 AA.
AC Q8IVI9; A8K2I9; B3KSF5; E7EPT9; Q27HG3; Q53S62; Q96CJ9;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 2.
DT 27-MAR-2024, entry version 178.
DE RecName: Full=Nostrin {ECO:0000305};
DE AltName: Full=BM247 homolog;
DE AltName: Full=Nitric oxide synthase traffic inducer;
DE AltName: Full=Nitric oxide synthase trafficker;
DE AltName: Full=eNOS-trafficking inducer;
GN Name=NOSTRIN {ECO:0000312|HGNC:HGNC:20203};
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), TISSUE SPECIFICITY, INTERACTION
RP WITH NOS3, SUBCELLULAR LOCATION, FUNCTION, AND VARIANT GLU-473.
RC TISSUE=Placenta;
RX PubMed=12446846; DOI=10.1073/pnas.252345399;
RA Zimmermann K., Opitz N., Dedio J., Renne C., Mueller-Esterl W., Oess S.;
RT "NOSTRIN: a protein modulating nitric oxide release and subcellular
RT distribution of endothelial nitric oxide synthase.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17167-17172(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT GLU-473.
RA Beese M., Kirsch T.;
RT "Molecular characterization of an alternatively spliced variant of human
RT NOSTRIN.";
RL Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4), AND VARIANT
RP GLU-473.
RC TISSUE=Colon, Placenta, and Testis;
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=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., 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., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., 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., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND VARIANT
RP GLU-473.
RC TISSUE=Placenta, and Thyroid;
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 1-304.
RC TISSUE=Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (APR-2003) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP IDENTIFICATION.
RX PubMed=11489260; DOI=10.1016/s0006-8993(01)02670-1;
RA Kirsch T., Wellner M., Luft F.C., Haller H., Lippoldt A.;
RT "Altered gene expression in cerebral capillaries of stroke-prone
RT spontaneously hypertensive rats.";
RL Brain Res. 910:106-115(2001).
RN [8]
RP TISSUE SPECIFICITY.
RX PubMed=15847871; DOI=10.1016/j.ijgo.2004.12.041;
RA Xiang W., Chen H., Xu X., Zhang M., Jiang R.;
RT "Expression of endothelial nitric oxide synthase traffic inducer in the
RT placentas of women with pre-eclampsia.";
RL Int. J. Gynecol. Obstet. 89:103-107(2005).
RN [9]
RP SUBUNIT, INTERACTION WITH DNM2 AND WASL, SUBCELLULAR LOCATION, AND
RP FUNCTION.
RX PubMed=16234328; DOI=10.1242/jcs.02620;
RA Icking A., Matt S., Opitz N., Wiesenthal A., Mueller-Esterl W.,
RA Schilling K.;
RT "NOSTRIN functions as a homotrimeric adaptor protein facilitating
RT internalization of eNOS.";
RL J. Cell Sci. 118:5059-5069(2005).
RN [10]
RP SUBCELLULAR LOCATION.
RX PubMed=16376344; DOI=10.1016/j.febslet.2005.11.078;
RA Icking A., Schilling K., Wiesenthal A., Opitz N., Mueller-Esterl W.;
RT "FCH/Cdc15 domain determines distinct subcellular localization of
RT NOSTRIN.";
RL FEBS Lett. 580:223-228(2006).
RN [11]
RP INTERACTION WITH CAV1, AND FUNCTION.
RX PubMed=16807357; DOI=10.1091/mbc.e05-08-0709;
RA Schilling K., Opitz N., Wiesenthal A., Oess S., Tikkanen R.,
RA Mueller-Esterl W., Icking A.;
RT "Translocation of endothelial nitric-oxide synthase involves a ternary
RT complex with caveolin-1 and NOSTRIN.";
RL Mol. Biol. Cell 17:3870-3880(2006).
RN [12]
RP SUBCELLULAR LOCATION (ISOFORM 3).
RX PubMed=18980613; DOI=10.1111/j.1600-0854.2008.00850.x;
RA Wiesenthal A., Hoffmeister M., Siddique M., Kovacevic I., Oess S.,
RA Muller-Esterl W., Siehoff-Icking A.;
RT "NOSTRINbeta--a shortened NOSTRIN variant with a role in transcriptional
RT regulation.";
RL Traffic 10:26-34(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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).
RN [14]
RP STRUCTURE BY NMR OF 439-506.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the SH3 domain of human nostrin.";
RL Submitted (OCT-2007) to the PDB data bank.
CC -!- FUNCTION: Multivalent adapter protein which may decrease NOS3 activity
CC by inducing its translocation away from the plasma membrane.
CC {ECO:0000269|PubMed:12446846, ECO:0000269|PubMed:16234328,
CC ECO:0000269|PubMed:16807357}.
CC -!- SUBUNIT: Homotrimer. Interacts with DAB2 (By similarity). Interacts
CC with NOS3, DNM2, WASL and CAV1. Interacts (via SH3 domain) with DNM2;
CC this interaction allows the recruitment of NOS3 to dynamin-positive
CC structures (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q5I0D6,
CC ECO:0000269|PubMed:12446846, ECO:0000269|PubMed:16234328,
CC ECO:0000269|PubMed:16807357}.
CC -!- INTERACTION:
CC Q8IVI9; Q05193: DNM1; NbExp=3; IntAct=EBI-1391643, EBI-713135;
CC Q8IVI9; P11362: FGFR1; NbExp=5; IntAct=EBI-1391643, EBI-1028277;
CC Q8IVI9; P29474: NOS3; NbExp=9; IntAct=EBI-1391643, EBI-1391623;
CC Q8IVI9; O08816: Wasl; Xeno; NbExp=3; IntAct=EBI-1391643, EBI-6142604;
CC Q8IVI9-3; P43360: MAGEA6; NbExp=3; IntAct=EBI-12280006, EBI-1045155;
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Cell membrane
CC {ECO:0000269|PubMed:12446846, ECO:0000269|PubMed:16376344}; Peripheral
CC membrane protein {ECO:0000269|PubMed:12446846,
CC ECO:0000269|PubMed:16376344}; Cytoplasmic side
CC {ECO:0000269|PubMed:12446846, ECO:0000269|PubMed:16376344}. Cytoplasmic
CC vesicle {ECO:0000269|PubMed:12446846}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:16234328, ECO:0000269|PubMed:16376344}.
CC Note=Enriched in selected actin structures (PubMed:16234328,
CC PubMed:16376344).
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus
CC {ECO:0000269|PubMed:18980613}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1; Synonyms=NOSTRINalpha;
CC IsoId=Q8IVI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IVI9-2; Sequence=VSP_025885;
CC Name=3; Synonyms=NOSTRINbeta;
CC IsoId=Q8IVI9-3; Sequence=VSP_025884;
CC Name=4;
CC IsoId=Q8IVI9-4; Sequence=VSP_044995;
CC -!- TISSUE SPECIFICITY: Expressed at highest levels in heart, kidney,
CC placenta and lung, and at lowest levels in brain, thymus and spleen.
CC Present in vascular endothelial cells and placenta. Over-expressed in
CC placenta from women with pre-eclampsia (at protein level).
CC {ECO:0000269|PubMed:12446846, ECO:0000269|PubMed:15847871}.
CC -!- DOMAIN: The SH3 domain mediates interaction with NOS3, DNM2 and WASL.
CC -!- DOMAIN: The F-BAR domain is necessary for membrane targeting.
CC -!- MISCELLANEOUS: [Isoform 3]: May negatively regulate transcription of
CC the NOSTRIN gene. {ECO:0000269|PubMed:18980613}.
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DR EMBL; AJ532842; CAD58724.1; -; mRNA.
DR EMBL; DQ402497; ABD62889.1; -; mRNA.
DR EMBL; AK002203; BAE46614.1; -; mRNA.
DR EMBL; AK093444; BAG52717.1; -; mRNA.
DR EMBL; AK290254; BAF82943.1; -; mRNA.
DR EMBL; AC069137; AAY24097.1; -; Genomic_DNA.
DR EMBL; AC009475; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014189; AAH14189.1; -; mRNA.
DR EMBL; BC093072; AAH93072.1; -; mRNA.
DR EMBL; AL550371; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS42771.1; -. [Q8IVI9-1]
DR CCDS; CCDS42772.1; -. [Q8IVI9-3]
DR CCDS; CCDS54415.1; -. [Q8IVI9-4]
DR CCDS; CCDS54416.1; -. [Q8IVI9-2]
DR RefSeq; NP_001034813.2; NM_001039724.3. [Q8IVI9-1]
DR RefSeq; NP_001165102.1; NM_001171631.1. [Q8IVI9-4]
DR RefSeq; NP_001165103.1; NM_001171632.1. [Q8IVI9-2]
DR RefSeq; NP_443178.2; NM_052946.3. [Q8IVI9-3]
DR PDB; 2YUN; NMR; -; A=441-506.
DR PDBsum; 2YUN; -.
DR AlphaFoldDB; Q8IVI9; -.
DR SMR; Q8IVI9; -.
DR BioGRID; 125446; 11.
DR CORUM; Q8IVI9; -.
DR IntAct; Q8IVI9; 15.
DR MINT; Q8IVI9; -.
DR STRING; 9606.ENSP00000394051; -.
DR iPTMnet; Q8IVI9; -.
DR PhosphoSitePlus; Q8IVI9; -.
DR BioMuta; NOSTRIN; -.
DR DMDM; 317373401; -.
DR EPD; Q8IVI9; -.
DR jPOST; Q8IVI9; -.
DR MassIVE; Q8IVI9; -.
DR MaxQB; Q8IVI9; -.
DR PeptideAtlas; Q8IVI9; -.
DR ProteomicsDB; 17440; -.
DR ProteomicsDB; 70712; -. [Q8IVI9-1]
DR ProteomicsDB; 70713; -. [Q8IVI9-2]
DR ProteomicsDB; 70714; -. [Q8IVI9-3]
DR Pumba; Q8IVI9; -.
DR ABCD; Q8IVI9; 6 sequenced antibodies.
DR Antibodypedia; 47609; 224 antibodies from 27 providers.
DR DNASU; 115677; -.
DR Ensembl; ENST00000317647.12; ENSP00000318921.7; ENSG00000163072.16. [Q8IVI9-1]
DR Ensembl; ENST00000397206.6; ENSP00000380390.2; ENSG00000163072.16. [Q8IVI9-3]
DR Ensembl; ENST00000397209.6; ENSP00000380392.2; ENSG00000163072.16. [Q8IVI9-2]
DR Ensembl; ENST00000444448.6; ENSP00000394051.2; ENSG00000163072.16. [Q8IVI9-4]
DR Ensembl; ENST00000445023.6; ENSP00000404413.2; ENSG00000163072.16. [Q8IVI9-3]
DR Ensembl; ENST00000458381.6; ENSP00000402140.2; ENSG00000163072.16. [Q8IVI9-4]
DR GeneID; 115677; -.
DR KEGG; hsa:115677; -.
DR MANE-Select; ENST00000317647.12; ENSP00000318921.7; NM_001039724.4; NP_001034813.2.
DR UCSC; uc002uef.4; human. [Q8IVI9-1]
DR AGR; HGNC:20203; -.
DR CTD; 115677; -.
DR DisGeNET; 115677; -.
DR GeneCards; NOSTRIN; -.
DR HGNC; HGNC:20203; NOSTRIN.
DR HPA; ENSG00000163072; Low tissue specificity.
DR MIM; 607496; gene.
DR neXtProt; NX_Q8IVI9; -.
DR OpenTargets; ENSG00000163072; -.
DR PharmGKB; PA134992787; -.
DR VEuPathDB; HostDB:ENSG00000163072; -.
DR GeneTree; ENSGT00510000048120; -.
DR HOGENOM; CLU_027170_1_0_1; -.
DR InParanoid; Q8IVI9; -.
DR OMA; YSAWCHV; -.
DR OrthoDB; 5400939at2759; -.
DR PhylomeDB; Q8IVI9; -.
DR PathwayCommons; Q8IVI9; -.
DR Reactome; R-HSA-203641; NOSTRIN mediated eNOS trafficking.
DR SignaLink; Q8IVI9; -.
DR BioGRID-ORCS; 115677; 10 hits in 1157 CRISPR screens.
DR ChiTaRS; NOSTRIN; human.
DR EvolutionaryTrace; Q8IVI9; -.
DR GenomeRNAi; 115677; -.
DR Pharos; Q8IVI9; Tbio.
DR PRO; PR:Q8IVI9; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8IVI9; Protein.
DR Bgee; ENSG00000163072; Expressed in right lung and 97 other cell types or tissues.
DR ExpressionAtlas; Q8IVI9; baseline and differential.
DR Genevisible; Q8IVI9; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0003677; F:DNA binding; IEA:Ensembl.
DR GO; GO:0007015; P:actin filament organization; IBA:GO_Central.
DR GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd11823; SH3_Nostrin; 1.
DR Gene3D; 6.10.140.470; -; 1.
DR Gene3D; 1.20.1270.60; Arfaptin homology (AH) domain/BAR domain; 1.
DR Gene3D; 2.30.30.40; SH3 Domains; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036274; HR1_rpt_sf.
DR InterPro; IPR035656; Nostrin_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR23065:SF62; NOSTRIN, ISOFORM H; 1.
DR PANTHER; PTHR23065; PROLINE-SERINE-THREONINE PHOSPHATASE INTERACTING PROTEIN 1; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF14604; SH3_9; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; BAR/IMD domain-like; 1.
DR SUPFAM; SSF46585; HR1 repeat; 1.
DR SUPFAM; SSF50044; SH3-domain; 1.
DR PROSITE; PS51741; F_BAR; 1.
DR PROSITE; PS51860; REM_1; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Coiled coil; Cytoplasm;
KW Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Membrane; Nucleus;
KW Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..506
FT /note="Nostrin"
FT /id="PRO_0000289089"
FT DOMAIN 1..260
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 292..372
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 438..497
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT COILED 160..222
FT /evidence="ECO:0000255"
FT MOD_RES 114
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5I0D6"
FT MOD_RES 479
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6WKZ7"
FT VAR_SEQ 1..78
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025884"
FT VAR_SEQ 38..65
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.2"
FT /id="VSP_025885"
FT VAR_SEQ 209
FT /note="Y -> YQVTHSICLYAFWVKRAWGKCVSDLRYQDTFLPGNLPPLWFGYDIVK
FT RLIMRLCSVCL (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044995"
FT VARIANT 473
FT /note="G -> E (in dbSNP:rs479661)"
FT /evidence="ECO:0000269|PubMed:12446846,
FT ECO:0000269|PubMed:14702039, ECO:0000269|PubMed:15489334,
FT ECO:0000269|Ref.2"
FT /id="VAR_032569"
FT CONFLICT 225
FT /note="N -> D (in Ref. 3; BAG52717)"
FT /evidence="ECO:0000305"
FT STRAND 441..447
FT /evidence="ECO:0007829|PDB:2YUN"
FT STRAND 464..469
FT /evidence="ECO:0007829|PDB:2YUN"
FT STRAND 472..474
FT /evidence="ECO:0007829|PDB:2YUN"
FT STRAND 476..482
FT /evidence="ECO:0007829|PDB:2YUN"
FT STRAND 484..487
FT /evidence="ECO:0007829|PDB:2YUN"
FT STRAND 492..497
FT /evidence="ECO:0007829|PDB:2YUN"
FT CONFLICT Q8IVI9-4:238
FT /note="T -> I (in Ref. 3; BAG52717)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 506 AA; 57660 MW; DC9A6DF5B9C2AED0 CRC64;
MRDPLTDCPY NKVYKNLKEF SQNGENFCKQ VTSVLQQRAN LEISYAKGLQ KLASKLSKAL
QNTRKSCVSS AWAWASEGMK STADLHQKLG KAIELEAIKP TYQVLNVQEK KRKSLDNEVE
KTANLVISNW NQQIKAKKKL MVSTKKHEAL FQLVESSKQS MTEKEKRKLL NKLTKSTEKL
EKEDENYYQK NMAGYSTRLK WENTLENCYQ SILELEKERI QLLCNNLNQY SQHISLFGQT
LTTCHTQIHC AISKIDIEKD IQAVMEETAI LSTENKSEFL LTDYFEEDPN SAMDKERRKS
LLKPKLLRLQ RDIEKASKDK EGLERMLKTY SSTSSFSDAK SQKDTAALMD ENNLKLDLLE
ANSYKLSSML AELEQRPQPS HPCSNSIFRW REKEHTHSYV KISRPFLMKR LENIVSKASS
GGQSNPGSST PAPGAAQLSS RLCKALYSFQ ARQDDELNLE KGDIVIIHEK KEGGWWFGSL
NGKKGHFPAA YVEELPSNAG NTATKA
//
