ID HAX1_HUMAN Reviewed; 279 AA. AC O00165; A8W4W9; A8W4X0; B4DUJ7; Q5VYD5; Q5VYD7; Q96AU4; Q9BS80; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 25-JAN-2012, entry version 109. DE RecName: Full=HCLS1-associated protein X-1; DE AltName: Full=HS1-associating protein X-1; DE Short=HAX-1; DE AltName: Full=HS1-binding protein 1; DE Short=HSP1BP-1; GN Name=HAX1; Synonyms=HS1BP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, SUBCELLULAR RP LOCATION, INTERACTION WITH HCLS1, AND TISSUE SPECIFICITY. RC TISSUE=Cervix adenocarcinoma; RX MEDLINE=97211841; PubMed=9058808; RA Suzuki Y., Demoliere C., Kitamura D., Takeshita H., Deuschle U., RA Watanabe T.; RT "HAX-1, a novel intracellular protein, localized on mitochondria, RT directly associates with HS1, a substrate of Src family tyrosine RT kinases."; RL J. Immunol. 158:2736-2744(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3; 4; 5 AND 6). RX PubMed=18472110; DOI=10.1016/j.jmb.2008.04.020; RA Lees D.M., Hart I.R., Marshall J.F.; RT "Existence of multiple isoforms of HS1-associated protein X-1 in RT murine and human tissues."; RL J. Mol. Biol. 379:645-655(2008). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4). RC TISSUE=Lung; RA Trebinska A., Grzybowska E.A.; RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2 AND 4). RC TISSUE=Amygdala, Heart, and Skeletal muscle; 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., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA 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., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., RA Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT RP GLY-151. RC TISSUE=Brain, Lung, and Skin; 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 RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [8] RP PROTEIN SEQUENCE OF 2-17 AND 140-150, CLEAVAGE OF INITIATOR RP METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY. RC TISSUE=Hepatoma; RA Bienvenut W.V., Boldt K., von Kriegsheim A.F., Kolch W.; RL Submitted (JUL-2007) to UniProtKB. RN [9] RP INTERACTION WITH PKD2. RX PubMed=10760273; DOI=10.1073/pnas.97.8.4017; RA Gallagher A.R., Cedzich A., Gretz N., Somlo S., Witzgall R.; RT "The polycystic kidney disease protein PKD2 interacts with Hax-1, a RT protein associated with the actin cytoskeleton."; RL Proc. Natl. Acad. Sci. U.S.A. 97:4017-4022(2000). RN [10] RP INTERACTION WITH GNA13, AND FUNCTION. RX PubMed=15339924; DOI=10.1074/jbc.M408836200; RA Radhika V., Onesime D., Ha J.H., Dhanasekaran N.; RT "Galpha13 stimulates cell migration through cortactin-interacting RT protein Hax-1."; RL J. Biol. Chem. 279:49406-49413(2004). RN [11] RP INTERACTION WITH CASP9, AND FUNCTION. RX PubMed=16857965; DOI=10.1161/01.RES.0000237387.05259.a5; RA Han Y., Chen Y.S., Liu Z., Bodyak N., Rigor D., Bisping E., Pu W.T., RA Kang P.M.; RT "Overexpression of HAX-1 protects cardiac myocytes from apoptosis RT through caspase-9 inhibition."; RL Circ. Res. 99:415-423(2006). RN [12] RP INTERACTION WITH ITGB6, FUNCTION, AND TISSUE SPECIFICITY. RX PubMed=17545607; DOI=10.1158/0008-5472.CAN-07-0318; RA Ramsay A.G., Keppler M.D., Jazayeri M., Thomas G.J., Parsons M., RA Violette S., Weinreb P., Hart I.R., Marshall J.F.; RT "HS1-associated protein X-1 regulates carcinoma cell migration and RT invasion via clathrin-mediated endocytosis of integrin alphavbeta6."; RL Cancer Res. 67:5275-5284(2007). RN [13] RP INTERACTION WITH PLN. RX PubMed=17241641; DOI=10.1016/j.jmb.2006.10.057; RA Vafiadaki E., Sanoudou D., Arvanitis D.A., Catino D.H., Kranias E.G., RA Kontrogianni-Konstantopoulos A.; RT "Phospholamban interacts with HAX-1, a mitochondrial protein with RT anti-apoptotic function."; RL J. Mol. Biol. 367:65-79(2007). RN [14] RP INVOLVEMENT IN SCN3. RX PubMed=17187068; DOI=10.1038/ng1940; RA Klein C., Grudzien M., Appaswamy G., Germeshausen M., Sandrock I., RA Schaeffer A.A., Rathinam C., Boztug K., Schwinzer B., Rezaei N., RA Bohn G., Melin M., Carlsson G., Fadeel B., Dahl N., Palmblad J., RA Henter J.-I., Zeidler C., Grimbacher B., Welte K.; RT "HAX1 deficiency causes autosomal recessive severe congenital RT neutropenia (Kostmann disease)."; RL Nat. Genet. 39:86-92(2007). RN [15] RP INVOLVEMENT IN SCN3, AND ISOFORM DEPENDENT GENOTYPE-PHENOTYPE RP ASSOCIATIONS. RX PubMed=18337561; DOI=10.1182/blood-2007-11-120667; RA Germeshausen M., Grudzien M., Zeidler C., Abdollahpour H., Yetgin S., RA Rezaei N., Ballmaier M., Grimbacher B., Welte K., Klein C.; RT "Novel HAX1 mutations in patients with severe congenital neutropenia RT reveal isoform-dependent genotype-phenotype associations."; RL Blood 111:4954-4957(2008). RN [16] RP CLEAVAGE SITE, AND FUNCTION. RX PubMed=18319618; RA Lee A.Y., Lee Y., Park Y.K., Bae K.-H., Cho S., Lee do H., Park B.C., RA Kang S., Park S.G.; RT "HS 1-associated protein X-1 is cleaved by caspase-3 during RT apoptosis."; RL Mol. Cells 25:86-90(2008). RN [17] RP INTERACTION WITH ATP2A2 AND PLN, FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=18971376; DOI=10.1091/mbc.E08-06-0587; RA Vafiadaki E., Arvanitis D.A., Pagakis S.N., Papalouka V., Sanoudou D., RA Kontrogianni-Konstantopoulos A., Kranias E.G.; RT "The anti-apoptotic protein HAX-1 interacts with SERCA2 and regulates RT its protein levels to promote cell survival."; RL Mol. Biol. Cell 20:306-318(2009). RN [18] 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., RA Buerckstuemmer T., 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 [19] RP INTERACTION WITH GRB7. RX PubMed=20665473; DOI=10.1002/jmr.1062; RA Siamakpour-Reihani S., Peterson T.A., Bradford A.M., Argiros H.J., RA Haas L.L., Lor S.N., Haulsee Z.M., Spuches A.M., Johnson D.L., RA Rohrschneider L.R., Shuster C.B., Lyons B.A.; RT "Grb7 binds to Hax-1 and undergoes an intramolecular domain RT association that offers a model for Grb7 regulation."; RL J. Mol. Recognit. 24:314-321(2011). RN [20] RP VARIANT SCN3 LEU-141. RX PubMed=19796188; DOI=10.1111/j.1399-0004.2009.01244.x; RA Faiyaz-Ul-Haque M., Al-Jefri A., Abalkhail H.A., Toulimat M., RA Al-Muallimi M.A., Pulicat M.S., Gaafar A., Alaiya A.A., Al-Dayel F., RA Peltekova I., Zaidi S.H.; RT "A novel missense mutation in the HAX1 gene in severe congenital RT neutropenia patients (Kostmann disease)."; RL Clin. Genet. 76:569-572(2009). RN [21] RP VARIANTS SCN3 ARG-130 AND ILE-172. RX PubMed=20220065; DOI=10.3324/haematol.2009.017665; RA Germeshausen M., Zeidler C., Stuhrmann M., Lanciotti M., Ballmaier M., RA Welte K.; RT "Digenic mutations in severe congenital neutropenia."; RL Haematologica 95:1207-1210(2010). CC -!- FUNCTION: Promotes cell survival. Potentiates GNA13-mediated cell CC migration. Involved in the clathrin-mediated endocytosis pathway. CC May be involved in internalization of ABC transporters such as CC ABCB11. May inhibit CASP9 and CASP3. May regulate intracellular CC calcium pools. CC -!- SUBUNIT: Interacts with ABCB1, ABCB4 and ABCB11 (By similarity). CC Directly associates with HCLS1/HS1, through binding to its N- CC terminal region. Interacts with CTTN. Interacts with PKD2. CC Interacts with GNA13. Interacts with CASP9. Interacts with ITGB6. CC Interacts with PLN and ATP2A2; these interactions are inhibited by CC calcium. Interacts with GRB7. CC -!- INTERACTION: CC P03372:ESR1; NbExp=2; IntAct=EBI-357001, EBI-78473; CC Q14451:GRB7; NbExp=2; IntAct=EBI-357001, EBI-970191; CC -!- SUBCELLULAR LOCATION: Mitochondrion. Endoplasmic reticulum. CC Nucleus membrane. Cytoplasmic vesicle (By similarity). CC Sarcoplasmic reticulum (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Comment=Additional isoforms seem to exist; CC Name=1; CC IsoId=O00165-1; Sequence=Displayed; CC Name=2; CC IsoId=O00165-2; Sequence=VSP_038537; CC Name=3; CC IsoId=O00165-3; Sequence=VSP_038536; CC Name=4; CC IsoId=O00165-4; Sequence=VSP_038538, VSP_038539; CC Name=5; CC IsoId=O00165-5; Sequence=VSP_038543; CC Name=6; CC IsoId=O00165-6; Sequence=VSP_038544, VSP_038545; CC -!- TISSUE SPECIFICITY: Ubiquitous. Up-regulated in oral cancers. CC -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis. CC -!- DISEASE: Defects in HAX1 are the cause of neutropenia severe CC congenital autosomal recessive type 3 (SCN3) [MIM:610738]; also CC known as Kostmann disease. A disorder of hematopoiesis CC characterized by maturation arrest of granulopoiesis at the level CC of promyelocytes with peripheral blood absolute neutrophil counts CC below 0.5 x 10(9)/l and early onset of severe bacterial CC infections. Some patients affected by severe congenital CC neutropenia type 3 have neurological manifestations such as CC psychomotor retardation and seizures. Note=The clinical phenotype CC due to HAX1 deficiency appears to depend on the localization of CC the mutations and their influence on the transcript variants. CC Mutations affecting exclusively isoform 1 are associated with CC isolated congenital neutropenia, whereas mutations affecting both CC isoform 1 and isoform 5 are associated with additional neurologic CC symptoms. CC -!- SIMILARITY: Belongs to the HAX1 family. CC -!- WEB RESOURCE: Name=HAX1base; Note=HAX1 mutation db; CC URL="http://bioinf.uta.fi/HAX1base/"; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U68566; AAB51196.1; -; mRNA. DR EMBL; EU190982; ABW73998.1; -; mRNA. DR EMBL; EU190983; ABW73999.1; -; mRNA. DR EMBL; AK290626; BAF83315.1; -; mRNA. DR EMBL; AK294298; BAG57580.1; -; mRNA. DR EMBL; AK300676; BAG62359.1; -; mRNA. DR EMBL; AL354980; CAH70479.1; -; Genomic_DNA. DR EMBL; AL354980; CAH70481.1; -; Genomic_DNA. DR EMBL; CH471121; EAW53212.1; -; Genomic_DNA. DR EMBL; BC005240; AAH05240.1; -; mRNA. DR EMBL; BC014314; AAH14314.1; -; mRNA. DR EMBL; BC015209; AAH15209.1; -; mRNA. DR EMBL; BC016730; AAH16730.1; -; mRNA. DR IPI; IPI00010440; -. DR IPI; IPI00604587; -. DR IPI; IPI00641973; -. DR IPI; IPI00878396; -. DR IPI; IPI00954512; -. DR IPI; IPI00954523; -. DR RefSeq; NP_001018238.1; NM_001018837.1. DR RefSeq; NP_006109.2; NM_006118.3. DR UniGene; Hs.199625; -. DR ProteinModelPortal; O00165; -. DR IntAct; O00165; 55. DR MINT; MINT-1137395; -. DR STRING; O00165; -. DR PRIDE; O00165; -. DR Ensembl; ENST00000328703; ENSP00000329002; ENSG00000143575. DR Ensembl; ENST00000447768; ENSP00000403848; ENSG00000143575. DR GeneID; 10456; -. DR KEGG; hsa:10456; -. DR UCSC; uc001fes.1; human. DR CTD; 10456; -. DR GeneCards; GC01P154244; -. DR H-InvDB; HIX0199953; -. DR HGNC; HGNC:16915; HAX1. DR MIM; 605998; gene. DR MIM; 610738; phenotype. DR neXtProt; NX_O00165; -. DR Orphanet; 99749; Kostmann syndrome. DR PharmGKB; PA142671700; -. DR eggNOG; prNOG12670; -. DR GeneTree; ENSGT00390000018324; -. DR HOVERGEN; HBG002991; -. DR InParanoid; O00165; -. DR OrthoDB; EOG49S678; -. DR PhylomeDB; O00165; -. DR NextBio; 39639; -. DR PMAP-CutDB; O00165; -. DR ArrayExpress; O00165; -. DR Bgee; O00165; -. DR CleanEx; HS_HAX1; -. DR Genevestigator; O00165; -. DR GermOnline; ENSG00000143575; Homo sapiens. DR GO; GO:0015629; C:actin cytoskeleton; ISS:BHF-UCL. DR GO; GO:0016023; C:cytoplasmic membrane-bounded vesicle; IEA:UniProtKB-SubCell. DR GO; GO:0030027; C:lamellipodium; ISS:BHF-UCL. DR GO; GO:0005739; C:mitochondrion; IDA:UniProtKB. DR GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016529; C:sarcoplasmic reticulum; IEA:UniProtKB-SubCell. DR GO; GO:0005625; C:soluble fraction; TAS:ProtInc. DR GO; GO:0019966; F:interleukin-1 binding; IDA:UniProtKB. DR GO; GO:0047485; F:protein N-terminus binding; IDA:UniProtKB. DR InterPro; IPR017248; HS1--assoc_X-1. DR PIRSF; PIRSF037634; HS1-associating_X-1; 1. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Complete proteome; KW Cytoplasmic vesicle; Direct protein sequencing; Disease mutation; KW Endoplasmic reticulum; Membrane; Mitochondrion; Nucleus; Polymorphism; KW Reference proteome; Sarcoplasmic reticulum. FT INIT_MET 1 1 Removed. FT CHAIN 2 279 HCLS1-associated protein X-1. FT /FTId=PRO_0000083906. FT REGION 2 41 Required for localization in mitochondria FT (By similarity). FT REGION 114 279 Involved in HCLS1 binding. FT REGION 175 206 Involved in CASP9 binding. FT REGION 176 247 Involved in GNA13 binding. FT REGION 183 279 Required for localization in sarcoplasmic FT reticulum (By similarity). FT REGION 184 279 Involved in PKD2 binding. FT REGION 203 245 Involved in ATP2A2 binding. FT REGION 203 225 Involved in PLN binding. FT REGION 270 279 Required for ITGB6 binding. FT COMPBIAS 30 40 Asp/Glu-rich (highly acidic). FT SITE 127 128 Cleavage; by caspase-3. FT MOD_RES 2 2 N-acetylserine. FT VAR_SEQ 1 26 Missing (in isoform 3). FT /FTId=VSP_038536. FT VAR_SEQ 18 65 Missing (in isoform 5). FT /FTId=VSP_038543. FT VAR_SEQ 85 264 VRDFNSIFSDMGAWTLPSHPPELPGPESETPGERLREGQTL FT RDSMLKYPDSHQPRIFGGVLESDARSESPQPAPDWGSQRPF FT HRFDDVWPMDPHPRTREDNDLDSQVSQEGLGPVLQPQPKSY FT FKSISVTKITKPDGIVEERRTVVDSEGRTETTVTRHEADSS FT PRGDPESPRPPALDDA -> NFQVLSQRHLVRDYGRDRHFG FT TQCLSIQIVTSPGSLGGSWRVMQEVNPPNQHQTGAPRGHFI FT GLMMYGLWTPILEPERTMILIPRFPRRVLARFYSPSPNPIS FT RASL (in isoform 6). FT /FTId=VSP_038544. FT VAR_SEQ 105 105 P -> PANTCHLSA (in isoform 2). FT /FTId=VSP_038537. FT VAR_SEQ 106 124 ELPGPESETPGERLREGQT -> GVWLSLRGNLWFLVGWWV FT K (in isoform 4). FT /FTId=VSP_038538. FT VAR_SEQ 125 279 Missing (in isoform 4). FT /FTId=VSP_038539. FT VAR_SEQ 265 279 Missing (in isoform 6). FT /FTId=VSP_038545. FT VARIANT 49 49 P -> S (in dbSNP:rs11556344). FT /FTId=VAR_062258. FT VARIANT 130 130 L -> R (in SCN3; dbSNP:rs179363871). FT /FTId=VAR_064514. FT VARIANT 141 141 F -> L (in SCN3; mild form; FT dbSNP:rs179363870). FT /FTId=VAR_062259. FT VARIANT 151 151 S -> G (in dbSNP:rs17851425). FT /FTId=VAR_062260. FT VARIANT 172 172 V -> I (in SCN3; dbSNP:rs141970914). FT /FTId=VAR_064515. FT VARIANT 278 278 S -> P (in dbSNP:rs1804715). FT /FTId=VAR_062261. FT CONFLICT 25 25 G -> V (in Ref. 3; BAG62359). FT CONFLICT 45 45 G -> R (in Ref. 1; AAB51196). FT CONFLICT 201 201 Q -> T (in Ref. 1; AAB51196). SQ SEQUENCE 279 AA; 31621 MW; 87EEF0C46857704B CRC64; MSLFDLFRGF FGFPGPRSHR DPFFGGMTRD EDDDEEEEEE GGSWGRGNPR FHSPQHPPEE FGFGFSFSPG GGIRFHDNFG FDDLVRDFNS IFSDMGAWTL PSHPPELPGP ESETPGERLR EGQTLRDSML KYPDSHQPRI FGGVLESDAR SESPQPAPDW GSQRPFHRFD DVWPMDPHPR TREDNDLDSQ VSQEGLGPVL QPQPKSYFKS ISVTKITKPD GIVEERRTVV DSEGRTETTV TRHEADSSPR GDPESPRPPA LDDAFSILDL FLGRWFRSR //