FNBP1_MOUSE
ID FNBP1_MOUSE Reviewed; 616 AA.
AC Q80TY0; A2AQ40; A2AQ46; Q3TA45; Q3TCW9; Q3U081; Q3UPI7; Q8C727; Q99L37;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Formin-binding protein 1;
DE AltName: Full=Formin-binding protein 17;
GN Name=Fnbp1; Synonyms=Fbp17, Kiaa0554;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4), AND
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 169-616 (ISOFORM 5).
RC STRAIN=C57BL/6J, and NOD;
RC TISSUE=Dendritic cell, Embryo, Kidney, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
RC STRAIN=FVB/N; TISSUE=Mammary gland;
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 [5]
RP TISSUE SPECIFICITY.
RX PubMed=15252009; DOI=10.1074/jbc.m404899200;
RA Kamioka Y., Fukuhara S., Sawa H., Nagashima K., Masuda M., Matsuda M.,
RA Mochizuki N.;
RT "A novel dynamin-associating molecule, formin-binding protein 17, induces
RT tubular membrane invaginations and participates in endocytosis.";
RL J. Biol. Chem. 279:40091-40099(2004).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496 AND TYR-499, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Mast cell;
RX PubMed=17947660; DOI=10.4049/jimmunol.179.9.5864;
RA Cao L., Yu K., Banh C., Nguyen V., Ritz A., Raphael B.J., Kawakami Y.,
RA Kawakami T., Salomon A.R.;
RT "Quantitative time-resolved phosphoproteomic analysis of mast cell
RT signaling.";
RL J. Immunol. 179:5864-5876(2007).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-296, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-496, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Required to coordinate membrane tubulation with
CC reorganization of the actin cytoskeleton during the late stage of
CC clathrin-mediated endocytosis. Binds to lipids such as
CC phosphatidylinositol 4,5-bisphosphate and phosphatidylserine and
CC promotes membrane invagination and the formation of tubules. Also
CC enhances actin polymerization via the recruitment of WASL/N-WASP, which
CC in turn activates the Arp2/3 complex. Actin polymerization may promote
CC the fission of membrane tubules to form endocytic vesicles. May act as
CC a link between RND2 signaling and regulation of the actin cytoskeleton.
CC May be required for the lysosomal retention of FASLG/FASL (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Homodimerizes, the dimers can polymerize end-to-end to form
CC filamentous structures. Interacts specifically with GTP-bound RND2 and
CC CDC42. Interacts with AKAP9, ARHGAP17, DAAM1, DIAPH1, DIAPH2, DNM1,
CC DNM2, DNM3, FASLG/FASL, microtubules, PDE6G, SNX2 and WASL/N-WASP. May
CC interact with TNKS (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Cytoplasm, cytoskeleton
CC {ECO:0000250}. Cytoplasm, cell cortex {ECO:0000250}. Lysosome
CC {ECO:0000250}. Cytoplasmic vesicle {ECO:0000250}. Cell membrane
CC {ECO:0000250}; Peripheral membrane protein {ECO:0000250}; Cytoplasmic
CC side {ECO:0000250}. Membrane, clathrin-coated pit {ECO:0000250}.
CC Note=Enriched in cortical regions coincident with F-actin. Also
CC localizes to endocytic vesicles and lysosomes. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q80TY0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TY0-2; Sequence=VSP_021698;
CC Name=3;
CC IsoId=Q80TY0-3; Sequence=VSP_021698, VSP_021703;
CC Name=4;
CC IsoId=Q80TY0-4; Sequence=VSP_021697, VSP_021699, VSP_021702;
CC Name=5;
CC IsoId=Q80TY0-5; Sequence=VSP_021700, VSP_021701;
CC -!- TISSUE SPECIFICITY: Expressed in brain and testis.
CC {ECO:0000269|PubMed:15252009}.
CC -!- DOMAIN: The F-BAR domain binds the phospholipid membrane with its
CC concave surface. The end-to-end polymerization of dimers of these
CC domains provides a curved surface that fits best membranes with around
CC 600 A diameter, and may drive tubulation (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FNBP1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65590.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAE33974.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK122308; BAC65590.1; ALT_INIT; mRNA.
DR EMBL; AK052652; BAC35082.1; -; mRNA.
DR EMBL; AK143512; BAE25408.1; -; mRNA.
DR EMBL; AK157135; BAE33974.1; ALT_INIT; mRNA.
DR EMBL; AK170497; BAE41836.1; -; mRNA.
DR EMBL; AK172100; BAE42825.1; -; mRNA.
DR EMBL; AL844546; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC003867; AAH03867.1; -; mRNA.
DR CCDS; CCDS15894.1; -. [Q80TY0-5]
DR CCDS; CCDS38097.1; -. [Q80TY0-2]
DR CCDS; CCDS50560.1; -. [Q80TY0-4]
DR CCDS; CCDS50561.1; -. [Q80TY0-1]
DR CCDS; CCDS57165.1; -. [Q80TY0-3]
DR RefSeq; NP_001033789.1; NM_001038700.2. [Q80TY0-2]
DR RefSeq; NP_001171119.1; NM_001177648.1. [Q80TY0-1]
DR RefSeq; NP_001171120.1; NM_001177649.1. [Q80TY0-3]
DR RefSeq; NP_001171121.1; NM_001177650.1. [Q80TY0-4]
DR RefSeq; NP_062279.1; NM_019406.3. [Q80TY0-5]
DR AlphaFoldDB; Q80TY0; -.
DR SMR; Q80TY0; -.
DR BioGRID; 199720; 16.
DR IntAct; Q80TY0; 2.
DR MINT; Q80TY0; -.
DR STRING; 10090.ENSMUSP00000109190; -.
DR iPTMnet; Q80TY0; -.
DR PhosphoSitePlus; Q80TY0; -.
DR EPD; Q80TY0; -.
DR jPOST; Q80TY0; -.
DR MaxQB; Q80TY0; -.
DR PaxDb; Q80TY0; -.
DR PeptideAtlas; Q80TY0; -.
DR PRIDE; Q80TY0; -.
DR ProteomicsDB; 267489; -. [Q80TY0-1]
DR ProteomicsDB; 267490; -. [Q80TY0-2]
DR ProteomicsDB; 267491; -. [Q80TY0-3]
DR ProteomicsDB; 267492; -. [Q80TY0-4]
DR ProteomicsDB; 267493; -. [Q80TY0-5]
DR Antibodypedia; 31452; 197 antibodies from 31 providers.
DR DNASU; 14269; -.
DR Ensembl; ENSMUST00000113552; ENSMUSP00000109181; ENSMUSG00000075415. [Q80TY0-5]
DR Ensembl; ENSMUST00000113559; ENSMUSP00000109189; ENSMUSG00000075415. [Q80TY0-4]
DR Ensembl; ENSMUST00000113560; ENSMUSP00000109190; ENSMUSG00000075415. [Q80TY0-1]
DR Ensembl; ENSMUST00000113562; ENSMUSP00000109192; ENSMUSG00000075415. [Q80TY0-2]
DR Ensembl; ENSMUST00000113564; ENSMUSP00000109194; ENSMUSG00000075415. [Q80TY0-3]
DR GeneID; 14269; -.
DR KEGG; mmu:14269; -.
DR UCSC; uc008jdh.1; mouse. [Q80TY0-4]
DR UCSC; uc008jdi.2; mouse. [Q80TY0-2]
DR UCSC; uc008jdj.2; mouse. [Q80TY0-1]
DR UCSC; uc008jdk.2; mouse. [Q80TY0-3]
DR UCSC; uc008jdm.2; mouse. [Q80TY0-5]
DR CTD; 23048; -.
DR MGI; MGI:109606; Fnbp1.
DR VEuPathDB; HostDB:ENSMUSG00000075415; -.
DR eggNOG; KOG3565; Eukaryota.
DR GeneTree; ENSGT00950000183047; -.
DR HOGENOM; CLU_870262_0_0_1; -.
DR InParanoid; Q80TY0; -.
DR OMA; EFMISKP; -.
DR OrthoDB; 348563at2759; -.
DR PhylomeDB; Q80TY0; -.
DR TreeFam; TF351162; -.
DR Reactome; R-MMU-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR BioGRID-ORCS; 14269; 0 hits in 75 CRISPR screens.
DR ChiTaRS; Fnbp1; mouse.
DR PRO; PR:Q80TY0; -.
DR Proteomes; UP000000589; Chromosome 2.
DR RNAct; Q80TY0; protein.
DR Bgee; ENSMUSG00000075415; Expressed in cerebellar cortex and 239 other tissues.
DR ExpressionAtlas; Q80TY0; baseline and differential.
DR Genevisible; Q80TY0; MM.
DR GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005764; C:lysosome; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0042802; F:identical protein binding; ISO:MGI.
DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
DR GO; GO:0006897; P:endocytosis; IEA:UniProtKB-KW.
DR GO; GO:0007399; P:nervous system development; ISO:MGI.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd07676; F-BAR_FBP17; 1.
DR CDD; cd12071; SH3_FBP17; 1.
DR Gene3D; 1.20.1270.60; -; 1.
DR InterPro; IPR027267; AH/BAR_dom_sf.
DR InterPro; IPR031160; F_BAR.
DR InterPro; IPR001060; FCH_dom.
DR InterPro; IPR028532; FNBP1/FBP17.
DR InterPro; IPR037449; FNBP1_F-BAR.
DR InterPro; IPR035492; FNBP1_SH3.
DR InterPro; IPR011072; HR1_rho-bd.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15735:SF13; PTHR15735:SF13; 1.
DR Pfam; PF00611; FCH; 1.
DR Pfam; PF00018; SH3_1; 1.
DR SMART; SM00055; FCH; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF103657; SSF103657; 1.
DR SUPFAM; SSF50044; SSF50044; 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 Acetylation; Alternative splicing; Cell membrane; Coated pit; Coiled coil;
KW Cytoplasm; Cytoplasmic vesicle; Cytoskeleton; Endocytosis; Lipid-binding;
KW Lysosome; Membrane; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..616
FT /note="Formin-binding protein 1"
FT /id="PRO_0000261431"
FT DOMAIN 1..264
FT /note="F-BAR"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01077"
FT DOMAIN 403..480
FT /note="REM-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01207"
FT DOMAIN 549..610
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..334
FT /note="Interaction with microtubules"
FT /evidence="ECO:0000250"
FT REGION 1..79
FT /note="Required for self-association and induction of
FT membrane tubulation"
FT /evidence="ECO:0000250"
FT REGION 251..616
FT /note="Required for self-association and induction of
FT membrane tubulation"
FT /evidence="ECO:0000250"
FT REGION 280..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 332..366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..551
FT /note="Interaction with RND2"
FT /evidence="ECO:0000250"
FT REGION 487..531
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 494..616
FT /note="Interaction with PDE6G"
FT /evidence="ECO:0000250"
FT REGION 513..616
FT /note="Required for interaction with TNKS"
FT /evidence="ECO:0000250"
FT REGION 534..616
FT /note="Interaction with DNM1 and DNM3"
FT /evidence="ECO:0000250"
FT REGION 549..616
FT /note="Interaction with ARHGAP17, DAAM1, DIAPH1 and DIAPH2"
FT /evidence="ECO:0000250"
FT REGION 552..609
FT /note="Interaction with FASLG"
FT /evidence="ECO:0000250"
FT REGION 552..608
FT /note="Interaction with DNM2 and WASL"
FT /evidence="ECO:0000250"
FT COILED 67..259
FT /evidence="ECO:0000250"
FT COILED 398..490
FT /evidence="ECO:0000250"
FT COMPBIAS 291..305
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 335..360
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 495..516
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 517..531
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 166
FT /note="Mediates end-to-end attachment of dimers"
FT /evidence="ECO:0000250"
FT MOD_RES 66
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96RU3"
FT MOD_RES 110
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q96RU3"
FT MOD_RES 296
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19144319"
FT MOD_RES 299
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RU3"
FT MOD_RES 348
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RU3"
FT MOD_RES 358
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q96RU3"
FT MOD_RES 496
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17947660,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 499
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:17947660"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8R511"
FT VAR_SEQ 1..79
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021697"
FT VAR_SEQ 329..394
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021698"
FT VAR_SEQ 329..338
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021699"
FT VAR_SEQ 329..338
FT /note="LMSLLTSPHQ -> VLAIWTLRGL (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021700"
FT VAR_SEQ 339..616
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_021701"
FT VAR_SEQ 390..394
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021702"
FT VAR_SEQ 515
FT /note="E -> ES (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_021703"
SQ SEQUENCE 616 AA; 71344 MW; 947BFCFCCA4BD1E2 CRC64;
MSWGTELWDQ FDNLEKHTQW GIDILEKYIK FVKERTEIEL SYAKQLRNLS KKYQPKKNSK
EEEEYKYTAC KAFLSTLNEM NDYAGQHEVI SENMTSQITV DLMRYVQELK QERKSNFHDG
RKAQQHIETC WKQLESSKRR FERDCKEADR AQQYFEKMDA DINVTKADVE KARQQAQIRQ
QMAEDSKADY SLILQRFNQE QWEYYHTHIP NIFQKIQEME ERRIVRIGES MKTYAEVDRQ
VIPIIGKCLD GIVKAAESID QKNDSQLVVE AYKSGFEPPG DIEFEDYTQP MKRTVSDNSL
SSSKEGKPEL RFGGKSRGKL WPFIKKNKLM SLLTSPHQPP PPPPASASPS AVPNGPQSPK
QPKEPLSHRF NEFMTSKPKI HCFRSLKRGL SLKLGVTPED FSNFPPEQRR KKLQQKVDDL
NREIQKETDQ RDAITKMKDV YLKNPQMGDP ASLDQKLTEV TQNIEKLRLE AQKFEAWLAE
VEGRLPARSE QARRQSGLYD GQTHQTVTNC AQDRESPDGS YTEEQSQESE HKVLAPDFDD
EFDDEEPLPA IGTCKALYTF EGQNEGTISV VEGETLSVIE EDKGDGWTRI RRNEDEEGYV
PTSYVEVYLD KNAKGS
