ID AP4B1_HUMAN Reviewed; 739 AA. AC Q9Y6B7; B7Z4X3; Q59EJ4; Q96CL6; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 20-FEB-2007, sequence version 2. DT 10-FEB-2021, entry version 173. DE RecName: Full=AP-4 complex subunit beta-1 {ECO:0000305}; DE AltName: Full=AP-4 adaptor complex subunit beta; DE AltName: Full=Adaptor-related protein complex 4 subunit beta-1; DE AltName: Full=Beta subunit of AP-4; DE AltName: Full=Beta4-adaptin; GN Name=AP4B1 {ECO:0000312|HGNC:HGNC:572}; 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), FUNCTION, SUBUNIT, SUBCELLULAR RP LOCATION, TOPOLOGY, AND VARIANT SER-480. RC TISSUE=Skeletal muscle; RX PubMed=10066790; DOI=10.1074/jbc.274.11.7278; RA Dell'Angelica E.C., Mullins C., Bonifacino J.S.; RT "AP-4, a novel protein complex related to clathrin adaptors."; RL J. Biol. Chem. 274:7278-7285(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Lung; 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 [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT SER-480. RC TISSUE=Brain; RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., RA Ohara O., Nagase T., Kikuno R.F.; RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases. RN [4] 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., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., 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., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., 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., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=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 project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [6] RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY. RX PubMed=10436028; DOI=10.1091/mbc.10.8.2787; RA Hirst J., Bright N.A., Rous B., Robinson M.S.; RT "Characterization of a fourth adaptor-related protein complex."; RL Mol. Biol. Cell 10:2787-2802(1999). RN [7] RP INVOLVEMENT IN SPG47. RX PubMed=21620353; DOI=10.1016/j.ajhg.2011.04.019; RA Abou Jamra R., Philippe O., Raas-Rothschild A., Eck S.H., Graf E., RA Buchert R., Borck G., Ekici A., Brockschmidt F.F., Nothen M.M., Munnich A., RA Strom T.M., Reis A., Colleaux L.; RT "Adaptor protein complex 4 deficiency causes severe autosomal-recessive RT intellectual disability, progressive spastic paraplegia, shy character, and RT short stature."; RL Am. J. Hum. Genet. 88:788-795(2011). RN [8] RP INTERACTION WITH TEPSIN, AND SUBCELLULAR LOCATION. RX PubMed=22472443; DOI=10.1083/jcb.201111049; RA Borner G.H., Antrobus R., Hirst J., Bhumbra G.S., Kozik P., Jackson L.P., RA Sahlender D.A., Robinson M.S.; RT "Multivariate proteomic profiling identifies novel accessory proteins of RT coated vesicles."; RL J. Cell Biol. 197:141-160(2012). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [10] RP INTERACTION WITH TEPSIN, REGION, AND MUTAGENESIS OF TRP-635 AND TYR-682. RX PubMed=26542808; DOI=10.1074/jbc.m115.683409; RA Mattera R., Guardia C.M., Sidhu S.S., Bonifacino J.S.; RT "Bivalent motif-ear interactions mediate the association of the accessory RT protein tepsin with the AP-4 adaptor complex."; RL J. Biol. Chem. 290:30736-30749(2015). RN [11] RP INTERACTION WITH TEPSIN, AND MUTAGENESIS OF ILE-669; ALA-670 AND TYR-682. RX PubMed=26756312; DOI=10.1111/tra.12375; RA Frazier M.N., Davies A.K., Voehler M., Kendall A.K., Borner G.H., RA Chazin W.J., Robinson M.S., Jackson L.P.; RT "Molecular basis for the interaction between AP4 beta4 and its accessory RT protein, tepsin."; RL Traffic 17:400-415(2016). RN [12] RP STRUCTURE BY NMR OF 610-739. RG Northeast structural genomics consortium (NESG); RT "Solution NMR structure of beta-adaptin appendage domain of human adapter RT protein complex 4 subunit beta, Northeast structural genomics consortium RT (NESG) target HR8998C."; RL Submitted (JAN-2014) to the PDB data bank. CC -!- FUNCTION: Component of the adaptor protein complex 4 (AP-4). Adaptor CC protein complexes are vesicle coat components involved both in vesicle CC formation and cargo selection. They control the vesicular transport of CC proteins in different trafficking pathways (PubMed:10066790, CC PubMed:10436028). AP-4 forms a non clathrin-associated coat on vesicles CC departing the trans-Golgi network (TGN) and may be involved in the CC targeting of proteins from the trans-Golgi network (TGN) to the CC endosomal-lysosomal system. It is also involved in protein sorting to CC the basolateral membrane in epithelial cells and the proper asymmetric CC localization of somatodendritic proteins in neurons. AP-4 is involved CC in the recognition and binding of tyrosine-based sorting signals found CC in the cytoplasmic part of cargos, but may also recognize other types CC of sorting signal (Probable). {ECO:0000269|PubMed:10066790, CC ECO:0000269|PubMed:10436028, ECO:0000305|PubMed:10066790, CC ECO:0000305|PubMed:10436028}. CC -!- SUBUNIT: Adaptor protein complex 4 (AP-4) is a heterotetramer composed CC of two large adaptins (epsilon-type subunit AP4E1 and beta-type subunit CC AP4B1), a medium adaptin (mu-type subunit AP4M1) and a small adaptin CC (sigma-type AP4S1) (PubMed:10066790, PubMed:10436028). Interacts with CC TEPSIN; this interaction requires the presence of a functional AP-4 CC complex (PubMed:22472443, PubMed:26542808, PubMed:26756312). Interacts CC with GRIA2; probably indirect it mediates the somatodendritic CC localization of GRIA2 in neurons (By similarity). CC {ECO:0000250|UniProtKB:Q9WV76, ECO:0000269|PubMed:10066790, CC ECO:0000269|PubMed:10436028, ECO:0000269|PubMed:22472443, CC ECO:0000269|PubMed:26542808, ECO:0000269|PubMed:26756312}. CC -!- INTERACTION: CC Q9Y6B7; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-1047606, EBI-11139477; CC Q9Y6B7; Q9H609: ZNF576; NbExp=7; IntAct=EBI-1047606, EBI-3921014; CC -!- SUBCELLULAR LOCATION: Golgi apparatus, trans-Golgi network membrane CC {ECO:0000269|PubMed:10066790, ECO:0000269|PubMed:10436028, CC ECO:0000269|PubMed:22472443}; Peripheral membrane protein CC {ECO:0000269|PubMed:10066790}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y6B7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y6B7-2; Sequence=VSP_055787, VSP_055788, VSP_055789; CC -!- TISSUE SPECIFICITY: Widely expressed. {ECO:0000269|PubMed:10436028}. CC -!- DISEASE: Spastic paraplegia 47, autosomal recessive (SPG47) CC [MIM:614066]: A form of spastic paraplegia, a neurodegenerative CC disorder characterized by a slow, gradual, progressive weakness and CC spasticity of the lower limbs. SPG47 is characterized by neonatal CC hypotonia that progresses to hypertonia and spasticity, and severe CC mental retardation with poor or absent speech development. CC {ECO:0000269|PubMed:21620353}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=BAD93054.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF092094; AAD20448.1; -; mRNA. DR EMBL; AK298037; BAH12709.1; -; mRNA. DR EMBL; AB209817; BAD93054.1; ALT_INIT; mRNA. DR EMBL; AL137856; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC014146; AAH14146.1; -; mRNA. DR CCDS; CCDS865.1; -. [Q9Y6B7-1] DR RefSeq; NP_001240781.1; NM_001253852.2. [Q9Y6B7-1] DR RefSeq; NP_001240782.1; NM_001253853.2. DR RefSeq; NP_001295241.1; NM_001308312.1. DR RefSeq; NP_006585.2; NM_006594.4. [Q9Y6B7-1] DR PDB; 2MJ7; NMR; -; A=610-739. DR PDBsum; 2MJ7; -. DR SMR; Q9Y6B7; -. DR BioGRID; 115943; 13. DR ComplexPortal; CPX-5151; AP-4 Adaptor complex. DR CORUM; Q9Y6B7; -. DR DIP; DIP-24209N; -. DR IntAct; Q9Y6B7; 8. DR STRING; 9606.ENSP00000358582; -. DR TCDB; 9.B.278.1.5; the organellar-targeting adaptor protein complex (o-apc) family. DR iPTMnet; Q9Y6B7; -. DR PhosphoSitePlus; Q9Y6B7; -. DR BioMuta; AP4B1; -. DR DMDM; 126302520; -. DR EPD; Q9Y6B7; -. DR jPOST; Q9Y6B7; -. DR MassIVE; Q9Y6B7; -. DR PaxDb; Q9Y6B7; -. DR PeptideAtlas; Q9Y6B7; -. DR PRIDE; Q9Y6B7; -. DR ProteomicsDB; 6643; -. DR ProteomicsDB; 86647; -. [Q9Y6B7-1] DR Antibodypedia; 33851; 147 antibodies. DR DNASU; 10717; -. DR Ensembl; ENST00000256658; ENSP00000256658; ENSG00000134262. [Q9Y6B7-1] DR Ensembl; ENST00000369569; ENSP00000358582; ENSG00000134262. [Q9Y6B7-1] DR GeneID; 10717; -. DR KEGG; hsa:10717; -. DR UCSC; uc001eeb.4; human. [Q9Y6B7-1] DR CTD; 10717; -. DR DisGeNET; 10717; -. DR GeneCards; AP4B1; -. DR HGNC; HGNC:572; AP4B1. DR HPA; ENSG00000134262; Low tissue specificity. DR MalaCards; AP4B1; -. DR MIM; 607245; gene. DR MIM; 614066; phenotype. DR neXtProt; NX_Q9Y6B7; -. DR OpenTargets; ENSG00000134262; -. DR Orphanet; 280763; Severe intellectual disability and progressive spastic paraplegia. DR PharmGKB; PA24864; -. DR VEuPathDB; HostDB:ENSG00000134262.12; -. DR eggNOG; KOG1061; Eukaryota. DR GeneTree; ENSGT00940000157025; -. DR HOGENOM; CLU_006320_4_2_1; -. DR InParanoid; Q9Y6B7; -. DR OMA; KMCFLYL; -. DR PhylomeDB; Q9Y6B7; -. DR TreeFam; TF354235; -. DR PathwayCommons; Q9Y6B7; -. DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis. DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis. DR BioGRID-ORCS; 10717; 5 hits in 882 CRISPR screens. DR GeneWiki; AP4B1; -. DR GenomeRNAi; 10717; -. DR Pharos; Q9Y6B7; Tbio. DR PRO; PR:Q9Y6B7; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q9Y6B7; protein. DR Bgee; ENSG00000134262; Expressed in right hemisphere of cerebellum and 213 other tissues. DR ExpressionAtlas; Q9Y6B7; baseline and differential. DR Genevisible; Q9Y6B7; HS. DR GO; GO:0030124; C:AP-4 adaptor complex; IDA:UniProtKB. DR GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro. DR GO; GO:0005829; C:cytosol; IDA:UniProtKB. DR GO; GO:0031904; C:endosome lumen; TAS:Reactome. DR GO; GO:0019898; C:extrinsic component of membrane; IDA:UniProtKB. DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB. DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome. DR GO; GO:0030276; F:clathrin binding; IEA:InterPro. DR GO; GO:0008104; P:protein localization; IC:UniProtKB. DR GO; GO:0006605; P:protein targeting; IC:UniProtKB. DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central. DR Gene3D; 1.25.10.10; -; 1. DR Gene3D; 3.30.310.10; -; 1. DR InterPro; IPR026739; AP_beta. DR InterPro; IPR016342; AP_complex_bsu_1_2_4. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR015151; B-adaptin_app_sub_C. DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N. DR InterPro; IPR012295; TBP_dom_sf. DR PANTHER; PTHR11134; PTHR11134; 1. DR Pfam; PF01602; Adaptin_N; 1. DR Pfam; PF09066; B2-adapt-app_C; 1. DR PIRSF; PIRSF002291; AP_complex_beta; 1. DR SMART; SM01020; B2-adapt-app_C; 1. DR SUPFAM; SSF48371; SSF48371; 1. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Golgi apparatus; KW Hereditary spastic paraplegia; Membrane; Neurodegeneration; KW Protein transport; Reference proteome; Transport. FT CHAIN 1..739 FT /note="AP-4 complex subunit beta-1" FT /id="PRO_0000193750" FT REGION 534..600 FT /note="Hinge" FT /evidence="ECO:0000305|PubMed:26542808" FT REGION 601..739 FT /note="Ear; mediates interaction with TEPSIN" FT /evidence="ECO:0000269|PubMed:26542808" FT VAR_SEQ 113..205 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055787" FT VAR_SEQ 373..395 FT /note="GIARTYTDQCVQILTELLGLRQE -> RCLLLFLLENLDQPARKLWLEEP FT (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055788" FT VAR_SEQ 396..739 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055789" FT VARIANT 480 FT /note="L -> S (in dbSNP:rs1217401)" FT /evidence="ECO:0000269|PubMed:10066790, ECO:0000269|Ref.3" FT /id="VAR_030804" FT MUTAGEN 635 FT /note="W->A: Decreased interaction with TEPSIN." FT /evidence="ECO:0000269|PubMed:26542808" FT MUTAGEN 669 FT /note="I->A: Decreased interaction with TEPSIN; when FT associated with S-670." FT /evidence="ECO:0000269|PubMed:26756312" FT MUTAGEN 670 FT /note="A->S: Decreased interaction with TEPSIN; when FT associated with A-669." FT /evidence="ECO:0000269|PubMed:26756312" FT MUTAGEN 682 FT /note="Y->A,V: Decreased interaction with TEPSIN." FT /evidence="ECO:0000269|PubMed:26542808, FT ECO:0000269|PubMed:26756312" FT CONFLICT 140 FT /note="A -> V (in Ref. 1; AAD20448)" FT /evidence="ECO:0000305" FT HELIX 628..637 FT /evidence="ECO:0000244|PDB:2MJ7" FT STRAND 641..647 FT /evidence="ECO:0000244|PDB:2MJ7" FT HELIX 654..663 FT /evidence="ECO:0000244|PDB:2MJ7" FT STRAND 667..671 FT /evidence="ECO:0000244|PDB:2MJ7" FT STRAND 677..687 FT /evidence="ECO:0000244|PDB:2MJ7" FT STRAND 692..699 FT /evidence="ECO:0000244|PDB:2MJ7" FT STRAND 701..703 FT /evidence="ECO:0000244|PDB:2MJ7" FT STRAND 705..714 FT /evidence="ECO:0000244|PDB:2MJ7" FT HELIX 717..735 FT /evidence="ECO:0000244|PDB:2MJ7" SQ SEQUENCE 739 AA; 83260 MW; B6FC92215BDA5EDC CRC64; MPYLGSEDVV KELKKALCNP HIQADRLRYR NVIQRVIRYM TQGLDMSGVF MEMVKASATV DIVQKKLVYL YMCTYAPLKP DLALLAINTL CKDCSDPNPM VRGLALRSMC SLRMPGVQEY IQQPILNGLR DKASYVRRVA VLGCAKMHNL HGDSEVDGAL VNELYSLLRD QDPIVVVNCL RSLEEILKQE GGVVINKPIA HHLLNRMSKL DQWGQAEVLN FLLRYQPRSE EELFDILNLL DSFLKSSSPG VVMGATKLFL ILAKMFPHVQ TDVLVRVKGP LLAACSSESR ELCFVALCHV RQILHSLPGH FSSHYKKFFC SYSEPHYIKL QKVEVLCELV NDENVQQVLE ELRGYCTDVS ADFAQAAIFA IGGIARTYTD QCVQILTELL GLRQEHITTV VVQTFRDLVW LCPQCTEAVC QALPGCEENI QDSEGKQALI WLLGVHGERI PNAPYVLEDF VENVKSETFP AVKMELLTAL LRLFLSRPAE CQDMLGRLLY YCIEEEKDMA VRDRGLFYYR LLLVGIDEVK RILCSPKSDP TLGLLEDPAE RPVNSWASDF NTLVPVYGKA HWATISKCQG AERCDPELPK TSSFAASGPL IPEENKERVQ ELPDSGALML VPNRQLTADY FEKTWLSLKV AHQQVLPWRG EFHPDTLQMA LQVVNIQTIA MSRAGSRPWK AYLSAQDDTG CLFLTELLLE PGNSEMQISV KQNEARTETL NSFISVLETV IGTIEEIKS //