AP4B1_HUMAN
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 03-AUG-2022, entry version 179.
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 intellectual disability 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};
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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 AlphaFoldDB; Q9Y6B7; -.
DR SMR; Q9Y6B7; -.
DR BioGRID; 115943; 20.
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 MaxQB; Q9Y6B7; -.
DR PaxDb; Q9Y6B7; -.
DR PeptideAtlas; Q9Y6B7; -.
DR PRIDE; Q9Y6B7; -.
DR ProteomicsDB; 6643; -.
DR ProteomicsDB; 86647; -. [Q9Y6B7-1]
DR Antibodypedia; 33851; 155 antibodies from 23 providers.
DR DNASU; 10717; -.
DR Ensembl; ENST00000256658.8; ENSP00000256658.4; ENSG00000134262.13. [Q9Y6B7-1]
DR Ensembl; ENST00000369569.6; ENSP00000358582.1; ENSG00000134262.13. [Q9Y6B7-1]
DR GeneID; 10717; -.
DR KEGG; hsa:10717; -.
DR MANE-Select; ENST00000369569.6; ENSP00000358582.1; NM_001253852.3; NP_001240781.1.
DR UCSC; uc001eeb.4; human. [Q9Y6B7-1]
DR CTD; 10717; -.
DR DisGeNET; 10717; -.
DR GeneCards; AP4B1; -.
DR GeneReviews; 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; -.
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 SignaLink; Q9Y6B7; -.
DR BioGRID-ORCS; 10717; 18 hits in 1085 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 granulocyte and 186 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:0061938; P:protein localization to somatodendritic compartment; IEA:Ensembl.
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:0007829|PDB:2MJ7"
FT STRAND 641..647
FT /evidence="ECO:0007829|PDB:2MJ7"
FT HELIX 654..663
FT /evidence="ECO:0007829|PDB:2MJ7"
FT STRAND 667..671
FT /evidence="ECO:0007829|PDB:2MJ7"
FT STRAND 677..687
FT /evidence="ECO:0007829|PDB:2MJ7"
FT STRAND 692..699
FT /evidence="ECO:0007829|PDB:2MJ7"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:2MJ7"
FT STRAND 705..714
FT /evidence="ECO:0007829|PDB:2MJ7"
FT HELIX 717..735
FT /evidence="ECO:0007829|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
