AP2A2_RAT
ID AP2A2_RAT Reviewed; 938 AA.
AC P18484;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=AP-2 complex subunit alpha-2;
DE AltName: Full=100 kDa coated vesicle protein C;
DE AltName: Full=Adaptor protein complex AP-2 subunit alpha-2;
DE AltName: Full=Adaptor-related protein complex 2 subunit alpha-2;
DE AltName: Full=Alpha-adaptin C;
DE AltName: Full=Alpha2-adaptin;
DE AltName: Full=Clathrin assembly protein complex 2 alpha-C large chain;
DE AltName: Full=Plasma membrane adaptor HA2/AP2 adaptin alpha C subunit;
GN Name=Ap2a2; Synonyms=Adtab;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RX PubMed=2402467; DOI=10.1093/nar/18.17.5306;
RA Tucker K.L., Nathanson K., Kirchhausen T.;
RT "Sequence of the rat alpha c large chain of the clathrin associated protein
RT complex AP-2.";
RL Nucleic Acids Res. 18:5306-5306(1990).
RN [2]
RP PROTEIN SEQUENCE OF 2-18.
RC TISSUE=Brain;
RX PubMed=2495531; DOI=10.1073/pnas.86.8.2612;
RA Kirchhausen T., Nathanson K.L., Matsui W., Vaisberg A., Chow E.P.,
RA Burne C., Keen J.H., Davis A.E.;
RT "Structural and functional division into two domains of the large (100- to
RT 115-kDa) chains of the clathrin-associated protein complex AP-2.";
RL Proc. Natl. Acad. Sci. U.S.A. 86:2612-2616(1989).
RN [3]
RP PROTEIN SEQUENCE OF 2-18.
RX PubMed=1325787; DOI=10.1016/s0006-291x(05)81473-1;
RA Voglmaier S.M., Keen J.H., Murphy J.E., Ferris C.D., Prestwich G.D.,
RA Snyder S.H., Theibert A.B.;
RT "Inositol hexakisphosphate receptor identified as the clathrin assembly
RT protein AP-2.";
RL Biochem. Biophys. Res. Commun. 187:158-163(1992).
RN [4]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=14745134; DOI=10.1247/csf.28.419;
RA Nakatsu F., Ohno H.;
RT "Adaptor protein complexes as the key regulators of protein sorting in the
RT post-Golgi network.";
RL Cell Struct. Funct. 28:419-429(2003).
RN [5]
RP FUNCTION OF THE AP-2 COMPLEX IN CLATHRIN-MEDIATED ENDOCYTOSIS.
RX PubMed=15473838; DOI=10.1146/annurev.cellbio.20.010403.104543;
RA Owen D.J., Collins B.M., Evans P.R.;
RT "Adaptors for clathrin coats: structure and function.";
RL Annu. Rev. Cell Dev. Biol. 20:153-191(2004).
RN [6]
RP INTERACTION WITH ABCB11.
RX PubMed=22262466; DOI=10.1002/hep.25591;
RA Hayashi H., Inamura K., Aida K., Naoi S., Horikawa R., Nagasaka H.,
RA Takatani T., Fukushima T., Hattori A., Yabuki T., Horii I., Sugiyama Y.;
RT "AP2 adaptor complex mediates bile salt export pump internalization and
RT modulates its hepatocanalicular expression and transport function.";
RL Hepatology 55:1889-1900(2012).
RN [7] {ECO:0007744|PDB:2VGL}
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-620 IN COMPLEX WITH AP2B1;
RP AP2M1; AP2S1 AND INOSITOL HEXAKISPHOSPHATE.
RX PubMed=12086608; DOI=10.1016/s0092-8674(02)00735-3;
RA Collins B.M., McCoy A.J., Kent H.M., Evans P.R., Owen D.J.;
RT "Molecular architecture and functional model of the endocytic AP2
RT complex.";
RL Cell 109:523-535(2002).
RN [8] {ECO:0007744|PDB:4UQI}
RP X-RAY CRYSTALLOGRAPHY (2.79 ANGSTROMS) OF 1-620 IN COMPLEX WITH AP2B1;
RP AP2M1; AP2S1 AND INOSITOL HEXAKISPHOSPHATE.
RX PubMed=25061211; DOI=10.1126/science.1254836;
RA Kelly B.T., Graham S.C., Liska N., Dannhauser P.N., Honing S.,
RA Ungewickell E.J., Owen D.J.;
RT "Clathrin adaptors. AP2 controls clathrin polymerization with a membrane-
RT activated switch.";
RL Science 345:459-463(2014).
CC -!- FUNCTION: Component of the adaptor protein complex 2 (AP-2). Adaptor
CC protein complexes function in protein transport via transport vesicles
CC in different membrane traffic pathways. Adaptor protein complexes are
CC vesicle coat components and appear to be involved in cargo selection
CC and vesicle formation. AP-2 is involved in clathrin-dependent
CC endocytosis in which cargo proteins are incorporated into vesicles
CC surrounded by clathrin (clathrin-coated vesicles, CCVs) which are
CC destined for fusion with the early endosome. The clathrin lattice
CC serves as a mechanical scaffold but is itself unable to bind directly
CC to membrane components. Clathrin-associated adaptor protein (AP)
CC complexes which can bind directly to both the clathrin lattice and to
CC the lipid and protein components of membranes are considered to be the
CC major clathrin adaptors contributing the CCV formation. AP-2 also
CC serves as a cargo receptor to selectively sort the membrane proteins
CC involved in receptor-mediated endocytosis. AP-2 seems to play a role in
CC the recycling of synaptic vesicle membranes from the presynaptic
CC surface. AP-2 recognizes Y-X-X-[FILMV] (Y-X-X-Phi) and [ED]-X-X-X-L-
CC [LI] endocytosis signal motifs within the cytosolic tails of
CC transmembrane cargo molecules. AP-2 may also play a role in maintaining
CC normal post-endocytic trafficking through the ARF6-regulated, non-
CC clathrin pathway. During long-term potentiation in hippocampal neurons,
CC AP-2 is responsible for the endocytosis of ADAM10 (By similarity). The
CC AP-2 alpha subunit binds polyphosphoinositide-containing lipids,
CC positioning AP-2 on the membrane. The AP-2 alpha subunit acts via its
CC C-terminal appendage domain as a scaffolding platform for endocytic
CC accessory proteins. The AP-2 alpha and AP-2 sigma subunits are thought
CC to contribute to the recognition of the [ED]-X-X-X-L-[LI] motif (By
CC similarity). {ECO:0000250, ECO:0000250|UniProtKB:P17427,
CC ECO:0000269|PubMed:14745134, ECO:0000269|PubMed:15473838}.
CC -!- SUBUNIT: Adaptor protein complex 2 (AP-2) is a heterotetramer composed
CC of two large adaptins (alpha-type subunit AP2A1 or AP2A2 and beta-type
CC subunit AP2B1), a medium adaptin (mu-type subunit AP2M1) and a small
CC adaptin (sigma-type subunit AP2S1). Interacts with clathrin (By
CC similarity). Binds EPN1, EPS15, AMPH, SNAP91 and BIN1 (By similarity).
CC Interacts with HIP1 (By similarity). Interacts with DGKD (By
CC similarity). Interacts with DENND1A, DENND1B and DENND1C (By
CC similarity). Interacts with FCHO1 and DAB2 (By similarity). Interacts
CC with ATAT1; this interaction is required for efficient alpha-tubulin
CC acetylation by ATAT1 (By similarity). Interacts with KIAA1107 (By
CC similarity). Together with AP2B1 and AP2M1, it interacts with ADAM10;
CC this interaction facilitates ADAM10 endocytosis from the plasma
CC membrane during long-term potentiation in hippocampal neurons (By
CC similarity). Interacts with CLN3 (via dileucine motif) (By similarity).
CC Interacts with ABCB11; this interaction regulates cell membrane
CC expression of ABCB11 through its internalization in a clathrin-
CC dependent manner and its subsequent degradation (PubMed:22262466).
CC {ECO:0000250|UniProtKB:O94973, ECO:0000250|UniProtKB:P17427,
CC ECO:0000269|PubMed:22262466}.
CC -!- INTERACTION:
CC P18484; P21707: Syt1; NbExp=5; IntAct=EBI-539360, EBI-458098;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P17427};
CC Peripheral membrane protein {ECO:0000250|UniProtKB:P17427}; Cytoplasmic
CC side {ECO:0000250|UniProtKB:P17427}. Membrane, coated pit
CC {ECO:0000250|UniProtKB:P17427}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P17427}; Cytoplasmic side
CC {ECO:0000250|UniProtKB:P17427}. Note=AP-2 appears to be excluded from
CC internalizing CCVs and to disengage from sites of endocytosis seconds
CC before internalization of the nascent CCV.
CC {ECO:0000250|UniProtKB:P17427}.
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC {ECO:0000305}.
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DR EMBL; X53773; CAA37791.1; -; mRNA.
DR PIR; S11276; S11276.
DR PDB; 2VGL; X-ray; 2.59 A; A=1-620.
DR PDB; 2XA7; X-ray; 3.10 A; A=1-621.
DR PDB; 4NEE; X-ray; 2.88 A; A/B/G/J=1-395.
DR PDB; 4UQI; X-ray; 2.79 A; A=1-620.
DR PDB; 6OWT; EM; 3.80 A; A=1-938.
DR PDB; 6QH5; X-ray; 2.56 A; A=1-620.
DR PDB; 6QH6; X-ray; 5.00 A; A=1-620.
DR PDB; 6QH7; X-ray; 3.40 A; A=1-620.
DR PDB; 6URI; X-ray; 3.00 A; A=1-620.
DR PDB; 6YAE; EM; 3.90 A; A=1-620.
DR PDB; 6YAF; EM; 9.10 A; A=1-622.
DR PDB; 6YAH; EM; 10.20 A; A=1-622.
DR PDBsum; 2VGL; -.
DR PDBsum; 2XA7; -.
DR PDBsum; 4NEE; -.
DR PDBsum; 4UQI; -.
DR PDBsum; 6OWT; -.
DR PDBsum; 6QH5; -.
DR PDBsum; 6QH6; -.
DR PDBsum; 6QH7; -.
DR PDBsum; 6URI; -.
DR PDBsum; 6YAE; -.
DR PDBsum; 6YAF; -.
DR PDBsum; 6YAH; -.
DR AlphaFoldDB; P18484; -.
DR BMRB; P18484; -.
DR SMR; P18484; -.
DR CORUM; P18484; -.
DR DIP; DIP-29765N; -.
DR IntAct; P18484; 14.
DR MINT; P18484; -.
DR STRING; 10116.ENSRNOP00000060992; -.
DR CarbonylDB; P18484; -.
DR jPOST; P18484; -.
DR PaxDb; P18484; -.
DR PeptideAtlas; P18484; -.
DR PRIDE; P18484; -.
DR UCSC; RGD:71015; rat.
DR RGD; 71015; Ap2a2.
DR eggNOG; KOG1077; Eukaryota.
DR InParanoid; P18484; -.
DR Reactome; R-RNO-177504; Retrograde neurotrophin signalling.
DR Reactome; R-RNO-2132295; MHC class II antigen presentation.
DR Reactome; R-RNO-416993; Trafficking of GluR2-containing AMPA receptors.
DR Reactome; R-RNO-437239; Recycling pathway of L1.
DR Reactome; R-RNO-5099900; WNT5A-dependent internalization of FZD4.
DR Reactome; R-RNO-5140745; WNT5A-dependent internalization of FZD2, FZD5 and ROR2.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR Reactome; R-RNO-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-RNO-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-RNO-8866427; VLDLR internalisation and degradation.
DR Reactome; R-RNO-8964038; LDL clearance.
DR EvolutionaryTrace; P18484; -.
DR PRO; PR:P18484; -.
DR Proteomes; UP000002494; Unplaced.
DR GO; GO:0030122; C:AP-2 adaptor complex; IMP:CAFA.
DR GO; GO:0031410; C:cytoplasmic vesicle; ISO:RGD.
DR GO; GO:0030117; C:membrane coat; ISO:RGD.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0008021; C:synaptic vesicle; IDA:RGD.
DR GO; GO:0140312; F:cargo adaptor activity; IBA:GO_Central.
DR GO; GO:0035615; F:clathrin adaptor activity; IBA:GO_Central.
DR GO; GO:0097718; F:disordered domain specific binding; ISO:RGD.
DR GO; GO:0019900; F:kinase binding; ISO:RGD.
DR GO; GO:0035091; F:phosphatidylinositol binding; IMP:CAFA.
DR GO; GO:0019904; F:protein domain specific binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0044877; F:protein-containing complex binding; IPI:RGD.
DR GO; GO:0072583; P:clathrin-dependent endocytosis; ISS:UniProtKB.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:0006898; P:receptor-mediated endocytosis; IBA:GO_Central.
DR Gene3D; 1.25.10.10; -; 1.
DR Gene3D; 3.30.310.10; -; 1.
DR IDEAL; IID50129; -.
DR InterPro; IPR017104; AP2_complex_asu.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR InterPro; IPR003164; Clathrin_a-adaptin_app_sub_C.
DR InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR InterPro; IPR012295; TBP_dom_sf.
DR Pfam; PF01602; Adaptin_N; 1.
DR Pfam; PF02296; Alpha_adaptin_C; 1.
DR Pfam; PF02883; Alpha_adaptinC2; 1.
DR PIRSF; PIRSF037091; AP2_complex_alpha; 1.
DR SMART; SM00809; Alpha_adaptinC2; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
DR SUPFAM; SSF49348; SSF49348; 1.
DR SUPFAM; SSF55711; SSF55711; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Coated pit; Direct protein sequencing;
KW Endocytosis; Lipid-binding; Membrane; Protein transport;
KW Reference proteome; Transport.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:1325787,
FT ECO:0000269|PubMed:2495531"
FT CHAIN 2..938
FT /note="AP-2 complex subunit alpha-2"
FT /id="PRO_0000193734"
FT REGION 615..681
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 615..638
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 11..12
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000305|PubMed:12086608,
FT ECO:0000305|PubMed:25061211, ECO:0007744|PDB:2VGL,
FT ECO:0007744|PDB:4UQI"
FT BINDING 43
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000305|PubMed:12086608,
FT ECO:0000305|PubMed:25061211, ECO:0007744|PDB:2VGL,
FT ECO:0007744|PDB:4UQI"
FT BINDING 53
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000305|PubMed:12086608,
FT ECO:0000305|PubMed:25061211, ECO:0007744|PDB:2VGL,
FT ECO:0007744|PDB:4UQI"
FT BINDING 57..61
FT /ligand="a 1,2-diacyl-sn-glycero-3-phospho-(1D-myo-
FT inositol-3,4,5-trisphosphate)"
FT /ligand_id="ChEBI:CHEBI:57836"
FT /evidence="ECO:0000305|PubMed:12086608,
FT ECO:0000305|PubMed:25061211, ECO:0007744|PDB:2VGL,
FT ECO:0007744|PDB:4UQI"
FT HELIX 11..22
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 26..43
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 52..67
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 76..84
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 88..100
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 106..121
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 125..138
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 141..147
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 158..160
FT /evidence="ECO:0007829|PDB:2VGL"
FT HELIX 162..178
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 180..182
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 189..195
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 201..217
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 219..222
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 225..237
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 240..242
FT /evidence="ECO:0007829|PDB:6URI"
FT STRAND 243..245
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 248..251
FT /evidence="ECO:0007829|PDB:6URI"
FT STRAND 252..254
FT /evidence="ECO:0007829|PDB:2VGL"
FT HELIX 255..264
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 265..267
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 268..270
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 273..289
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 299..319
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 323..336
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 342..355
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 356..358
FT /evidence="ECO:0007829|PDB:6QH7"
FT HELIX 359..366
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 369..376
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 382..394
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 398..400
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 401..413
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 417..419
FT /evidence="ECO:0007829|PDB:6URI"
FT HELIX 420..434
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 438..452
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 453..455
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 458..467
FT /evidence="ECO:0007829|PDB:6QH5"
FT TURN 468..470
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:4UQI"
FT HELIX 475..486
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 488..490
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 493..506
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 508..511
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 514..516
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 518..529
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 534..550
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 552..554
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 555..563
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 565..568
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 573..585
FT /evidence="ECO:0007829|PDB:6QH5"
FT HELIX 592..597
FT /evidence="ECO:0007829|PDB:6QH5"
FT STRAND 598..600
FT /evidence="ECO:0007829|PDB:2VGL"
FT HELIX 610..616
FT /evidence="ECO:0007829|PDB:6URI"
SQ SEQUENCE 938 AA; 104045 MW; 406428A9BFFB1E53 CRC64;
MPAVSKGEGM RGLAVFISDI RNCKSKEAEI KRINKELANI RSKFKGDKAL DGYSKKKYVC
KLLFIFLLGH DIDFGHMEAV NLLSSNRYTE KQIGYLFISV LVNSNSELIR LINNAIKNDL
ASRNPTFMGL ALHCIANVGS REMAEAFAGE IPKILVAGDT MDSVKQSAAL CLLRLYRTSP
DLVPMGDWTS RVVHLLNDQH LGVVTAATSL ITTLAQKNPE EFKTSVSLAV SRLSRIVTSA
STDLQDYTYY FVPAPWLSVK LLRLLQCYPP PDPAVRGRLT ECLETILNKA QEPPKSKKVQ
HSNAKNAVLF EAISLIIHHD SEPNLLVRAC NQLGQFLQHR ETNLRYLALE SMCTLASSEF
SHEAVKTHIE TVINALKTER DVSVRQRAVD LLYAMCDRSN AQQIVAEMLS YLETADYSIR
EEIVLKVAIL AEKYAVDYTW YVDTILNLIR IAGDYVSEEV WYRVIQIVIN RDDVQGYAAK
TVFEALQAPA CHENLVKVGG YILGEFGNLI AGDPRSSPLI QFNLLHSKFH LCSVPTRALL
LSTYIKFVNL FPEVKATIQD VLRSDSQLKN ADVELQQRAV EYLRLSTVAS TDILATVLEE
MPPFPERESS ILAKLKKKKG PSTVTDLEET KRERSIDVNG GPEPVPASTS AASTPSPSAD
LLGLGAVPPA PTGPPPSSGG GLLVDVFSDS ASAVAPLAPG SEDNFARFVC KNNGVLFENQ
LLQIGLKSEF RQNLGRMFIF YGNKTSTQFL NFTPTLICAD DLQTNLNLQT KPVDPTVDGG
AQVQQVINIE CISDFTEAPV LNIQFRYGGT FQNVSVKLPI TLNKFFQPTE MASQDFFQRW
KQLSNPQQEV QNIFKAKHPM DTEITKAKII GFGSALLEEV DPNPANFVGA GIIHTKTTQI
GCLLRLEPNL QAQMYRLTLR TSKDTVSQRL CELLSEQF
