AP1S2_HUMAN
ID AP1S2_HUMAN Reviewed; 157 AA.
AC P56377; B4DSU4; O95326; Q9H2N6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 1.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=AP-1 complex subunit sigma-2;
DE AltName: Full=Adaptor protein complex AP-1 subunit sigma-1B;
DE AltName: Full=Adaptor-related protein complex 1 subunit sigma-1B;
DE AltName: Full=Clathrin assembly protein complex 1 sigma-1B small chain;
DE AltName: Full=Golgi adaptor HA1/AP1 adaptin sigma-1B subunit;
DE AltName: Full=Sigma 1B subunit of AP-1 clathrin;
DE AltName: Full=Sigma-adaptin 1B;
DE AltName: Full=Sigma1B-adaptin;
GN Name=AP1S2; ORFNames=DC22;
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).
RX PubMed=9733768; DOI=10.1074/jbc.273.38.24693;
RA Takatsu H., Sakurai M., Shin H.-W., Murakami K., Nakayama K.;
RT "Identification and characterization of novel clathrin adaptor-related
RT proteins.";
RL J. Biol. Chem. 273:24693-24700(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Dendritic cell;
RA Xu X., Yang Y., Gao G., Xiao H., Chen Z., Han Z.;
RT "Novel genes expressed in human dendritic cell.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
RA Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
RA Phelan M., Farmer A.;
RT "Cloning of human full-length CDSs in BD Creator(TM) system donor vector.";
RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Skin, and Uterus;
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 [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-98 (ISOFORM 1).
RA Barrow I.K.-P., Boguski M.S., Touchman J.W., Spencer F.;
RT "Full-insert sequence of mapped XREF EST.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP INTERACTION WITH MUC1.
RX PubMed=15471854; DOI=10.1074/jbc.m409360200;
RA Kinlough C.L., Poland P.A., Bruns J.B., Harkleroad K.L., Hughey R.P.;
RT "MUC1 membrane trafficking is modulated by multiple interactions.";
RL J. Biol. Chem. 279:53071-53077(2004).
RN [9]
RP INVOLVEMENT IN PGS.
RX PubMed=17186471; DOI=10.1086/510137;
RA Tarpey P.S., Stevens C., Teague J., Edkins S., O'Meara S., Avis T.,
RA Barthorpe S., Buck G., Butler A., Cole J., Dicks E., Gray K., Halliday K.,
RA Harrison R., Hills K., Hinton J., Jones D., Menzies A., Mironenko T.,
RA Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C.,
RA Varian J., West S., Widaa S., Yates A., Catford R., Butler J., Mallya U.,
RA Moon J., Luo Y., Dorkins H., Thompson D., Easton D.F., Wooster R.,
RA Bobrow M., Carpenter N., Simensen R.J., Schwartz C.E., Stevenson R.E.,
RA Turner G., Partington M., Gecz J., Stratton M.R., Futreal P.A.,
RA Raymond F.L.;
RT "Mutations in the gene encoding the sigma 2 subunit of the adaptor protein
RT 1 complex, AP1S2, cause X-linked mental retardation.";
RL Am. J. Hum. Genet. 79:1119-1124(2006).
RN [10]
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., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex 1 that
CC plays a role in protein sorting in the late-Golgi/trans-Golgi network
CC (TGN) and/or endosomes. The AP complexes mediate both the recruitment
CC of clathrin to membranes and the recognition of sorting signals within
CC the cytosolic tails of transmembrane cargo molecules.
CC -!- SUBUNIT: Adaptor protein complex 1 (AP-1) is a heterotetramer composed
CC of two large adaptins (gamma-type subunit AP1G1 and beta-type subunit
CC AP1B1), a medium adaptin (mu-type subunit AP1M1 or AP1M2) and a small
CC adaptin (sigma-type subunit AP1S1 or AP1S2 or AP1S3). Binds to MUC1.
CC -!- INTERACTION:
CC P56377; O43747-2: AP1G1; NbExp=4; IntAct=EBI-1054374, EBI-10185819;
CC P56377; Q9Y586: MAB21L2; NbExp=5; IntAct=EBI-1054374, EBI-6659161;
CC -!- SUBCELLULAR LOCATION: Golgi apparatus. Cytoplasmic vesicle membrane;
CC Peripheral membrane protein; Cytoplasmic side. Membrane, clathrin-
CC coated pit. Note=Component of the coat surrounding the cytoplasmic face
CC of coated vesicles located at the Golgi complex.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P56377-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P56377-2; Sequence=VSP_053671, VSP_053672;
CC -!- TISSUE SPECIFICITY: Widely expressed.
CC -!- DISEASE: Pettigrew syndrome (PGS) [MIM:304340]: An X-linked syndrome
CC characterized by intellectual disability and additional highly variable
CC features, including choreoathetosis, hydrocephalus, Dandy-Walker
CC malformation, seizures, and iron or calcium deposition in the brain.
CC Intellectual disability is characterized by significantly below average
CC general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:17186471}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the adaptor complexes small subunit family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAG44595.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB015320; BAA33392.1; -; mRNA.
DR EMBL; AF251295; AAG44595.1; ALT_INIT; mRNA.
DR EMBL; BT006738; AAP35384.1; -; mRNA.
DR EMBL; AK299921; BAG61756.1; -; mRNA.
DR EMBL; AC004106; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC001117; AAH01117.1; -; mRNA.
DR EMBL; BC071867; AAH71867.1; -; mRNA.
DR EMBL; AF091077; AAC72946.1; -; mRNA.
DR CCDS; CCDS14173.1; -. [P56377-1]
DR RefSeq; NP_003907.3; NM_003916.4. [P56377-1]
DR RefSeq; XP_011543901.1; XM_011545599.1.
DR RefSeq; XP_016885414.1; XM_017029925.1.
DR AlphaFoldDB; P56377; -.
DR SMR; P56377; -.
DR BioGRID; 114419; 49.
DR ComplexPortal; CPX-5048; Ubiquitous AP-1 Adaptor complex, sigma1b variant.
DR CORUM; P56377; -.
DR IntAct; P56377; 36.
DR STRING; 9606.ENSP00000444957; -.
DR iPTMnet; P56377; -.
DR PhosphoSitePlus; P56377; -.
DR BioMuta; AP1S2; -.
DR DMDM; 3023308; -.
DR CPTAC; CPTAC-1534; -.
DR CPTAC; CPTAC-1535; -.
DR EPD; P56377; -.
DR jPOST; P56377; -.
DR MassIVE; P56377; -.
DR MaxQB; P56377; -.
DR PaxDb; P56377; -.
DR PeptideAtlas; P56377; -.
DR PRIDE; P56377; -.
DR ProteomicsDB; 5052; -.
DR ProteomicsDB; 56915; -. [P56377-1]
DR Antibodypedia; 23979; 71 antibodies from 22 providers.
DR DNASU; 8905; -.
DR Ensembl; ENST00000329235.6; ENSP00000328789.2; ENSG00000182287.15. [P56377-1]
DR GeneID; 8905; -.
DR KEGG; hsa:8905; -.
DR CTD; 8905; -.
DR DisGeNET; 8905; -.
DR GeneCards; AP1S2; -.
DR HGNC; HGNC:560; AP1S2.
DR HPA; ENSG00000182287; Tissue enriched (epididymis).
DR MalaCards; AP1S2; -.
DR MIM; 300629; gene.
DR MIM; 304340; phenotype.
DR neXtProt; NX_P56377; -.
DR OpenTargets; ENSG00000182287; -.
DR Orphanet; 85335; Fried syndrome.
DR Orphanet; 1568; X-linked intellectual disability-Dandy-Walker malformation-basal ganglia disease-seizures syndrome.
DR Orphanet; 85329; X-linked intellectual disability-hypotonia-facial dysmorphism-aggressive behavior syndrome.
DR PharmGKB; PA24851; -.
DR VEuPathDB; HostDB:ENSG00000182287; -.
DR eggNOG; KOG0934; Eukaryota.
DR GeneTree; ENSGT00970000193372; -.
DR InParanoid; P56377; -.
DR OrthoDB; 1307450at2759; -.
DR PhylomeDB; P56377; -.
DR TreeFam; TF312921; -.
DR PathwayCommons; P56377; -.
DR Reactome; R-HSA-164940; Nef mediated downregulation of MHC class I complex cell surface expression.
DR Reactome; R-HSA-2132295; MHC class II antigen presentation.
DR Reactome; R-HSA-432720; Lysosome Vesicle Biogenesis.
DR Reactome; R-HSA-432722; Golgi Associated Vesicle Biogenesis.
DR SignaLink; P56377; -.
DR BioGRID-ORCS; 8905; 149 hits in 693 CRISPR screens.
DR ChiTaRS; AP1S2; human.
DR GeneWiki; AP1S2; -.
DR GenomeRNAi; 8905; -.
DR Pharos; P56377; Tbio.
DR PRO; PR:P56377; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; P56377; protein.
DR Bgee; ENSG00000182287; Expressed in corpus epididymis and 205 other tissues.
DR ExpressionAtlas; P56377; baseline and differential.
DR Genevisible; P56377; HS.
DR GO; GO:0030121; C:AP-1 adaptor complex; IC:ComplexPortal.
DR GO; GO:0030119; C:AP-type membrane coat adaptor complex; TAS:ProtInc.
DR GO; GO:0005905; C:clathrin-coated pit; IEA:UniProtKB-SubCell.
DR GO; GO:0030659; C:cytoplasmic vesicle membrane; TAS:Reactome.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005769; C:early endosome; IC:ComplexPortal.
DR GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
DR GO; GO:0000139; C:Golgi membrane; TAS:Reactome.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR GO; GO:0005765; C:lysosomal membrane; TAS:Reactome.
DR GO; GO:0032588; C:trans-Golgi network membrane; TAS:Reactome.
DR GO; GO:0035615; F:clathrin adaptor activity; IEA:InterPro.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR GO; GO:1903232; P:melanosome assembly; IC:ComplexPortal.
DR GO; GO:0060155; P:platelet dense granule organization; IC:ComplexPortal.
DR GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR CDD; cd14831; AP1_sigma; 1.
DR InterPro; IPR044733; AP1_sigma.
DR InterPro; IPR016635; AP_complex_ssu.
DR InterPro; IPR022775; AP_mu_sigma_su.
DR InterPro; IPR000804; Clathrin_sm-chain_CS.
DR InterPro; IPR011012; Longin-like_dom_sf.
DR PANTHER; PTHR11753; PTHR11753; 1.
DR Pfam; PF01217; Clat_adaptor_s; 1.
DR PIRSF; PIRSF015588; AP_complex_sigma; 1.
DR SUPFAM; SSF64356; SSF64356; 1.
DR PROSITE; PS00989; CLAT_ADAPTOR_S; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coated pit; Cytoplasmic vesicle; Golgi apparatus;
KW Intellectual disability; Membrane; Protein transport; Reference proteome;
KW Transport.
FT CHAIN 1..157
FT /note="AP-1 complex subunit sigma-2"
FT /id="PRO_0000193799"
FT VAR_SEQ 1
FT /note="M -> MPAGCPPHSTTASLPQHGDRGFPFAAAAAAGQAPPRPRPAAAM (in
FT isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053671"
FT VAR_SEQ 143..157
FT /note="EAETPRSVLEEIGLT -> KTETMYHSKSFIGFKKAY (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_053672"
FT CONFLICT 1
FT /note="M -> L (in Ref. 2; AAG44595)"
FT /evidence="ECO:0000305"
FT CONFLICT 72..74
FT /note="DQD -> ESRN (in Ref. 7; AAC72946)"
FT /evidence="ECO:0000305"
FT CONFLICT 96..98
FT /note="SVC -> QCL (in Ref. 7; AAC72946)"
FT /evidence="ECO:0000305"
FT CONFLICT 143
FT /note="E -> EE (in Ref. 2; AAG44595)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 157 AA; 18615 MW; DD9F59119909D89C CRC64;
MQFMLLFSRQ GKLRLQKWYV PLSDKEKKKI TRELVQTVLA RKPKMCSFLE WRDLKIVYKR
YASLYFCCAI EDQDNELITL EIIHRYVELL DKYFGSVCEL DIIFNFEKAY FILDEFLLGG
EVQETSKKNV LKAIEQADLL QEEAETPRSV LEEIGLT
