SESQ1_HUMAN
ID SESQ1_HUMAN Reviewed; 249 AA.
AC Q8N4B1; J3KP50; Q6PJL9; Q96MH8;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Sesquipedalian-1 {ECO:0000305|PubMed:20133602};
DE Short=Ses1;
DE AltName: Full=27 kDa inositol polyphosphate phosphatase-interacting protein A;
DE Short=IPIP27A;
DE AltName: Full=PH domain-containing endocytic trafficking adaptor 1 {ECO:0000305};
GN Name=PHETA1 {ECO:0000312|HGNC:HGNC:26509};
GN Synonyms=FAM109A {ECO:0000312|HGNC:HGNC:26509};
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 [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Prostate;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1-80 (ISOFORM 4).
RC TISSUE=Brain;
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 [4]
RP INTERACTION WITH OCRL AND INPP5B, SUBCELLULAR LOCATION, F&H MOTIF, AND
RP MUTAGENESIS OF PHE-224 AND HIS-228.
RX PubMed=20133602; DOI=10.1073/pnas.0914658107;
RA Swan L.E., Tomasini L., Pirruccello M., Lunardi J., De Camilli P.;
RT "Two closely related endocytic proteins that share a common OCRL-binding
RT motif with APPL1.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:3511-3516(2010).
RN [5]
RP FUNCTION, INTERACTION WITH OCRL AND INPP5B, SUBUNIT, SUBCELLULAR LOCATION,
RP AND MUTAGENESIS OF PHE-224; HIS-228 AND 234-GLU-ILE-235.
RX PubMed=21233288; DOI=10.1091/mbc.e10-08-0730;
RA Noakes C.J., Lee G., Lowe M.;
RT "The PH domain proteins IPIP27A and B link OCRL1 to receptor recycling in
RT the endocytic pathway.";
RL Mol. Biol. Cell 22:606-623(2011).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-213, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [7]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 223-235 IN COMPLEX WITH OCRL, AND
RP F&H MOTIF.
RX PubMed=21666675; DOI=10.1038/nsmb.2071;
RA Pirruccello M., Swan L.E., Folta-Stogniew E., De Camilli P.;
RT "Recognition of the F&H motif by the Lowe syndrome protein OCRL.";
RL Nat. Struct. Mol. Biol. 18:789-795(2011).
CC -!- FUNCTION: Plays a role in endocytic trafficking. Required for receptor
CC recycling from endosomes, both to the trans-Golgi network and the
CC plasma membrane. {ECO:0000269|PubMed:21233288}.
CC -!- SUBUNIT: Forms homodimers and heterodimers with PHETA2
CC (PubMed:21233288). Interacts with OCRL and INPP5B (PubMed:20133602,
CC PubMed:21233288, PubMed:21666675). Interaction with OCRL may be
CC important for endosomal morphology and function (By similarity).
CC {ECO:0000250|UniProtKB:D3ZL52, ECO:0000269|PubMed:20133602,
CC ECO:0000269|PubMed:21233288, ECO:0000269|PubMed:21666675}.
CC -!- INTERACTION:
CC Q8N4B1-4; Q9NYB9-2: ABI2; NbExp=8; IntAct=EBI-14131832, EBI-11096309;
CC Q8N4B1-4; Q9H3H3-3: C11orf68; NbExp=3; IntAct=EBI-14131832, EBI-12002214;
CC Q8N4B1-4; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-14131832, EBI-3867333;
CC Q8N4B1-4; A0A0C3SFZ9: FCHO1; NbExp=3; IntAct=EBI-14131832, EBI-11977403;
CC Q8N4B1-4; P62993: GRB2; NbExp=3; IntAct=EBI-14131832, EBI-401755;
CC Q8N4B1-4; P49639: HOXA1; NbExp=3; IntAct=EBI-14131832, EBI-740785;
CC Q8N4B1-4; Q8IUG1: KRTAP1-3; NbExp=3; IntAct=EBI-14131832, EBI-11749135;
CC Q8N4B1-4; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-14131832, EBI-11953846;
CC Q8N4B1-4; O43639: NCK2; NbExp=3; IntAct=EBI-14131832, EBI-713635;
CC Q8N4B1-4; Q01968-2: OCRL; NbExp=3; IntAct=EBI-14131832, EBI-11749425;
CC Q8N4B1-4; O43482: OIP5; NbExp=3; IntAct=EBI-14131832, EBI-536879;
CC Q8N4B1-4; Q6ICB4: PHETA2; NbExp=5; IntAct=EBI-14131832, EBI-11081747;
CC Q8N4B1-4; Q9NW61: PLEKHJ1; NbExp=3; IntAct=EBI-14131832, EBI-1057560;
CC Q8N4B1-4; O60504: SORBS3; NbExp=3; IntAct=EBI-14131832, EBI-741237;
CC -!- SUBCELLULAR LOCATION: Early endosome {ECO:0000269|PubMed:21233288}.
CC Recycling endosome {ECO:0000269|PubMed:21233288}. Golgi apparatus,
CC trans-Golgi network {ECO:0000269|PubMed:21233288}. Cytoplasmic vesicle,
CC clathrin-coated vesicle {ECO:0000269|PubMed:21233288}. Note=Interaction
CC with OCRL may be crucial for targeting to endosome and to the trans-
CC Golgi network. Also found on macropinosomes. Not detected in late
CC endosomes, nor in lysosomes. {ECO:0000269|PubMed:20133602,
CC ECO:0000269|PubMed:21233288}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q8N4B1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8N4B1-2; Sequence=VSP_021239, VSP_021240;
CC Name=3;
CC IsoId=Q8N4B1-3; Sequence=VSP_021241, VSP_021242;
CC Name=4;
CC IsoId=Q8N4B1-4; Sequence=VSP_044836;
CC -!- DOMAIN: The F&H motif, an approximately 12-13 amino-acid sequence
CC centered around Phe and His residues, is essential for binding to OCRL
CC and INPP5B. {ECO:0000269|PubMed:21666675}.
CC -!- MISCELLANEOUS: Was named after 'sesquipedalian', an unnecessarily long
CC description of a simple thing. {ECO:0000305|PubMed:20133602}.
CC -!- SIMILARITY: Belongs to the sesquipedalian family. {ECO:0000305}.
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DR EMBL; AK056918; BAB71310.1; -; mRNA.
DR EMBL; AC005805; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC014091; AAH14091.1; -; mRNA.
DR EMBL; BC034809; AAH34809.1; -; mRNA.
DR EMBL; CX758147; -; NOT_ANNOTATED_CDS; mRNA.
DR CCDS; CCDS53833.1; -. [Q8N4B1-4]
DR CCDS; CCDS9152.1; -. [Q8N4B1-1]
DR RefSeq; NP_001171467.1; NM_001177996.1. [Q8N4B1-4]
DR RefSeq; NP_001171468.1; NM_001177997.1. [Q8N4B1-1]
DR RefSeq; NP_653272.2; NM_144671.4. [Q8N4B1-1]
DR RefSeq; XP_006719320.1; XM_006719257.3. [Q8N4B1-1]
DR RefSeq; XP_011536278.1; XM_011537976.2. [Q8N4B1-1]
DR RefSeq; XP_016874372.1; XM_017018883.1. [Q8N4B1-1]
DR PDB; 3QIS; X-ray; 2.30 A; B=223-235.
DR PDBsum; 3QIS; -.
DR AlphaFoldDB; Q8N4B1; -.
DR SMR; Q8N4B1; -.
DR BioGRID; 126873; 39.
DR ELM; Q8N4B1; -.
DR IntAct; Q8N4B1; 19.
DR MINT; Q8N4B1; -.
DR STRING; 9606.ENSP00000354461; -.
DR iPTMnet; Q8N4B1; -.
DR PhosphoSitePlus; Q8N4B1; -.
DR BioMuta; FAM109A; -.
DR DMDM; 74728832; -.
DR EPD; Q8N4B1; -.
DR jPOST; Q8N4B1; -.
DR MassIVE; Q8N4B1; -.
DR MaxQB; Q8N4B1; -.
DR PaxDb; Q8N4B1; -.
DR PeptideAtlas; Q8N4B1; -.
DR PRIDE; Q8N4B1; -.
DR ProteomicsDB; 71901; -. [Q8N4B1-1]
DR ProteomicsDB; 71902; -. [Q8N4B1-2]
DR ProteomicsDB; 71903; -. [Q8N4B1-3]
DR Antibodypedia; 45279; 73 antibodies from 16 providers.
DR DNASU; 144717; -.
DR Ensembl; ENST00000361483.4; ENSP00000354461.3; ENSG00000198324.14. [Q8N4B1-4]
DR Ensembl; ENST00000547838.2; ENSP00000447353.1; ENSG00000198324.14. [Q8N4B1-1]
DR Ensembl; ENST00000548163.1; ENSP00000449994.1; ENSG00000198324.14. [Q8N4B1-1]
DR Ensembl; ENST00000683047.1; ENSP00000507123.1; ENSG00000198324.14. [Q8N4B1-1]
DR GeneID; 144717; -.
DR KEGG; hsa:144717; -.
DR MANE-Select; ENST00000683047.1; ENSP00000507123.1; NM_144671.6; NP_653272.2.
DR UCSC; uc021rdy.1; human. [Q8N4B1-1]
DR CTD; 144717; -.
DR DisGeNET; 144717; -.
DR GeneCards; PHETA1; -.
DR HGNC; HGNC:26509; PHETA1.
DR HPA; ENSG00000198324; Low tissue specificity.
DR MIM; 614239; gene.
DR neXtProt; NX_Q8N4B1; -.
DR OpenTargets; ENSG00000198324; -.
DR PharmGKB; PA143485466; -.
DR VEuPathDB; HostDB:ENSG00000198324; -.
DR eggNOG; ENOG502QQ94; Eukaryota.
DR GeneTree; ENSGT00940000162791; -.
DR HOGENOM; CLU_060423_0_1_1; -.
DR InParanoid; Q8N4B1; -.
DR OMA; NGCAVWN; -.
DR OrthoDB; 1329965at2759; -.
DR PhylomeDB; Q8N4B1; -.
DR TreeFam; TF326731; -.
DR PathwayCommons; Q8N4B1; -.
DR SignaLink; Q8N4B1; -.
DR BioGRID-ORCS; 144717; 9 hits in 1077 CRISPR screens.
DR ChiTaRS; FAM109A; human.
DR GenomeRNAi; 144717; -.
DR Pharos; Q8N4B1; Tbio.
DR PRO; PR:Q8N4B1; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q8N4B1; protein.
DR Bgee; ENSG00000198324; Expressed in pancreatic ductal cell and 176 other tissues.
DR ExpressionAtlas; Q8N4B1; baseline and differential.
DR Genevisible; Q8N4B1; HS.
DR GO; GO:0030136; C:clathrin-coated vesicle; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IEA:GOC.
DR GO; GO:0005769; C:early endosome; IDA:UniProtKB.
DR GO; GO:0055037; C:recycling endosome; IDA:UniProtKB.
DR GO; GO:0005802; C:trans-Golgi network; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0007032; P:endosome organization; IMP:UniProtKB.
DR GO; GO:0001881; P:receptor recycling; IMP:UniProtKB.
DR GO; GO:0042147; P:retrograde transport, endosome to Golgi; IMP:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR045188; Boi1/Boi2-like.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR PANTHER; PTHR22902; PTHR22902; 1.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR PROSITE; PS50003; PH_DOMAIN; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasmic vesicle; Endosome;
KW Golgi apparatus; Phosphoprotein; Reference proteome.
FT CHAIN 1..249
FT /note="Sesquipedalian-1"
FT /id="PRO_0000254572"
FT DOMAIN 17..113
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 134..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 194..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 223..235
FT /note="F&H"
FT COMPBIAS 142..159
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..213
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 213
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..123
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021239"
FT VAR_SEQ 1
FT /note="M -> MAPGSPPGPAIATM (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_044836"
FT VAR_SEQ 64..88
FT /note="EGCTVELVEAAEEFAFAVRFAGTRA -> VAVALWPRALSVSPWWLSQGSPD
FT TP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021241"
FT VAR_SEQ 89..249
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_021242"
FT VAR_SEQ 124..138
FT /note="EQQLAAVRGGGGMAL -> MQKQRPREMNSLPGV (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_021240"
FT MUTAGEN 224
FT /note="F->A: Loss of OCRL-binding. Drastically reduces
FT membrane targeting."
FT /evidence="ECO:0000269|PubMed:20133602,
FT ECO:0000269|PubMed:21233288"
FT MUTAGEN 228
FT /note="H->A: Loss of OCRL-binding."
FT /evidence="ECO:0000269|PubMed:20133602,
FT ECO:0000269|PubMed:21233288"
FT MUTAGEN 234..235
FT /note="EI->AA: Loss of OCRL-binding."
FT /evidence="ECO:0000269|PubMed:21233288"
FT HELIX 224..231
FT /evidence="ECO:0007829|PDB:3QIS"
FT TURN 232..234
FT /evidence="ECO:0007829|PDB:3QIS"
SQ SEQUENCE 249 AA; 27215 MW; 73410C946DA6113A CRC64;
MKLNERSLAF YATCDAPVDN AGFLYKKGGR HAAYHRRWFV LRGNMLFYFE DAASREPVGV
IILEGCTVEL VEAAEEFAFA VRFAGTRART YVLAAESQDA MEGWVKALSR ASFDYLRLVV
RELEQQLAAV RGGGGMALPQ PQPQSLPLPP SLPSALAPVP SLPSAPAPVP ALPLPRRPSA
LPPKENGCAV WSTEATFRPG PEPPPPPPRR RASAPHGPLD MAPFARLHEC YGQEIRALRG
QWLSSRVQP
