GOGA5_HUMAN
ID GOGA5_HUMAN Reviewed; 731 AA.
AC Q8TBA6; C9JRU1; O95287; Q03962; Q2TS49; Q9UQQ7;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 3.
DT 03-AUG-2022, entry version 169.
DE RecName: Full=Golgin subfamily A member 5;
DE AltName: Full=Cell proliferation-inducing gene 31 protein;
DE AltName: Full=Golgin-84;
DE AltName: Full=Protein Ret-II;
DE AltName: Full=RET-fused gene 5 protein;
GN Name=GOLGA5; Synonyms=RETII, RFG5; ORFNames=PIG31;
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), SUBCELLULAR LOCATION, TOPOLOGY,
RP DIMERIZATION, INTERACTION WITH OCRL1, AND TISSUE SPECIFICITY.
RC TISSUE=Testis;
RX PubMed=9915833; DOI=10.1074/jbc.274.5.2953;
RA Bascom R.A., Srinivasan S., Nussbaum R.L.;
RT "Identification and characterization of golgin-84, a novel Golgi integral
RT membrane protein with a cytoplasmic coiled-coil domain.";
RL J. Biol. Chem. 274:2953-2962(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Kim J.W.;
RT "Identification of a human cell proliferation gene.";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLY-67.
RC TISSUE=Placenta;
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 NUCLEOTIDE SEQUENCE [MRNA] OF 1-497 (ISOFORM 1), AND CHROMOSOMAL
RP TRANSLOCATION WITH RET.
RC TISSUE=Fibroblast;
RX PubMed=2734021;
RA Ishizaka Y., Ochiai M., Tahira T., Suhimura T., Nahao M.;
RT "Activation of the ret-II oncogene without a sequence encoding a
RT transmembrane domain and transforming activity of two ret-II oncogene
RT products differing in carboxy-termini due to alternative splicing.";
RL Oncogene 4:789-794(1989).
RN [7]
RP ERRATUM OF PUBMED:2734021.
RA Ishizaka Y., Ochiai M., Tahira T., Suhimura T., Nahao M.;
RL Oncogene 4:1415-1415(1989).
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-585, AND CHROMOSOMAL TRANSLOCATION WITH
RP RET.
RC TISSUE=Thyroid;
RX PubMed=9443391;
RA Klugbauer S., Demidchik E.P., Lengfelder E., Rabes H.M.;
RT "Detection of a novel type of Ret rearrangement (PTC5) in thyroid
RT carcinomas after Chernobyl and analysis of the involved Ret-fused gene
RT RFG5.";
RL Cancer Res. 58:198-203(1998).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 576-731 (ISOFORM 2).
RC TISSUE=Neuroblastoma;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [10]
RP FUNCTION, PHOSPHORYLATION, AND INTERACTION WITH RAB1A.
RX PubMed=12538640; DOI=10.1083/jcb.200207045;
RA Diao A., Rahman D., Pappin D.J.C., Lucocq J., Lowe M.;
RT "The coiled-coil membrane protein golgin-84 is a novel rab effector
RT required for Golgi ribbon formation.";
RL J. Cell Biol. 160:201-212(2003).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=15144186; DOI=10.1021/ac035352d;
RA Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
RA Peters E.C.;
RT "Robust phosphoproteomic profiling of tyrosine phosphorylation sites from
RT human T cells using immobilized metal affinity chromatography and tandem
RT mass spectrometry.";
RL Anal. Chem. 76:2763-2772(2004).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [13]
RP FUNCTION, AND INTERACTION WITH CUX1.
RX PubMed=15718469; DOI=10.1126/science.1108061;
RA Malsam J., Satoh A., Pelletier L., Warren G.;
RT "Golgin tethers define subpopulations of COPI vesicles.";
RL Science 307:1095-1098(2005).
RN [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [16]
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).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
CC -!- FUNCTION: Involved in maintaining Golgi structure. Stimulates the
CC formation of Golgi stacks and ribbons. Involved in intra-Golgi
CC retrograde transport. {ECO:0000269|PubMed:12538640,
CC ECO:0000269|PubMed:15718469}.
CC -!- SUBUNIT: Homodimer. Interacts with RAB1A that has been activated by
CC GTP-binding, and possibly also with OCRL1. Interacts with isoform CASP
CC of CUX1. {ECO:0000269|PubMed:12538640, ECO:0000269|PubMed:15718469,
CC ECO:0000269|PubMed:9915833}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane
CC {ECO:0000269|PubMed:9915833}; Single-pass type IV membrane protein
CC {ECO:0000269|PubMed:9915833}. Note=Found throughout the Golgi, both on
CC cisternae and, at higher abundance, on the tubulo-vesicular structures
CC of the cis-Golgi network.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q8TBA6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8TBA6-2; Sequence=VSP_007731, VSP_007732;
CC -!- TISSUE SPECIFICITY: Ubiquitous. Highly expressed in seminiferous
CC tubules and Leydig cells in testis, and detected at much lower levels
CC in the other tissues tested. Expression is very low or not detectable
CC in spermatozoa. {ECO:0000269|PubMed:9915833}.
CC -!- PTM: Highly phosphorylated during mitosis. Phosphorylation is barely
CC detectable during interphase. {ECO:0000269|PubMed:12538640}.
CC -!- DISEASE: Note=A chromosomal aberration involving GOLGA5 is found in
CC papillary thyroid carcinomas (PTCs). Translocation t(10;14)(q11;q32)
CC with RET. The translocation generates the RET/GOLGA5 (PTC5) oncogene.
CC {ECO:0000269|PubMed:2734021, ECO:0000269|PubMed:9443391}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA33787.1; Type=Miscellaneous discrepancy; Note=Chimeric cDNA. A chimeric cDNA originating from chromosomes 14 and 10.; Evidence={ECO:0000305};
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DR EMBL; AF085199; AAD09753.1; -; mRNA.
DR EMBL; AY644768; AAV85456.1; -; mRNA.
DR EMBL; AL132987; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81502.1; -; Genomic_DNA.
DR EMBL; BC023021; AAH23021.1; -; mRNA.
DR EMBL; X15786; CAA33787.1; ALT_SEQ; mRNA.
DR EMBL; AJ132949; CAB36967.1; -; mRNA.
DR EMBL; BX248744; CAD66551.1; -; mRNA.
DR CCDS; CCDS9905.1; -. [Q8TBA6-1]
DR PIR; I38153; I38153.
DR RefSeq; NP_005104.3; NM_005113.3. [Q8TBA6-1]
DR RefSeq; XP_011535722.1; XM_011537420.2. [Q8TBA6-2]
DR AlphaFoldDB; Q8TBA6; -.
DR SMR; Q8TBA6; -.
DR BioGRID; 115275; 218.
DR IntAct; Q8TBA6; 56.
DR MINT; Q8TBA6; -.
DR STRING; 9606.ENSP00000163416; -.
DR TCDB; 9.B.392.1.1; the golgi apparatus golgin (golgin) family.
DR iPTMnet; Q8TBA6; -.
DR PhosphoSitePlus; Q8TBA6; -.
DR BioMuta; GOLGA5; -.
DR DMDM; 296439337; -.
DR EPD; Q8TBA6; -.
DR jPOST; Q8TBA6; -.
DR MassIVE; Q8TBA6; -.
DR MaxQB; Q8TBA6; -.
DR PaxDb; Q8TBA6; -.
DR PeptideAtlas; Q8TBA6; -.
DR PRIDE; Q8TBA6; -.
DR ProteomicsDB; 73978; -. [Q8TBA6-1]
DR ProteomicsDB; 73979; -. [Q8TBA6-2]
DR ABCD; Q8TBA6; 1 sequenced antibody.
DR Antibodypedia; 15; 264 antibodies from 26 providers.
DR DNASU; 9950; -.
DR Ensembl; ENST00000163416.7; ENSP00000163416.2; ENSG00000066455.13. [Q8TBA6-1]
DR GeneID; 9950; -.
DR KEGG; hsa:9950; -.
DR MANE-Select; ENST00000163416.7; ENSP00000163416.2; NM_005113.4; NP_005104.4.
DR UCSC; uc001yaz.3; human. [Q8TBA6-1]
DR CTD; 9950; -.
DR DisGeNET; 9950; -.
DR GeneCards; GOLGA5; -.
DR HGNC; HGNC:4428; GOLGA5.
DR HPA; ENSG00000066455; Low tissue specificity.
DR MalaCards; GOLGA5; -.
DR MIM; 606918; gene.
DR neXtProt; NX_Q8TBA6; -.
DR OpenTargets; ENSG00000066455; -.
DR Orphanet; 146; Differentiated thyroid carcinoma.
DR PharmGKB; PA28809; -.
DR VEuPathDB; HostDB:ENSG00000066455; -.
DR eggNOG; KOG4677; Eukaryota.
DR GeneTree; ENSGT00390000018470; -.
DR HOGENOM; CLU_022484_0_0_1; -.
DR InParanoid; Q8TBA6; -.
DR OMA; CSSYEAH; -.
DR OrthoDB; 1325011at2759; -.
DR PhylomeDB; Q8TBA6; -.
DR TreeFam; TF319468; -.
DR PathwayCommons; Q8TBA6; -.
DR Reactome; R-HSA-6811438; Intra-Golgi traffic.
DR SignaLink; Q8TBA6; -.
DR BioGRID-ORCS; 9950; 5 hits in 1078 CRISPR screens.
DR ChiTaRS; GOLGA5; human.
DR GeneWiki; GOLGA5; -.
DR GenomeRNAi; 9950; -.
DR Pharos; Q8TBA6; Tbio.
DR PRO; PR:Q8TBA6; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8TBA6; protein.
DR Bgee; ENSG00000066455; Expressed in secondary oocyte and 194 other tissues.
DR ExpressionAtlas; Q8TBA6; baseline and differential.
DR Genevisible; Q8TBA6; HS.
DR GO; GO:0005801; C:cis-Golgi network; IDA:UniProtKB.
DR GO; GO:0005794; C:Golgi apparatus; IDA:UniProtKB.
DR GO; GO:0031985; C:Golgi cisterna; IDA:UniProtKB.
DR GO; GO:0000139; C:Golgi membrane; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030133; C:transport vesicle; TAS:Reactome.
DR GO; GO:0042803; F:protein homodimerization activity; IPI:UniProtKB.
DR GO; GO:0031267; F:small GTPase binding; IDA:UniProtKB.
DR GO; GO:0007030; P:Golgi organization; IMP:UniProtKB.
DR GO; GO:0048193; P:Golgi vesicle transport; IMP:UniProtKB.
DR GO; GO:0000301; P:retrograde transport, vesicle recycling within Golgi; IBA:GO_Central.
DR InterPro; IPR019177; Golgin_subfamily_A_member_5.
DR PANTHER; PTHR13815; PTHR13815; 1.
DR Pfam; PF09787; Golgin_A5; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosomal rearrangement; Coiled coil;
KW Golgi apparatus; Membrane; Methylation; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:22223895"
FT CHAIN 2..731
FT /note="Golgin subfamily A member 5"
FT /id="PRO_0000190061"
FT TOPO_DOM 2..698
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 699..719
FT /note="Helical; Anchor for type IV membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 720..731
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 93..222
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 216..632
FT /evidence="ECO:0000255"
FT COMPBIAS 147..187
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 497..498
FT /note="Breakpoint for translocation to form RET-GOLGA5
FT oncogene"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0007744|PubMed:22223895"
FT MOD_RES 89
FT /note="Dimethylated arginine"
FT /evidence="ECO:0000250|UniProtKB:Q3ZU82"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT VAR_SEQ 684..691
FT /note="SIRLGIFL -> RLCFTSGS (in isoform 2)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_007731"
FT VAR_SEQ 692..731
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.9"
FT /id="VSP_007732"
FT VARIANT 67
FT /note="A -> G (in dbSNP:rs17128572)"
FT /evidence="ECO:0000269|PubMed:15489334"
FT /id="VAR_055859"
FT VARIANT 486
FT /note="M -> V (in dbSNP:rs34139657)"
FT /id="VAR_055860"
FT CONFLICT 350
FT /note="F -> L (in Ref. 1; AAD09753, 2; AAV85456, 4;
FT EAW81502, 5; AAH23021, 6; CAA33787 and 8; CAB36967)"
FT /evidence="ECO:0000305"
FT CONFLICT 584..585
FT /note="QS -> PV (in Ref. 8; CAB36967)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 731 AA; 83024 MW; 650B5D46096A2DDE CRC64;
MSWFVDLAGK AEDLLNRVDQ GAATALSRKD NASNIYSKNT DYTELHQQNT DLIYQTGPKS
TYISSAADNI RNQKATILAG TANVKVGSRT PVEASHPVEN ASVPRPSSHF VRRKKSEPDD
ELLFDFLNSS QKEPTGRVEI RKEKGKTPVF QSSQTSSVSS VNPSVTTIKT IEENSFGSQT
HEAASNSDSS HEGQEESSKE NVSSNAACPD HTPTPNDDGK SHELSNLRLE NQLLRNEVQS
LNQEMASLLQ RSKETQEELN KARARVEKWN ADHSKSDRMT RGLRAQVDDL TEAVAAKDSQ
LAVLKVRLQE ADQLLSTRTE ALEALQSEKS RIMQDQSEGN SLQNQALQTF QERLHEADAT
LKREQESYKQ MQSEFAARLN KVEMERQNLA EAITLAERKY SDEKKRVDEL QQQVKLYKLN
LESSKQELID YKQKATRILQ SKEKLINSLK EGSGFEGLDS STASSMELEE LRHEKEMQRE
EIQKLMGQIH QLRSELQDME AQQVNEAESA REQLQDLHDQ IAGQKASKQE LETELERLKQ
EFHYIEEDLY RTKNTLQSRI KDRDEEIQKL RNQLTNKTLS NSSQSELENR LHQLTETLIQ
KQTMLESLST EKNSLVFQLE RLEQQMNSAS GSSSNGSSIN MSGIDNGEGT RLRNVPVLFN
DTETNLAGMY GKVRKAASSI DQFSIRLGIF LRRYPIARVF VIIYMALLHL WVMIVLLTYT
PEMHHDQPYG K
