GLDN_HUMAN
ID GLDN_HUMAN Reviewed; 551 AA.
AC Q6ZMI3; Q6UXZ7; Q7Z359;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Gliomedin;
DE Contains:
DE RecName: Full=Gliomedin shedded ectodomain;
DE Flags: Precursor;
GN Name=GLDN; Synonyms=COLM; ORFNames=UNQ9339/PRO34011;
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 1).
RC TISSUE=Colon;
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 MRNA] (ISOFORM 2).
RC TISSUE=Colon endothelium;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 125-551 (ISOFORMS 1/2), AND
RP VARIANT ASN-265.
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [4]
RP IDENTIFICATION, AND TISSUE SPECIFICITY.
RX PubMed=16039564; DOI=10.1016/j.neuron.2005.06.026;
RA Eshed Y., Feinberg K., Poliak S., Sabanay H., Sarig-Nadir O., Spiegel I.,
RA Bermingham J.R. Jr., Peles E.;
RT "Gliomedin mediates Schwann cell-axon interaction and the molecular
RT assembly of the nodes of Ranvier.";
RL Neuron 47:215-229(2005).
RN [5]
RP INVOLVEMENT IN LCCS11, VARIANTS LCCS11 GLU-32 AND PRO-475, CHARACTERIZATION
RP OF VARIANTS LCCS11 GLU-32 AND PRO-475, INTERACTION WITH NFASC, AND
RP SUBCELLULAR LOCATION.
RX PubMed=27616481; DOI=10.1016/j.ajhg.2016.07.021;
RA Maluenda J., Manso C., Quevarec L., Vivanti A., Marguet F., Gonzales M.,
RA Guimiot F., Petit F., Toutain A., Whalen S., Grigorescu R., Coeslier A.D.,
RA Gut M., Gut I., Laquerriere A., Devaux J., Melki J.;
RT "Mutations in GLDN, encoding gliomedin, a critical component of the nodes
RT of ranvier, are responsible for lethal arthrogryposis.";
RL Am. J. Hum. Genet. 99:928-933(2016).
CC -!- FUNCTION: Ligand for NRCAM and NFASC/neurofascin that plays a role in
CC the formation and maintenance of the nodes of Ranvier on myelinated
CC axons. Mediates interaction between Schwann cell microvilli and axons
CC via its interactions with NRCAM and NFASC. Nodes of Ranvier contain
CC clustered sodium channels that are crucial for the saltatory
CC propagation of action potentials along myelinated axons. During
CC development, nodes of Ranvier are formed by the fusion of two
CC heminodes. Required for normal clustering of sodium channels at
CC heminodes; not required for the formation of mature nodes with normal
CC sodium channel clusters. Required, together with NRCAM, for maintaining
CC NFASC and sodium channel clusters at mature nodes of Ranvier.
CC {ECO:0000250|UniProtKB:Q8BMF8}.
CC -!- SUBUNIT: Homotrimer (via collagen-like domains). Interacts with NRCAM
CC and NFASC/neurofascin (PubMed:27616481). Interaction with glial NRCAM
CC enhances interaction with axonal NFASC. Interacts with MYOC.
CC {ECO:0000250|UniProtKB:Q8BMF8, ECO:0000269|PubMed:27616481}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q80WL1,
CC ECO:0000269|PubMed:27616481}; Single-pass type II membrane protein
CC {ECO:0000250|UniProtKB:Q80WL1}. Cell projection, axon
CC {ECO:0000250|UniProtKB:Q80WL1}. Note=Detected at the nodes of Ranvier.
CC Detected at immature heminodes. {ECO:0000250|UniProtKB:Q80WL1}.
CC -!- SUBCELLULAR LOCATION: [Gliomedin shedded ectodomain]: Secreted
CC {ECO:0000250|UniProtKB:Q80WL1}. Secreted, extracellular space,
CC extracellular matrix {ECO:0000250|UniProtKB:Q80WL1}. Note=Proteolytic
CC processing gives rise to a soluble extracellular domain that is
CC secreted. The gliomedin shedded ectodomain localizes to the nodes of
CC Ranvier. {ECO:0000250|UniProtKB:Q80WL1}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q6ZMI3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6ZMI3-2; Sequence=VSP_019845;
CC -!- TISSUE SPECIFICITY: Specifically expressed in spinal cord, brain,
CC placenta and sciatic nerve. More abundant in peripheral than central
CC nervous system. {ECO:0000269|PubMed:16039564}.
CC -!- DOMAIN: The olfactomedin-like domain mediates NFASC/neurofascin and
CC NRCAM binding. {ECO:0000250|UniProtKB:Q8BMF8}.
CC -!- PTM: N-glycosylated. {ECO:0000250|UniProtKB:Q8BMF8}.
CC -!- PTM: Proteolytic proccessing by a furin-like protease causes shedding
CC of the ectodomain. Further cleavage by BMP1 releases the olfactomedin-
CC like domain. {ECO:0000250|UniProtKB:Q8BMF8}.
CC -!- DISEASE: Lethal congenital contracture syndrome 11 (LCCS11)
CC [MIM:617194]: A form of lethal congenital contracture syndrome, an
CC autosomal recessive disorder characterized by degeneration of anterior
CC horn neurons, extreme skeletal muscle atrophy and congenital non-
CC progressive joint contractures. The contractures can involve the upper
CC or lower limbs and/or the vertebral column, leading to various degrees
CC of flexion or extension limitations evident at birth.
CC {ECO:0000269|PubMed:27616481}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK172756; BAD18742.1; -; mRNA.
DR EMBL; BX538105; CAD98018.1; -; mRNA.
DR EMBL; AY358144; AAQ88511.1; -; mRNA.
DR EMBL; BK001262; DAA01143.1; -; mRNA.
DR CCDS; CCDS10140.2; -. [Q6ZMI3-1]
DR CCDS; CCDS81882.1; -. [Q6ZMI3-2]
DR RefSeq; NP_001317226.1; NM_001330297.1. [Q6ZMI3-2]
DR RefSeq; NP_861454.2; NM_181789.2. [Q6ZMI3-1]
DR RefSeq; XP_016877611.1; XM_017022122.1. [Q6ZMI3-2]
DR RefSeq; XP_016877613.1; XM_017022124.1. [Q6ZMI3-2]
DR PDB; 5YBY; X-ray; 1.43 A; A=301-551.
DR PDBsum; 5YBY; -.
DR AlphaFoldDB; Q6ZMI3; -.
DR SMR; Q6ZMI3; -.
DR IntAct; Q6ZMI3; 1.
DR STRING; 9606.ENSP00000335196; -.
DR GlyConnect; 1939; 5 N-Linked glycans (2 sites).
DR GlyGen; Q6ZMI3; 5 sites, 5 N-linked glycans (2 sites).
DR iPTMnet; Q6ZMI3; -.
DR PhosphoSitePlus; Q6ZMI3; -.
DR BioMuta; GLDN; -.
DR DMDM; 74749534; -.
DR EPD; Q6ZMI3; -.
DR MassIVE; Q6ZMI3; -.
DR PaxDb; Q6ZMI3; -.
DR PeptideAtlas; Q6ZMI3; -.
DR PRIDE; Q6ZMI3; -.
DR ProteomicsDB; 67876; -. [Q6ZMI3-1]
DR ProteomicsDB; 67877; -. [Q6ZMI3-2]
DR Antibodypedia; 24837; 103 antibodies from 18 providers.
DR DNASU; 342035; -.
DR Ensembl; ENST00000335449.11; ENSP00000335196.6; ENSG00000186417.14. [Q6ZMI3-1]
DR Ensembl; ENST00000396399.6; ENSP00000379681.2; ENSG00000186417.14. [Q6ZMI3-2]
DR Ensembl; ENST00000612989.1; ENSP00000479249.1; ENSG00000186417.14. [Q6ZMI3-2]
DR GeneID; 342035; -.
DR KEGG; hsa:342035; -.
DR MANE-Select; ENST00000335449.11; ENSP00000335196.6; NM_181789.4; NP_861454.2.
DR UCSC; uc002aba.4; human. [Q6ZMI3-1]
DR CTD; 342035; -.
DR DisGeNET; 342035; -.
DR GeneCards; GLDN; -.
DR HGNC; HGNC:29514; GLDN.
DR HPA; ENSG00000186417; Tissue enriched (brain).
DR MalaCards; GLDN; -.
DR MIM; 608603; gene.
DR MIM; 617194; phenotype.
DR neXtProt; NX_Q6ZMI3; -.
DR OpenTargets; ENSG00000186417; -.
DR PharmGKB; PA134882405; -.
DR VEuPathDB; HostDB:ENSG00000186417; -.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000158020; -.
DR HOGENOM; CLU_035236_3_0_1; -.
DR InParanoid; Q6ZMI3; -.
DR OMA; HYFHGCG; -.
DR OrthoDB; 421994at2759; -.
DR PhylomeDB; Q6ZMI3; -.
DR TreeFam; TF315964; -.
DR PathwayCommons; Q6ZMI3; -.
DR SignaLink; Q6ZMI3; -.
DR SIGNOR; Q6ZMI3; -.
DR BioGRID-ORCS; 342035; 4 hits in 1061 CRISPR screens.
DR ChiTaRS; GLDN; human.
DR GenomeRNAi; 342035; -.
DR Pharos; Q6ZMI3; Tbio.
DR PRO; PR:Q6ZMI3; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q6ZMI3; protein.
DR Bgee; ENSG00000186417; Expressed in inferior vagus X ganglion and 164 other tissues.
DR ExpressionAtlas; Q6ZMI3; baseline and differential.
DR Genevisible; Q6ZMI3; HS.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; IDA:UniProtKB.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IEA:Ensembl.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; IEA:Ensembl.
DR GO; GO:0032528; P:microvillus organization; IEA:Ensembl.
DR GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR InterPro; IPR008160; Collagen.
DR InterPro; IPR031224; Gliomedin.
DR InterPro; IPR003112; Olfac-like_dom.
DR PANTHER; PTHR23192:SF5; PTHR23192:SF5; 1.
DR Pfam; PF01391; Collagen; 2.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR PROSITE; PS51132; OLF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cell membrane; Cell projection;
KW Collagen; Developmental protein; Differentiation; Disease variant;
KW Extracellular matrix; Glycoprotein; Membrane; Neurogenesis;
KW Reference proteome; Repeat; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..551
FT /note="Gliomedin"
FT /id="PRO_0000246321"
FT CHAIN 95..454
FT /note="Gliomedin shedded ectodomain"
FT /evidence="ECO:0000250|UniProtKB:Q8BMF8"
FT /id="PRO_0000434265"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..39
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 40..551
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT DOMAIN 137..195
FT /note="Collagen-like 1"
FT DOMAIN 196..222
FT /note="Collagen-like 2"
FT DOMAIN 299..546
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT REGION 72..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..257
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 94..95
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000250|UniProtKB:Q8BMF8"
FT SITE 280..281
FT /note="Cleavage; by BMP1"
FT /evidence="ECO:0000250|UniProtKB:Q8BMF8"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 329
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 357
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 378
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 464
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1..124
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:17974005"
FT /id="VSP_019845"
FT VARIANT 32
FT /note="A -> E (in LCCS11; abolishes cell surface
FT localization; abolishes interaction with NFASC;
FT dbSNP:rs779432560)"
FT /evidence="ECO:0000269|PubMed:27616481"
FT /id="VAR_078545"
FT VARIANT 141
FT /note="S -> N (in dbSNP:rs17648128)"
FT /id="VAR_027039"
FT VARIANT 265
FT /note="S -> N (in dbSNP:rs17648128)"
FT /evidence="ECO:0000269|PubMed:12975309"
FT /id="VAR_050424"
FT VARIANT 351
FT /note="D -> N (in dbSNP:rs35223886)"
FT /id="VAR_061484"
FT VARIANT 475
FT /note="A -> P (in LCCS11; abolishes cell surface
FT localization; abolishes interaction with NFASC;
FT dbSNP:rs764239923)"
FT /evidence="ECO:0000269|PubMed:27616481"
FT /id="VAR_078546"
FT CONFLICT 376
FT /note="V -> A (in Ref. 2; CAD98018)"
FT /evidence="ECO:0000305"
FT STRAND 303..307
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 311..315
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 319..325
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 328..330
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 335..351
FT /evidence="ECO:0007829|PDB:5YBY"
FT HELIX 352..357
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 361..372
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 375..377
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 380..385
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:5YBY"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:5YBY"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 426..430
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 433..440
FT /evidence="ECO:0007829|PDB:5YBY"
FT TURN 441..443
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 446..452
FT /evidence="ECO:0007829|PDB:5YBY"
FT TURN 454..456
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 459..468
FT /evidence="ECO:0007829|PDB:5YBY"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 481..485
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 489..497
FT /evidence="ECO:0007829|PDB:5YBY"
FT TURN 498..501
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 502..504
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 517..523
FT /evidence="ECO:0007829|PDB:5YBY"
FT TURN 524..527
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 528..533
FT /evidence="ECO:0007829|PDB:5YBY"
FT STRAND 536..545
FT /evidence="ECO:0007829|PDB:5YBY"
SQ SEQUENCE 551 AA; 58957 MW; CE14A36120DECE18 CRC64;
MARGAEGGRG DAGWGLRGAL AAVALLSALN AAGTVFALCQ WRGLSSALRA LEAQRGREQR
EDSALRSFLA ELSRAPRGAS APPQDPASSA RNKRSHSGEP APHIRAESHD MLMMMTYSMV
PIRVMVDLCN STKGICLTGP SGPPGPPGAG GLPGHNGLDG QPGPQGPKGE KGANGKRGKM
GIPGAAGNPG ERGEKGDHGE LGLQGNEGPP GQKGEKGDKG DVSNDVLLAG AKGDQGPPGP
PGPPGPPGPP GPPGSRRAKG PRQPSMFNGQ CPGETCAIPN DDTLVGKADE KASEHHSPQA
ESMITSIGNP VQVLKVTETF GTWIRESANK SDDRIWVTEH FSGIMVKEFK DQPSLLNGSY
TFIHLPYYFH GCGHVVYNNS LYYHKGGSNT LVRFEFGQET SQTLKLENAL YFDRKYLFAN
SKTYFNLAVD EKGLWIIYAS SVDGSSILVA QLDERTFSVV QHVNTTYPKS KAGNAFIARG
ILYVTDTKDM RVTFAFDLLG GKQINANFDL RTSQSVLAML AYNMRDQHLY SWEDGHLMLY
PVQFLSTTLN Q
