GLDN_MOUSE
ID GLDN_MOUSE Reviewed; 549 AA.
AC Q8BMF8; Q80ZC5;
DT 25-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=Gliomedin;
DE AltName: Full=Cancer-related gene liver 2 protein;
DE Short=CRG-L2;
DE Contains:
DE RecName: Full=Gliomedin shedded ectodomain;
DE Flags: Precursor;
GN Name=Gldn; Synonyms=Crgl2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Fetal testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 103-549, AND TISSUE SPECIFICITY.
RC STRAIN=C3H/HeJ; TISSUE=Liver tumor;
RX PubMed=12642876; DOI=10.1038/sj.onc.1206309;
RA Graveel C.R., Harkins-Perry S.R., Acevedo L.G., Farnham P.J.;
RT "Identification and characterization of CRG-L2, a new marker for liver
RT tumor development.";
RL Oncogene 22:1730-1736(2003).
RN [3]
RP INTERACTION WITH NRCAM.
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 [4]
RP SUBCELLULAR LOCATION, GLYCOSYLATION, SUBUNIT, PROTEIN SEQUENCE OF 95-99;
RP 122-128 AND 278-289, AND MUTAGENESIS OF ARG-91 AND 278-ASP-ASP-279.
RX PubMed=17293346; DOI=10.1074/jbc.m611339200;
RA Maertens B., Hopkins D., Franzke C.W., Keene D.R., Bruckner-Tuderman L.,
RA Greenspan D.S., Koch M.;
RT "Cleavage and oligomerization of gliomedin, a transmembrane collagen
RT required for node of ranvier formation.";
RL J. Biol. Chem. 282:10647-10659(2007).
RN [5]
RP DISRUPTION PHENOTYPE, FUNCTION, INTERACTION WITH NRCAM AND NFASC, DOMAIN,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=20188654; DOI=10.1016/j.neuron.2010.02.004;
RA Feinberg K., Eshed-Eisenbach Y., Frechter S., Amor V., Salomon D.,
RA Sabanay H., Dupree J.L., Grumet M., Brophy P.J., Shrager P., Peles E.;
RT "A glial signal consisting of gliomedin and NrCAM clusters axonal Na+
RT channels during the formation of nodes of Ranvier.";
RL Neuron 65:490-502(2010).
RN [6]
RP INTERACTION WITH MYOC.
RX PubMed=23897819; DOI=10.1074/jbc.m112.446138;
RA Kwon H.S., Johnson T.V., Joe M.K., Abu-Asab M., Zhang J., Chan C.C.,
RA Tomarev S.I.;
RT "Myocilin mediates myelination in the peripheral nervous system through
RT ErbB2/3 signaling.";
RL J. Biol. Chem. 288:26357-26371(2013).
RN [7]
RP DISRUPTION PHENOTYPE, FUNCTION, AND TISSUE SPECIFICITY.
RX PubMed=24719088; DOI=10.1523/jneurosci.4752-13.2014;
RA Amor V., Feinberg K., Eshed-Eisenbach Y., Vainshtein A., Frechter S.,
RA Grumet M., Rosenbluth J., Peles E.;
RT "Long-term maintenance of Na+ channels at nodes of Ranvier depends on glial
RT contact mediated by gliomedin and NrCAM.";
RL J. Neurosci. 34:5089-5098(2014).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 279-549.
RX PubMed=26121352; DOI=10.1371/journal.pone.0130888;
RA Hill S.E., Donegan R.K., Nguyen E., Desai T.M., Lieberman R.L.;
RT "Molecular details of olfactomedin domains provide pathway to structure-
RT function studies.";
RL PLoS ONE 10:E0130888-E0130888(2015).
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 (PubMed:20188654). Nodes of
CC Ranvier contain clustered sodium channels that are crucial for the
CC saltatory propagation of action potentials along myelinated axons.
CC During 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 (PubMed:20188654). Required, together with
CC NRCAM, for maintaining NFASC and sodium channel clusters at mature
CC nodes of Ranvier (PubMed:24719088). {ECO:0000250|UniProtKB:Q80WL1,
CC ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:24719088}.
CC -!- SUBUNIT: Homotrimer (via collagen-like domains) (PubMed:17293346).
CC Interacts with NRCAM and NFASC/neurofascin (PubMed:16039564,
CC PubMed:20188654). Interaction with glial NRCAM enhances interaction
CC with axonal NFASC (PubMed:20188654). Interacts with MYOC
CC (PubMed:23897819). {ECO:0000269|PubMed:16039564,
CC ECO:0000269|PubMed:17293346, ECO:0000269|PubMed:20188654,
CC ECO:0000269|PubMed:23897819}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:17293346};
CC Single-pass type II membrane protein {ECO:0000305|PubMed:17293346}.
CC Cell projection, axon {ECO:0000269|PubMed:17293346,
CC ECO:0000269|PubMed:20188654}. Note=Localizes to the nodes of Ranvier
CC (PubMed:17293346, PubMed:20188654). Detected at immature heminodes (By
CC similarity). {ECO:0000250|UniProtKB:Q80WL1,
CC ECO:0000269|PubMed:17293346, ECO:0000269|PubMed:20188654}.
CC -!- SUBCELLULAR LOCATION: [Gliomedin shedded ectodomain]: Secreted
CC {ECO:0000269|PubMed:17293346}. 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 (PubMed:17293346). The gliomedin shedded ectodomain localizes
CC to the nodes of Ranvier (By similarity). {ECO:0000250|UniProtKB:Q80WL1,
CC ECO:0000269|PubMed:17293346}.
CC -!- TISSUE SPECIFICITY: Detected in sciatic nerve (at protein level)
CC (PubMed:17293346, PubMed:20188654, PubMed:24719088). Widely expressed
CC with higher expression in testis and skeletal muscle (PubMed:12642876).
CC {ECO:0000269|PubMed:12642876, ECO:0000269|PubMed:17293346,
CC ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:24719088}.
CC -!- DOMAIN: The olfactomedin-like domain mediates NFASC/neurofascin and
CC NRCAM binding. {ECO:0000269|PubMed:20188654}.
CC -!- PTM: N-glycosylated. {ECO:0000269|PubMed:17293346}.
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:0000269|PubMed:17293346}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice present no obvious neurological
CC phenotype and have normal nerve conduction. Nerves from their
CC peripheral nervous system have myelin sheets that are indistinguishable
CC from wild-type. In contrast, they present impaired and disorganized
CC attachment of Schwann cell microvilli to the axolemma at nodes of
CC Ranvier. Mature nodes are formed by the fusion of two heminodes. During
CC development, mutant mice present defective clustering of sodium
CC channels at heminodes, but display normal sodium channel clustering at
CC mature nodes (PubMed:20188654). Mice lacking both Gldn and Nrcam are
CC born at the expected Mendelian rate, but are smaller than control
CC littermates and display important neurological impairments, in spite of
CC seemingly normal nerve myelination. Motor abnormalities vary between
CC individuals, ranging from ataxia, uncoordinated movements and premature
CC death to weakness of the hind limbs, hypomotility, strongly impaired
CC ability to hang from a horizontal bar with their forelimbs and a
CC tendency to stumble. The motor defects correlate with decreased
CC velocity of nerve conduction and slower propagation of action
CC potentials. Most mice die within 60 days after birth, and none are
CC fertile. Mutant mice display delayed formation of mature nodes of
CC Ranvier; 15 days after birth about 20% of the nodes lack detectable
CC sodium channel clusters. Sodium channel clustering and nerve conduction
CC appear normal 60 and 75 days after birth, but subsequently a gradual
CC disintegration of the nodal protein complexes is seen. About 70% of the
CC mutant nodes present high-density sodium channel clustering at 120 days
CC after birth, as opposed to nearly 100% for wild-type. Contrary to wild-
CC type, in adult nodes of Ranvier the sodium channels are often clustered
CC near the paranode border with an empty gap in the middle. At nodes of
CC Ranvier, Schwann cell microvilli are sparse or absent and show defects
CC in their orientation, resulting in various structural abnormalities at
CC the node and the paranode border (PubMed:24719088).
CC {ECO:0000269|PubMed:20188654, ECO:0000269|PubMed:24719088}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO49510.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK031523; BAC27432.1; -; mRNA.
DR EMBL; AF548022; AAO49510.1; ALT_INIT; mRNA.
DR CCDS; CCDS23189.1; -.
DR RefSeq; NP_796324.1; NM_177350.5.
DR PDB; 4XAV; X-ray; 2.05 A; A/B/C/D=279-549.
DR PDBsum; 4XAV; -.
DR AlphaFoldDB; Q8BMF8; -.
DR SMR; Q8BMF8; -.
DR STRING; 10090.ENSMUSP00000056080; -.
DR GlyGen; Q8BMF8; 6 sites.
DR iPTMnet; Q8BMF8; -.
DR PhosphoSitePlus; Q8BMF8; -.
DR PaxDb; Q8BMF8; -.
DR PRIDE; Q8BMF8; -.
DR ProteomicsDB; 266776; -.
DR Antibodypedia; 24837; 103 antibodies from 18 providers.
DR DNASU; 235379; -.
DR Ensembl; ENSMUST00000056740; ENSMUSP00000056080; ENSMUSG00000046167.
DR GeneID; 235379; -.
DR KEGG; mmu:235379; -.
DR UCSC; uc009pqx.1; mouse.
DR CTD; 342035; -.
DR MGI; MGI:2388361; Gldn.
DR VEuPathDB; HostDB:ENSMUSG00000046167; -.
DR eggNOG; KOG3545; Eukaryota.
DR GeneTree; ENSGT00940000158020; -.
DR HOGENOM; CLU_035236_3_0_1; -.
DR InParanoid; Q8BMF8; -.
DR OMA; HYFHGCG; -.
DR OrthoDB; 421994at2759; -.
DR PhylomeDB; Q8BMF8; -.
DR TreeFam; TF315964; -.
DR BioGRID-ORCS; 235379; 2 hits in 72 CRISPR screens.
DR ChiTaRS; Gldn; mouse.
DR PRO; PR:Q8BMF8; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q8BMF8; protein.
DR Bgee; ENSMUSG00000046167; Expressed in lip and 21 other tissues.
DR GO; GO:0030424; C:axon; IEA:UniProtKB-SubCell.
DR GO; GO:0009986; C:cell surface; ISO:MGI.
DR GO; GO:0005581; C:collagen trimer; IEA:UniProtKB-KW.
DR GO; GO:0005615; C:extracellular space; IDA:MGI.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:MGI.
DR GO; GO:0086080; F:protein binding involved in heterotypic cell-cell adhesion; IGI:MGI.
DR GO; GO:0045162; P:clustering of voltage-gated sodium channels; IMP:MGI.
DR GO; GO:0032528; P:microvillus organization; IMP:MGI.
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; 1.
DR Pfam; PF02191; OLF; 1.
DR SMART; SM00284; OLF; 1.
DR PROSITE; PS51132; OLF; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Cell projection; Collagen;
KW Developmental protein; Differentiation; Direct protein sequencing;
KW Extracellular matrix; Glycoprotein; Membrane; Neurogenesis;
KW Reference proteome; Repeat; Secreted; Signal-anchor; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..549
FT /note="Gliomedin"
FT /id="PRO_0000246322"
FT CHAIN 95..451
FT /note="Gliomedin shedded ectodomain"
FT /evidence="ECO:0000305|PubMed:17293346"
FT /id="PRO_0000434266"
FT TOPO_DOM 1..17
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 18..38
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 39..549
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 296..543
FT /note="Olfactomedin-like"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00446"
FT REGION 75..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 137..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..256
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 259..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 94..95
FT /note="Cleavage; by furin-like protease"
FT /evidence="ECO:0000269|PubMed:17293346"
FT SITE 277..278
FT /note="Cleavage; by BMP1"
FT /evidence="ECO:0000269|PubMed:17293346"
FT CARBOHYD 130
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 326
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 461
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT MUTAGEN 91
FT /note="R->A: Abolishes furin-mediated cleavage and shedding
FT of ectodomain."
FT /evidence="ECO:0000269|PubMed:17293346"
FT MUTAGEN 278..279
FT /note="DD->AA: Abolishes BMP1-mediated cleavage of
FT ectodomain release of olfactomedin-like domain."
FT /evidence="ECO:0000269|PubMed:17293346"
FT CONFLICT 451
FT /note="E -> G (in Ref. 2; AAO49510)"
FT /evidence="ECO:0000305"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 308..312
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 325..327
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 332..348
FT /evidence="ECO:0007829|PDB:4XAV"
FT HELIX 349..353
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 358..369
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 375..382
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 385..392
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 399..402
FT /evidence="ECO:0007829|PDB:4XAV"
FT HELIX 416..418
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 423..427
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 430..437
FT /evidence="ECO:0007829|PDB:4XAV"
FT TURN 438..440
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 443..450
FT /evidence="ECO:0007829|PDB:4XAV"
FT TURN 451..454
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 455..465
FT /evidence="ECO:0007829|PDB:4XAV"
FT HELIX 466..468
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 486..494
FT /evidence="ECO:0007829|PDB:4XAV"
FT TURN 495..498
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 499..501
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 514..520
FT /evidence="ECO:0007829|PDB:4XAV"
FT TURN 521..524
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 525..530
FT /evidence="ECO:0007829|PDB:4XAV"
FT STRAND 533..541
FT /evidence="ECO:0007829|PDB:4XAV"
SQ SEQUENCE 549 AA; 59137 MW; 43F1B89FF9634F1D CRC64;
MTRAAERGQG ATGWGLRGAL VAIALLSALN AAGTVFVLCQ WRGLSAALRA LEAQRGREQR
EDSALRAFLA ELSRAPGRVP EPSQDPMSAA RNKRSHNGEP ASHIRAESQD MMMMMTYSMV
PIRVMIDLCN STQGICLTGP PGPPGPPGAG GLPGHNGSDG QPGLQGPKGE KGAIGKRGKM
GLPGATGNPG EKGEKGDAGE LGLPGNEGPP GQKGDKGDKG DVSNDVLLTG AKGDQGPPGP
PGPPGPPGPP GSRRSKGPRP PNVFNSQCPG ETCVIPNDDT LVGRADEKAN ERHSPQTESM
ITSIGNPAQV LKVRETFGTW MRESANKSDD RIWVTEHFSG IMVKEFKDLP ALLNSSFTLL
HLPHYFHGCG HAVYNNSLYY HKGGSNTIVR FEFGKETPQT LKLENALYFD RKYLFANSKT
YFNIAVDEKG IWIIYASSVD GSSILVAQLD ERTFSVTQHI NTTYPKSKAG NAFIARGILY
VTDTKDTRVT FAFDLLGGKQ INANFDFRMS QSVLAMLSYN MRDQHLYSWE DGHLMLYPVQ
FLSAASSQR
