THS7A_MOUSE
ID THS7A_MOUSE Reviewed; 1645 AA.
AC Q69ZU6; Q3TP01; Q3UWV1;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 2.
DT 25-MAY-2022, entry version 111.
DE RecName: Full=Thrombospondin type-1 domain-containing protein 7A;
DE Contains:
DE RecName: Full=Thrombospondin type-1 domain-containing protein 7A, soluble form;
DE Flags: Precursor;
GN Name=Thsd7a; Synonyms=Gm837, Kiaa0960;
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 TISSUE=Brain;
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 258-610 AND 1603-1645.
RC STRAIN=C57BL/6J; TISSUE=Egg, and Head;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Kidney;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=27214550; DOI=10.1172/jci85265;
RA Tomas N.M., Hoxha E., Reinicke A.T., Fester L., Helmchen U., Gerth J.,
RA Bachmann F., Budde K., Koch-Nolte F., Zahner G., Rune G., Lambeau G.,
RA Meyer-Schwesinger C., Stahl R.A.;
RT "Autoantibodies against thrombospondin type 1 domain-containing 7A induce
RT membranous nephropathy.";
RL J. Clin. Invest. 126:2519-2532(2016).
CC -!- FUNCTION: [Thrombospondin type-1 domain-containing protein 7A]: Plays a
CC role in actin cytoskeleton rearrangement.
CC {ECO:0000269|PubMed:27214550}.
CC -!- FUNCTION: [Thrombospondin type-1 domain-containing protein 7A, soluble
CC form]: The soluble form promotes endothelial cell migration and
CC filopodia formation during sprouting angiogenesis via a FAK-dependent
CC mechanism. {ECO:0000250|UniProtKB:Q9UPZ6}.
CC -!- SUBCELLULAR LOCATION: [Thrombospondin type-1 domain-containing protein
CC 7A]: Cell membrane {ECO:0000269|PubMed:27214550}; Single-pass type I
CC membrane protein {ECO:0000305|PubMed:27214550}. Cell projection
CC {ECO:0000269|PubMed:27214550}. Note=Detected on podocyte foot
CC processes. {ECO:0000269|PubMed:27214550}.
CC -!- SUBCELLULAR LOCATION: [Thrombospondin type-1 domain-containing protein
CC 7A, soluble form]: Secreted {ECO:0000250|UniProtKB:Q9UPZ6}.
CC Note=Proteolytic cleavage in the extracellular region generates a 210
CC kDa soluble form. {ECO:0000250|UniProtKB:Q9UPZ6}.
CC -!- TISSUE SPECIFICITY: Detected on kidney podocytes along the glomerular
CC capillary wall (at protein level). {ECO:0000269|PubMed:27214550}.
CC -!- DOMAIN: Sequence analysis combined with the expression of constructs
CC corresponding each to two or three adjacent TSP type-1 domains suggests
CC the presence of 21 TSP type-1 domains; not all of these are detected by
CC standard bioinformatic tools. {ECO:0000250|UniProtKB:Q9UPZ6}.
CC -!- PTM: Proteolytic cleavage in the extracellular region generates a 210
CC kDa soluble form. {ECO:0000250|UniProtKB:Q9UPZ6}.
CC -!- PTM: Extensively N-glycosylated. {ECO:0000250|UniProtKB:Q9UPZ6}.
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; AK173072; BAD32350.1; -; Transcribed_RNA.
DR EMBL; AK136087; BAE22813.1; -; mRNA.
DR EMBL; AK164834; BAE37936.1; -; mRNA.
DR RefSeq; NP_001158277.1; NM_001164805.1.
DR AlphaFoldDB; Q69ZU6; -.
DR BioGRID; 236931; 2.
DR IntAct; Q69ZU6; 3.
DR MINT; Q69ZU6; -.
DR STRING; 10090.ENSMUSP00000040176; -.
DR GlyConnect; 2767; 10 N-Linked glycans (4 sites).
DR GlyGen; Q69ZU6; 13 sites, 10 N-linked glycans (4 sites).
DR iPTMnet; Q69ZU6; -.
DR PhosphoSitePlus; Q69ZU6; -.
DR MaxQB; Q69ZU6; -.
DR PaxDb; Q69ZU6; -.
DR PRIDE; Q69ZU6; -.
DR ProteomicsDB; 259386; -.
DR DNASU; 330267; -.
DR GeneID; 330267; -.
DR KEGG; mmu:330267; -.
DR CTD; 221981; -.
DR MGI; MGI:2685683; Thsd7a.
DR eggNOG; KOG3538; Eukaryota.
DR InParanoid; Q69ZU6; -.
DR OrthoDB; 20284at2759; -.
DR PhylomeDB; Q69ZU6; -.
DR Reactome; R-MMU-5173214; O-glycosylation of TSR domain-containing proteins.
DR BioGRID-ORCS; 330267; 1 hit in 70 CRISPR screens.
DR ChiTaRS; Thsd7a; mouse.
DR PRO; PR:Q69ZU6; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q69ZU6; protein.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0098846; C:podocyte foot; IDA:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; IMP:UniProtKB.
DR GO; GO:0001525; P:angiogenesis; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR Gene3D; 2.20.100.10; -; 11.
DR InterPro; IPR000884; TSP1_rpt.
DR InterPro; IPR036383; TSP1_rpt_sf.
DR InterPro; IPR044004; TSP1_spondin_dom.
DR Pfam; PF19028; TSP1_spondin; 5.
DR Pfam; PF00090; TSP_1; 3.
DR SMART; SM00209; TSP1; 16.
DR SUPFAM; SSF82895; SSF82895; 10.
DR PROSITE; PS50092; TSP1; 11.
PE 1: Evidence at protein level;
KW Angiogenesis; Cell membrane; Cell projection; Coiled coil; Differentiation;
KW Disulfide bond; Glycoprotein; Membrane; Reference proteome; Repeat;
KW Secreted; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..38
FT /evidence="ECO:0000255"
FT CHAIN 39..1645
FT /note="Thrombospondin type-1 domain-containing protein 7A"
FT /id="PRO_0000256127"
FT CHAIN 39..?
FT /note="Thrombospondin type-1 domain-containing protein 7A,
FT soluble form"
FT /id="PRO_0000444431"
FT TOPO_DOM 39..1595
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 1596..1616
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 1617..1645
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 46..105
FT /note="TSP type-1 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 109..181
FT /note="TSP type-1 2"
FT /evidence="ECO:0000255"
FT DOMAIN 183..236
FT /note="TSP type-1 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 349..405
FT /note="TSP type-1 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 412..499
FT /note="TSP type-1 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 501..563
FT /note="TSP type-1 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 623..684
FT /note="TSP type-1 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 685..758
FT /note="TSP type-1 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 760..820
FT /note="TSP type-1 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 821..893
FT /note="TSP type-1 10"
FT /evidence="ECO:0000255"
FT DOMAIN 895..948
FT /note="TSP type-1 11"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 949..1022
FT /note="TSP type-1 12"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1024..1084
FT /note="TSP type-1 13"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1085..1152
FT /note="TSP type-1 14"
FT /evidence="ECO:0000255"
FT DOMAIN 1154..1208
FT /note="TSP type-1 15"
FT /evidence="ECO:0000255"
FT DOMAIN 1209..1272
FT /note="TSP type-1 16"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1274..1329
FT /note="TSP type-1 17"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1330..1400
FT /note="TSP type-1 18"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DOMAIN 1402..1463
FT /note="TSP type-1 19"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT REGION 255..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 256..304
FT /evidence="ECO:0000255"
FT COMPBIAS 266..291
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 223
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 321
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 439
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 489
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 668
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 706
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 957
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1032
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1213
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1264
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1354
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1488
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1535
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 424..494
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 444..498
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 455..483
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 624..666
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 635..639
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 678..683
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 696..753
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 717..757
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 728..741
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 761..803
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 772..776
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 813..819
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 961..1017
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 983..1021
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 994..1007
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1025..1062
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1036..1040
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1079..1083
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1201..1207
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1220..1267
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1228..1271
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1239..1252
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1275..1313
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1286..1290
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1323..1328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1339..1395
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1346..1399
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1357..1376
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1403..1447
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1414..1418
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT DISULFID 1457..1462
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00210"
FT CONFLICT 597..610
FT /note="GEEVDRQLCRDAIF -> ASKIVSSCGSVAAQ (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1645 AA; 183527 MW; 698A3990C39C41EB CRC64;
MGLRAGRLAS PSRGVLQLLR LPLLLLLLLS SGARGAAAQG DTEVPTLYLW KTGPWGRCMG
DDCGPGGIQT RAVWCAHVEG WTTLHTNCKQ AVRPSNQQNC FKVCDWHKEL YDWRLGTWDR
CQPVISKSLE KSRECVKGEE GIQVREIMCI QKDKDIPAED IICEYFEPKP LLEQACLIPC
QKDCIVSEFS PWSECSRTCG SGLQHRTRHV VAPPQYGGSG CPNLTEFQVC QSNPCEEDES
LYSLQVGPWS ACSVPHTRQA RQARRRGKNK EREKERGKAV KDPEARELIK KKRNRNRQNR
QENRYWDIQI GYQTRDVTCL NRTGKSADLS FCQQERLPMT FQSCVITKEC QVSEWLEWSP
CSKTCHDVTS PTGTRVRTRT ITQFPIGSEK ECPALEEKEP CVSQGDGAVL CATYGWRTTE
WTECHVDPLL SQQDKRRANQ TALCGGGVQT REIYCIQTND NMLSHGNTQK DKEASKPVDS
KLCTGPVPNT TQLCHVPCPI ECEVSPWSAW GPCTYENCND QQGKKGFKLR KRRITNEPTG
GSGATGNCPH LLEAIPCEEP SCYDWKSVRL GDCEPDNGKS CGPGTQVQEV VCINSDGEEV
DRQLCRDAIF PIPVACDAPC PKDCVLSAWS SWSSCSHTCS GKTTEGKQTR ARSILAYAGE
EGGIRCPNIS ALQEVRSCNE HPCTVYHWQT GPWGQCIEDT SVSSFNTTTT WNGEASCSVG
MQTRKVICVR VNVGQVGPKK CPESLRPETV RPCLLPCRKD CVVTPYSDWT PCPSSCREGD
SGARKQSRQR VIIQLPANGG KECSDPLYEE KACEAPPTCH SYRWKTHKWR RCQLVPWSIQ
QDVPGAQEGC GPGRQARAIT CRKQDGGQAS IQECLQYAGP VPALTQACQI PCQDDCQFTS
WSKFSSCNGD CGAVRTRKRA IVGKSKKKEK CKNSHLYPLI ETQYCPCDKY NAQPVGNWSD
CILPEGKAEV LLGMKVQGDS KECGQGYRYQ AMACYDQNGR LVETSRCNSH GYIEEACIIP
CPSDCKLSEW SNWSRCSKSC GSGVKVRSKW LREKPYNGGR PCPKLDHVNQ AQVYEVVPCH
SDCNQYIWVT EPWSVCKVTF VDMRDNCGEG VQTRKVRCMQ NTADGPSEHV EDYLCDPEDM
PLGSRECKLP CPEDCVISEW GPWTCALPCN PSGSRQRSAD PIRQPADEGR ACPDAVEKEP
CSLNKNCYHY DYNVTDWSTC QLSEKAVCGN GIKTRMLDCV RSDGKSVDLK YCEELGLEKN
WPMNTSCTVE CPVNCQLSDW SSWSQCSQTC GLTGKMIRKR TVTQPFQGDG RPCPSLMEQS
KPCPVKPCYR WQYGQWSPCQ VQEAQCGEGT RTRNISCVVS DGSAEDFSKV VDEEFCANTE
LIIDGNKQIV LEETCTQPCP GDCYLNDWSS WSLCQLTCVN GEDLGFGGIQ VRSRAVIIQE
LENQHLCPEQ MLETKSCDDG QCYEYKWVAS AWKGSSRTVW CQRSDGINVT GGCLVVSQPD
TDRSCNPPCS QPHSYCSEMK TCRCEEGYTE VMSSNSTLEQ CTLIPVVVIP TVEDKRGDVK
TSRAVHPTQP SINPAGRGRT WFLQPFGPDG RLKTWVYGVA AGAFVLLVFI VSMIYLACKK
PKKPQRRQNN RLKPLTLAYD GDADM
