ID   CSTN2_HUMAN             Reviewed;         955 AA.
AC   Q9H4D0; B2RCW5; D3DNF4; Q3SX54; Q3ZB76; Q5UE56; Q96HZ2; Q9BSS0;
DT   19-SEP-2002, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 2.
DT   03-MAY-2023, entry version 174.
DE   RecName: Full=Calsyntenin-2 {ECO:0000303|PubMed:12498782};
DE   AltName: Full=Alcadein-gamma {ECO:0000303|PubMed:12972431};
DE            Short=Alc-gamma {ECO:0000303|PubMed:12972431};
DE   Flags: Precursor;
GN   Name=CLSTN2 {ECO:0000312|HGNC:HGNC:17448}; Synonyms=CS2;
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], TISSUE SPECIFICITY, AND VARIANT ILE-366.
RC   TISSUE=Fetal brain;
RX   PubMed=12498782; DOI=10.1006/mcne.2002.1181;
RA   Hintsch G., Zurlinden A., Meskenaite V., Steuble M., Fink-Widmer K.,
RA   Kinter J., Sonderegger P.;
RT   "The calsyntenins - a family of postsynaptic membrane proteins with
RT   distinct neuronal expression patterns.";
RL   Mol. Cell. Neurosci. 21:393-409(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT ILE-366.
RX   PubMed=12972431; DOI=10.1074/jbc.m306024200;
RA   Araki Y., Tomita S., Yamaguchi H., Miyagi N., Sumioka A., Kirino Y.,
RA   Suzuki T.;
RT   "Novel cadherin-related membrane proteins, Alcadeins, enhance the X11-like
RT   protein-mediated stabilization of amyloid beta-protein precursor
RT   metabolism.";
RL   J. Biol. Chem. 278:49448-49458(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Uterus;
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   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16641997; DOI=10.1038/nature04728;
RA   Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J.,
RA   Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P.,
RA   Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A.,
RA   Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L.,
RA   Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G.,
RA   Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W.,
RA   Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M.,
RA   Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P.,
RA   Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H.,
RA   Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J.,
RA   Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W.,
RA   Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B.,
RA   Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O.,
RA   Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B.,
RA   Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H.,
RA   Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J.,
RA   Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X.,
RA   Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R.,
RA   Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.;
RT   "The DNA sequence, annotation and analysis of human chromosome 3.";
RL   Nature 440:1194-1198(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT ILE-366.
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, and Lung;
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   [7]
RP   PROTEOLYTIC CLEAVAGE.
RX   PubMed=15037614; DOI=10.1074/jbc.m401925200;
RA   Araki Y., Miyagi N., Kato N., Yoshida T., Wada S., Nishimura M., Komano H.,
RA   Yamamoto T., De Strooper B., Yamamoto K., Suzuki T.;
RT   "Coordinated metabolism of Alcadein and amyloid beta-protein precursor
RT   regulates FE65-dependent gene transactivation.";
RL   J. Biol. Chem. 279:24343-24354(2004).
RN   [8]
RP   VARIANTS [LARGE SCALE ANALYSIS] ILE-193 AND GLN-765.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Postsynaptic adhesion molecule that binds to presynaptic
CC       neurexins to mediate synapse formation, and which is involved in
CC       learning and memory (By similarity). Promotes synapse development by
CC       acting as a cell adhesion molecule at the postsynaptic membrane, which
CC       associates with neurexin-alpha at the presynaptic membrane (By
CC       similarity). {ECO:0000250|UniProtKB:Q99JH7,
CC       ECO:0000250|UniProtKB:Q9ER65}.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic cell membrane
CC       {ECO:0000250|UniProtKB:Q9ER65}; Single-pass type I membrane protein
CC       {ECO:0000255}. Endoplasmic reticulum membrane
CC       {ECO:0000250|UniProtKB:Q9ER65}; Single-pass type I membrane protein
CC       {ECO:0000255}. Golgi apparatus membrane {ECO:0000250|UniProtKB:Q9ER65};
CC       Single-pass type I membrane protein {ECO:0000255}. Cell projection,
CC       dendrite {ECO:0000250|UniProtKB:Q9ER65}. Note=Most prominent in the
CC       postsynaptic specializations of asymmetric (type I) synapses with both
CC       axodendritic and axospinous localization.
CC       {ECO:0000250|UniProtKB:Q9ER65}.
CC   -!- TISSUE SPECIFICITY: Restricted to the brain.
CC       {ECO:0000269|PubMed:12498782}.
CC   -!- DOMAIN: Binds synaptic Ca(2+) with its cytoplasmic domain.
CC       {ECO:0000250|UniProtKB:Q9EPL2}.
CC   -!- PTM: Proteolytically processed under normal cellular conditions
CC       (PubMed:15037614). A primary zeta-cleavage generates a large
CC       extracellular (soluble) N-terminal domain (sAlc) and a short C-terminal
CC       transmembrane fragment (CTF1) (PubMed:15037614). A secondary cleavage
CC       catalyzed by gamma-secretase within the transmembrane domain releases
CC       the beta-Alc-gamma chain in the extracellular milieu and produces an
CC       intracellular fragment (AlcICD) (PubMed:15037614). This processing is
CC       strongly suppressed in the tripartite complex formed with APBA2 and
CC       APP, which seems to prevent the association with PSEN1
CC       (PubMed:15037614). {ECO:0000269|PubMed:15037614}.
CC   -!- SIMILARITY: Belongs to the calsyntenin family. {ECO:0000305}.
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DR   EMBL; AJ278018; CAC14924.1; -; mRNA.
DR   EMBL; AY753303; AAV30553.1; -; mRNA.
DR   EMBL; AK315308; BAG37712.1; -; mRNA.
DR   EMBL; AC010181; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC048346; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092988; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC108744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117396; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC117449; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471052; EAW79018.1; -; Genomic_DNA.
DR   EMBL; BC004871; AAH04871.2; -; mRNA.
DR   EMBL; BC007943; AAH07943.2; -; mRNA.
DR   EMBL; BC103496; AAI03497.1; -; mRNA.
DR   EMBL; BC103506; AAI03507.1; -; mRNA.
DR   EMBL; BC104485; AAI04486.1; -; mRNA.
DR   CCDS; CCDS3112.1; -.
DR   RefSeq; NP_071414.2; NM_022131.2.
DR   AlphaFoldDB; Q9H4D0; -.
DR   SMR; Q9H4D0; -.
DR   BioGRID; 122049; 21.
DR   STRING; 9606.ENSP00000402460; -.
DR   GlyConnect; 1061; 3 N-Linked glycans (2 sites).
DR   GlyCosmos; Q9H4D0; 6 sites, 2 glycans.
DR   GlyGen; Q9H4D0; 6 sites, 2 N-linked glycans (2 sites).
DR   iPTMnet; Q9H4D0; -.
DR   PhosphoSitePlus; Q9H4D0; -.
DR   BioMuta; CLSTN2; -.
DR   DMDM; 296434469; -.
DR   jPOST; Q9H4D0; -.
DR   MassIVE; Q9H4D0; -.
DR   PaxDb; Q9H4D0; -.
DR   PeptideAtlas; Q9H4D0; -.
DR   ProteomicsDB; 80823; -.
DR   Antibodypedia; 33471; 137 antibodies from 21 providers.
DR   DNASU; 64084; -.
DR   Ensembl; ENST00000458420.7; ENSP00000402460.2; ENSG00000158258.16.
DR   GeneID; 64084; -.
DR   KEGG; hsa:64084; -.
DR   MANE-Select; ENST00000458420.7; ENSP00000402460.2; NM_022131.3; NP_071414.2.
DR   UCSC; uc003etn.4; human.
DR   AGR; HGNC:17448; -.
DR   CTD; 64084; -.
DR   DisGeNET; 64084; -.
DR   GeneCards; CLSTN2; -.
DR   HGNC; HGNC:17448; CLSTN2.
DR   HPA; ENSG00000158258; Group enriched (adipose tissue, brain, ovary).
DR   MIM; 611323; gene.
DR   neXtProt; NX_Q9H4D0; -.
DR   OpenTargets; ENSG00000158258; -.
DR   PharmGKB; PA38239; -.
DR   VEuPathDB; HostDB:ENSG00000158258; -.
DR   eggNOG; KOG1834; Eukaryota.
DR   GeneTree; ENSGT00950000183086; -.
DR   HOGENOM; CLU_008904_0_0_1; -.
DR   InParanoid; Q9H4D0; -.
DR   OMA; AKRIEYQ; -.
DR   OrthoDB; 3615717at2759; -.
DR   PhylomeDB; Q9H4D0; -.
DR   TreeFam; TF315946; -.
DR   PathwayCommons; Q9H4D0; -.
DR   BioGRID-ORCS; 64084; 9 hits in 1149 CRISPR screens.
DR   ChiTaRS; CLSTN2; human.
DR   GenomeRNAi; 64084; -.
DR   Pharos; Q9H4D0; Tbio.
DR   PRO; PR:Q9H4D0; -.
DR   Proteomes; UP000005640; Chromosome 3.
DR   RNAct; Q9H4D0; protein.
DR   Bgee; ENSG00000158258; Expressed in endothelial cell and 150 other tissues.
DR   Genevisible; Q9H4D0; HS.
DR   GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR   GO; GO:0030425; C:dendrite; IEA:UniProtKB-SubCell.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098839; C:postsynaptic density membrane; IEA:Ensembl.
DR   GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
DR   GO; GO:0001540; F:amyloid-beta binding; IEA:InterPro.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0019894; F:kinesin binding; IEA:InterPro.
DR   GO; GO:0042988; F:X11-like protein binding; IEA:InterPro.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0051965; P:positive regulation of synapse assembly; IBA:GO_Central.
DR   GO; GO:0050806; P:positive regulation of synaptic transmission; IBA:GO_Central.
DR   CDD; cd11304; Cadherin_repeat; 2.
DR   Gene3D; 2.60.120.200; -; 1.
DR   Gene3D; 2.60.40.60; Cadherins; 2.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR026914; Calsyntenin.
DR   InterPro; IPR045588; CLSTN_C.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   PANTHER; PTHR14139; CALSYNTENIN; 1.
DR   PANTHER; PTHR14139:SF3; CALSYNTENIN-2; 1.
DR   Pfam; PF00028; Cadherin; 1.
DR   Pfam; PF19699; CLSTN_C; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 2.
DR   SUPFAM; SSF49313; Cadherin-like; 2.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS50268; CADHERIN_2; 2.
PE   1: Evidence at protein level;
KW   Calcium; Cell adhesion; Cell membrane; Cell projection;
KW   Endoplasmic reticulum; Glycoprotein; Golgi apparatus; Membrane;
KW   Postsynaptic cell membrane; Reference proteome; Repeat; Signal; Synapse;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..955
FT                   /note="Calsyntenin-2"
FT                   /id="PRO_0000004023"
FT   TOPO_DOM        21..831
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        832..852
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        853..955
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          44..160
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          161..280
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          887..955
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        899..928
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        56
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        98
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        342
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        374
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        716
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        729
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VARIANT         193
FT                   /note="S -> I (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036112"
FT   VARIANT         331
FT                   /note="I -> T (in dbSNP:rs17348572)"
FT                   /id="VAR_055615"
FT   VARIANT         366
FT                   /note="V -> I (in dbSNP:rs7632885)"
FT                   /evidence="ECO:0000269|PubMed:12498782,
FT                   ECO:0000269|PubMed:12972431, ECO:0000269|Ref.5"
FT                   /id="VAR_039557"
FT   VARIANT         765
FT                   /note="R -> Q (in a colorectal cancer sample; somatic
FT                   mutation; dbSNP:rs766718816)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036113"
FT   CONFLICT        847
FT                   /note="V -> D (in Ref. 6; AAI03507)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        946
FT                   /note="L -> P (in Ref. 6; AAI03507)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   955 AA;  107006 MW;  6059F3277F152E75 CRC64;
     MLPGRLCWVP LLLALGVGSG SGGGGDSRQR RLLAAKVNKH KPWIETSYHG VITENNDTVI
     LDPPLVALDK DAPVPFAGEI CAFKIHGQEL PFEAVVLNKT SGEGRLRAKS PIDCELQKEY
     TFIIQAYDCG AGPHETAWKK SHKAVVHIQV KDVNEFAPTF KEPAYKAVVT EGKIYDSILQ
     VEAIDEDCSP QYSQICNYEI VTTDVPFAID RNGNIRNTEK LSYDKQHQYE ILVTAYDCGQ
     KPAAQDTLVQ VDVKPVCKPG WQDWTKRIEY QPGSGSMPLF PSIHLETCDG AVSSLQIVTE
     LQTNYIGKGC DRETYSEKSL QKLCGASSGI IDLLPSPSAA TNWTAGLLVD SSEMIFKFDG
     RQGAKVPDGI VPKNLTDQFT ITMWMKHGPS PGVRAEKETI LCNSDKTEMN RHHYALYVHN
     CRLVFLLRKD FDQADTFRPA EFHWKLDQIC DKEWHYYVIN VEFPVVTLYM DGATYEPYLV
     TNDWPIHPSH IAMQLTVGAC WQGGEVTKPQ FAQFFHGSLA SLTIRPGKME SQKVISCLQA
     CKEGLDINSL ESLGQGIKYH FNPSQSILVM EGDDIGNINR ALQKVSYINS RQFPTAGVRR
     LKVSSKVQCF GEDVCISIPE VDAYVMVLQA IEPRITLRGT DHFWRPAAQF ESARGVTLFP
     DIKIVSTFAK TEAPGDVKTT DPKSEVLEEM LHNLDFCDIL VIGGDLDPRQ ECLELNHSEL
     HQRHLDATNS TAGYSIYGVG SMSRYEQVLH HIRYRNWRPA SLEARRFRIK CSELNGRYTS
     NEFNLEVSIL HEDQVSDKEH VNHLIVQPPF LQSVHHPESR SSIQHSSVVP SIATVVIIIS
     VCMLVFVVAM GVYRVRIAHQ HFIQETEAAK ESEMDWDDSA LTITVNPMEK HEGPGHGEDE
     TEGEEEEEAE EEMSSSSGSD DSEEEEEEEG MGRGRHGQNG ARQAQLEWDD STLPY
//