ID   CADH4_HUMAN             Reviewed;         916 AA.
AC   P55283; B3KWB8; G3V1P8; Q2M208; Q5VZ44; Q9BZ05;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 2.
DT   02-SEP-2026, entry version 197.
DE   RecName: Full=Cadherin-4;
DE   AltName: Full=Retinal cadherin;
DE            Short=R-CAD;
DE            Short=R-cadherin;
DE   Flags: Precursor;
GN   Name=CDH4;
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), AND VARIANT ARG-625.
RC   TISSUE=Brain;
RX   PubMed=7982033; DOI=10.3109/15419069409014199;
RA   Tanihara H., Sano K., Heimark R.L., St John T., Suzuki S.;
RT   "Cloning of five human cadherins clarifies characteristic features of
RT   cadherin extracellular domain and provides further evidence for two
RT   structurally different types of cadherin.";
RL   Cell Adhes. Commun. 2:15-26(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Brain;
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=11780052; DOI=10.1038/414865a;
RA   Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA   Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA   Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA   Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA   Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA   Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA   Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA   Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA   Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA   Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA   Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA   Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA   Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA   Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA   Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA   Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA   Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA   Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA   Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA   Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA   Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA   Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 20.";
RL   Nature 414:865-871(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton 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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   TISSUE=Brain cortex;
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 393-916 (ISOFORM 1), AND VARIANT ARG-625.
RC   TISSUE=Fetal brain;
RX   PubMed=2059658; DOI=10.1091/mbc.2.4.261;
RA   Suzuki S., Sano K., Tanihara H.;
RT   "Diversity of the cadherin family: evidence for eight new cadherins in
RT   nervous tissue.";
RL   Cell Regul. 2:261-270(1991).
CC   -!- FUNCTION: Cadherins are calcium-dependent cell adhesion proteins. They
CC       preferentially interact with themselves in a homophilic manner in
CC       connecting cells; cadherins may thus contribute to the sorting of
CC       heterogeneous cell types. May play an important role in retinal
CC       development.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC       protein.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=P55283-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=P55283-2; Sequence=VSP_045548;
CC   -!- TISSUE SPECIFICITY: Expressed mainly in brain but also found in other
CC       tissues.
CC   -!- DOMAIN: Three calcium ions are usually bound at the interface of each
CC       cadherin domain and rigidify the connections, imparting a strong
CC       curvature to the full-length ectodomain. {ECO:0000250}.
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DR   EMBL; L34059; AAA35627.1; -; mRNA.
DR   EMBL; AK124724; BAG54080.1; -; mRNA.
DR   EMBL; AL365401; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL162457; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL109911; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL365229; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL079336; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL160412; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL391316; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL450463; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX640515; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471077; EAW75409.1; -; Genomic_DNA.
DR   EMBL; BC101651; AAI01652.1; -; mRNA.
DR   EMBL; BC112150; AAI12151.1; -; mRNA.
DR   CCDS; CCDS13488.1; -. [P55283-1]
DR   CCDS; CCDS58784.1; -. [P55283-2]
DR   PIR; C38992; C38992.
DR   RefSeq; NP_001239268.1; NM_001252339.3. [P55283-2]
DR   RefSeq; NP_001785.2; NM_001794.5. [P55283-1]
DR   RefSeq; XP_047295768.1; XM_047439812.1. [P55283-2]
DR   RefSeq; XP_047295769.1; XM_047439813.1. [P55283-2]
DR   RefSeq; XP_054178787.1; XM_054322812.1. [P55283-2]
DR   RefSeq; XP_054178788.1; XM_054322813.1. [P55283-2]
DR   AlphaFoldDB; P55283; -.
DR   SMR; P55283; -.
DR   BioGRID; 107437; 12.
DR   FunCoup; P55283; 228.
DR   IntAct; P55283; 10.
DR   MINT; P55283; -.
DR   NDEx; IQUERY-CP-CDH4; 5 NDEx IQuery Curated Pathways.
DR   STRING; 9606.ENSP00000484928; -.
DR   GlyCosmos; P55283; 6 sites, No reported glycans.
DR   GlyGen; P55283; 10 sites, 2 O-linked glycans (4 sites).
DR   iPTMnet; P55283; -.
DR   PhosphoSitePlus; P55283; -.
DR   BioMuta; CDH4; -.
DR   DMDM; 81175161; -.
DR   jPOST; P55283; -.
DR   MassIVE; P55283; -.
DR   PaxDb; 9606-ENSP00000484928; -.
DR   PeptideAtlas; P55283; -.
DR   ProteomicsDB; 32401; -.
DR   ProteomicsDB; 56833; -. [P55283-1]
DR   Antibodypedia; 2666; 345 antibodies from 34 providers.
DR   DNASU; 1002; -.
DR   Ensembl; ENST00000543233.2; ENSP00000443301.1; ENSG00000179242.16. [P55283-2]
DR   Ensembl; ENST00000614565.5; ENSP00000484928.1; ENSG00000179242.16. [P55283-1]
DR   GeneID; 1002; -.
DR   KEGG; hsa:1002; -.
DR   MANE-Select; ENST00000614565.5; ENSP00000484928.1; NM_001794.5; NP_001785.2.
DR   UCSC; uc032pok.1; human. [P55283-1]
DR   AGR; HGNC:1763; -.
DR   ClinPGx; PA26300; -.
DR   CTD; 1002; -.
DR   DisGeNET; 1002; -.
DR   GeneCards; CDH4; -.
DR   HGNC; HGNC:1763; CDH4.
DR   HPA; ENSG00000179242; Group enriched (brain, lymphoid tissue, ovary, skeletal muscle).
DR   MalaCards; CDH4; -.
DR   MIM; 603006; gene.
DR   OpenTargets; ENSG00000179242; -.
DR   VEuPathDB; HostDB:ENSG00000179242; -.
DR   eggNOG; KOG3594; Eukaryota.
DR   GeneTree; ENSGT00940000158073; -.
DR   InParanoid; P55283; -.
DR   OMA; QICERPG; -.
DR   OrthoDB; 6079678at2759; -.
DR   PAN-GO; P55283; 10 GO annotations based on evolutionary models.
DR   PhylomeDB; P55283; -.
DR   PathwayCommons; P55283; -.
DR   Reactome; R-HSA-418990; Adherens junctions interactions.
DR   Reactome; R-HSA-525793; Myogenesis.
DR   SignaLink; P55283; -.
DR   SIGNOR; P55283; -.
DR   Agora; ENSG00000179242; -.
DR   BioGRID-ORCS; 1002; 11 hits in 1149 CRISPR screens.
DR   CD-CODE; FB4E32DD; Presynaptic clusters and postsynaptic densities.
DR   ChiTaRS; CDH4; human.
DR   GeneWiki; CDH4; -.
DR   GenomeRNAi; 1002; -.
DR   Pharos; P55283; Tbio.
DR   PRO; PR:P55283; -.
DR   Proteomes; UP000005640; Chromosome 20.
DR   RNAct; P55283; protein.
DR   Bgee; ENSG00000179242; Expressed in ventricular zone and 90 other cell types or tissues.
DR   ExpressionAtlas; P55283; baseline and differential.
DR   GO; GO:0005912; C:adherens junction; IBA:GO_Central.
DR   GO; GO:0016342; C:catenin complex; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR   GO; GO:0008013; F:beta-catenin binding; IBA:GO_Central.
DR   GO; GO:0045296; F:cadherin binding; IBA:GO_Central.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0034332; P:adherens junction organization; IBA:GO_Central.
DR   GO; GO:0016339; P:calcium-dependent cell-cell adhesion; IBA:GO_Central.
DR   GO; GO:0007155; P:cell adhesion; TAS:ProtInc.
DR   GO; GO:0016477; P:cell migration; IBA:GO_Central.
DR   GO; GO:0000902; P:cell morphogenesis; IBA:GO_Central.
DR   GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IBA:GO_Central.
DR   GO; GO:0007043; P:cell-cell junction assembly; IBA:GO_Central.
DR   GO; GO:0007156; P:homophilic cell-cell adhesion; IEA:InterPro.
DR   CDD; cd11304; Cadherin_repeat; 3.
DR   FunFam; 2.60.40.60:FF:000011; Cadherin 1; 1.
DR   FunFam; 2.60.40.60:FF:000022; Cadherin 2; 1.
DR   FunFam; 2.60.40.60:FF:000027; Cadherin 2; 1.
DR   FunFam; 2.60.40.60:FF:000045; Cadherin 2; 1.
DR   FunFam; 4.10.900.10:FF:000001; Cadherin 2; 1.
DR   FunFam; 2.60.40.60:FF:000615; Cadherin-2; 1.
DR   FunFam; 2.60.40.60:FF:000287; Cadherin-4; 1.
DR   Gene3D; 2.60.40.60; Cadherins; 6.
DR   Gene3D; 4.10.900.10; TCF3-CBD (Catenin binding domain); 1.
DR   InterPro; IPR039808; Cadherin.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR014868; Cadherin_pro_dom.
DR   InterPro; IPR000233; Cadherin_Y-type_LIR.
DR   InterPro; IPR027397; Catenin-bd_sf.
DR   PANTHER; PTHR24027; CADHERIN-23; 1.
DR   PANTHER; PTHR24027:SF81; CADHERIN-4; 1.
DR   Pfam; PF01049; CADH_Y-type_LIR; 1.
DR   Pfam; PF00028; Cadherin; 4.
DR   Pfam; PF08758; Cadherin_pro; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   PRINTS; PR01820; DESMOCOLLIN.
DR   SMART; SM00112; CA; 5.
DR   SMART; SM01055; Cadherin_pro; 1.
DR   SUPFAM; SSF49313; Cadherin-like; 6.
DR   PROSITE; PS00232; CADHERIN_1; 3.
DR   PROSITE; PS50268; CADHERIN_2; 5.
PE   1: Evidence at protein level;
KW   Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW   Cleavage on pair of basic residues; Glycoprotein; Membrane; Metal-binding;
KW   Proteomics identification; Reference proteome; Repeat; Signal;
KW   Transmembrane; Transmembrane helix.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   PROPEP          21..169
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000003749"
FT   CHAIN           170..916
FT                   /note="Cadherin-4"
FT                   /id="PRO_0000003750"
FT   TOPO_DOM        170..734
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        735..756
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        757..916
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          170..277
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          278..392
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          393..507
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          508..613
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          614..724
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          124..168
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          806..838
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        129..138
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CARBOHYD        283
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        412
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        557
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        632
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        661
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        702
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   VAR_SEQ         1..74
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_045548"
FT   VARIANT         141
FT                   /note="A -> V (in dbSNP:rs34937312)"
FT                   /id="VAR_048504"
FT   VARIANT         625
FT                   /note="K -> R (in dbSNP:rs6142884)"
FT                   /evidence="ECO:0000269|PubMed:2059658,
FT                   ECO:0000269|PubMed:7982033"
FT                   /id="VAR_033699"
FT   CONFLICT        88
FT                   /note="T -> A (in Ref. 2; BAG54080)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        223
FT                   /note="D -> N (in Ref. 1; AAA35627)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        274
FT                   /note="R -> H (in Ref. 1; AAA35627)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        284
FT                   /note="G -> C (in Ref. 1; AAA35627)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        299
FT                   /note="V -> I (in Ref. 1; AAA35627)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        347
FT                   /note="L -> W (in Ref. 1; AAA35627)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        390
FT                   /note="P -> S (in Ref. 1; AAA35627)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        405
FT                   /note="R -> S (in Ref. 1; AAA35627 and 6; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        502
FT                   /note="N -> S (in Ref. 2; BAG54080)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        540
FT                   /note="Q -> R (in Ref. 2; BAG54080)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        566
FT                   /note="A -> V (in Ref. 1; AAA35627 and 6; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        641
FT                   /note="D -> H (in Ref. 1; AAA35627 and 6; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        778..779
FT                   /note="DN -> EK (in Ref. 1; AAA35627 and 6; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        826
FT                   /note="A -> P (in Ref. 1; AAA35627 and 6; no nucleotide
FT                   entry)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   916 AA;  100281 MW;  E4512F94E58046D7 CRC64;
     MTAGAGVLLL LLSLSGALRA HNEDLTTRET CKAGFSEDDY TALISQNILE GEKLLQVKFS
     SCVGTKGTQY ETNSMDFKVG ADGTVFATRE LQVPSEQVAF TVTAWDSQTA EKWDAVVRLL
     VAQTSSPHSG HKPQKGKKVV ALDPSPPPKD TLLPWPQHQN ANGLRRRKRD WVIPPINVPE
     NSRGPFPQQL VRIRSDKDND IPIRYSITGV GADQPPMEVF SIDSMSGRMY VTRPMDREEH
     ASYHLRAHAV DMNGNKVENP IDLYIYVIDM NDNRPEFINQ VYNGSVDEGS KPGTYVMTVT
     ANDADDSTTA NGMVRYRIVT QTPQSPSQNM FTINSETGDI VTVAAGLDRE KVQQYTVIVQ
     ATDMEGNLNY GLSNTATAII TVTDVNDNPP EFTASTFAGE VPENRVETVV ANLTVMDRDQ
     PHSPNWNAVY RIISGDPSGH FSVRTDPVTN EGMVTVVKAV DYELNRAFML TVMVSNQAPL
     ASGIQMSFQS TAGVTISIMD INEAPYFPSN HKLIRLEEGV PPGTVLTTFS AVDPDRFMQQ
     AVRYSKLSDP ASWLHINATN GQITTAAVLD RESLYTKNNV YEATFLAADN GIPPASGTGT
     LQIYLIDIND NAPELLPKEA QICEKPNLNA INITAADADV DPNIGPYVFE LPFVPAAVRK
     NWTITRLNGD YAQLSLRILY LEAGMYDVPI IVTDSGNPPL SNTSIIKVKV CPCDDNGDCT
     TIGAVAAAGL GTGAIVAILI CILILLTMVL LFVMWMKRRE KERHTKQLLI DPEDDVRDNI
     LKYDEEGGGE EDQDYDLSQL QQPEAMGHVP SKAPGVRRVD ERPVGAEPQY PIRPMVPHPG
     DIGDFINEGL RAADNDPTAP PYDSLLVFDY EGSGSTAGSV SSLNSSSSGD QDYDYLNDWG
     PRFKKLADMY GGGEED
//