PCDA4_MOUSE
ID PCDA4_MOUSE Reviewed; 947 AA.
AC O88689; Q3UEX3; Q6PAM9; Q8K487; Q8K489;
DT 27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Protocadherin alpha-4 {ECO:0000305};
DE Short=PCDH-alpha-4 {ECO:0000305};
DE Flags: Precursor;
GN Name=Pcdha4 {ECO:0000312|MGI:MGI:1298406}; Synonyms=Cnr1;
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 [MRNA] (ISOFORM 1), INTERACTION WITH FYN, SUBCELLULAR
RP LOCATION, TOPOLOGY, TISSUE SPECIFICITY, AND REGION.
RC STRAIN=C57BL/6J; TISSUE=Brain;
RX PubMed=9655502; DOI=10.1016/s0896-6273(00)80495-x;
RA Kohmura N., Senzaki K., Hamada S., Kai N., Yasuda R., Watanabe M.,
RA Ishii H., Yasuda M., Mishina M., Yagi T.;
RT "Diversity revealed by a novel family of cadherins expressed in neurons at
RT a synaptic complex.";
RL Neuron 20:1137-1151(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=11230163; DOI=10.1101/gr.167301;
RA Wu Q., Zhang T., Cheng J.-F., Kim Y., Grimwood J., Schmutz J., Dickson M.,
RA Noonan J.P., Zhang M.Q., Myers R.M., Maniatis T.;
RT "Comparative DNA sequence analysis of mouse and human protocadherin gene
RT clusters.";
RL Genome Res. 11:389-404(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J;
RX PubMed=12154121; DOI=10.1101/gad.1004802;
RA Wang X., Su H., Bradley A.;
RT "Molecular mechanisms governing Pcdh-gamma gene expression: evidence for a
RT multiple promoter and cis-alternative splicing model.";
RL Genes Dev. 16:1890-1905(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Brain;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-919 (ISOFORM 1).
RC STRAIN=C57BL/6J; TISSUE=Retina;
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 [6]
RP STRUCTURE BY NMR OF 27-129, AND DISULFIDE BONDS.
RX PubMed=15929006; DOI=10.1007/s10858-005-2450-4;
RA Umitsu M., Morishita H., Murata Y., Udaka K., Akutsu H., Yagi T.,
RA Ikegami T.;
RT "1H, 13C and 15N resonance assignments of the first cadherin domain of
RT cadherin-related neuronal receptor (CNR)/protocadherin alpha.";
RL J. Biomol. NMR 31:365-366(2005).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.43 ANGSTROMS) OF 30-450 OF HOMODIMER IN COMPLEX
RP WITH CALCIUM, FUNCTION, SUBUNIT, TOPOLOGY, DOMAIN, GLYCOSYLATION AT
RP ASN-265; THR-438; SER-440 AND SER-442, AND DISULFIDE BONDS.
RX PubMed=27161523; DOI=10.1016/j.neuron.2016.04.004;
RA Goodman K.M., Rubinstein R., Thu C.A., Bahna F., Mannepalli S., Ahlsen G.,
RA Rittenhouse C., Maniatis T., Honig B., Shapiro L.;
RT "Structural basis of diverse homophilic recognition by clustered alpha- and
RT beta-protocadherins.";
RL Neuron 90:709-723(2016).
CC -!- FUNCTION: Calcium-dependent cell-adhesion protein involved in cells
CC self-recognition and non-self discrimination (Probable). Thereby, it is
CC involved in the establishment and maintenance of specific neuronal
CC connections in the brain (PubMed:27161523).
CC {ECO:0000305|PubMed:27161523}.
CC -!- SUBUNIT: Forms homodimers in trans (molecules expressed by two
CC different cells) (PubMed:27161523). Forms promiscuous heterodimers in
CC cis (at the plasma membrane of the same cell) with other protocadherins
CC (PubMed:27161523). Interacts with FYN (PubMed:9655502).
CC {ECO:0000269|PubMed:27161523, ECO:0000269|PubMed:9655502}.
CC -!- INTERACTION:
CC O88689-1; Q99LI8: Hgs; NbExp=2; IntAct=EBI-15880299, EBI-2119135;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:9655502};
CC Single-pass type I membrane protein {ECO:0000305|PubMed:27161523,
CC ECO:0000305|PubMed:9655502}. Note=Detected in dendrites and synapses.
CC {ECO:0000269|PubMed:9655502}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O88689-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O88689-2; Sequence=VSP_019413, VSP_019415;
CC Name=3;
CC IsoId=O88689-3; Sequence=VSP_019414;
CC -!- TISSUE SPECIFICITY: Detected in brain throughout embryonic development.
CC Detected in adult brain, in particular in cerebellum and forebrain.
CC {ECO:0000269|PubMed:9655502}.
CC -!- DOMAIN: Cadherin 1 to cadherin 4 domains mediate homophilic trans-
CC interaction, the interaction with an identical protocadherin expressed
CC by a neighboring cell (PubMed:27161523). This is an head-to-tail
CC interaction, the cadherin 1 domain interacting with the cadherin 4
CC domain and the cadherin 2 domain interacting the cadherin 3 domain of
CC the other protocadherin (PubMed:27161523). The cadherin 6 domain
CC mediates promiscuous interactions with protocadherins on the same cell
CC membrane (PubMed:27161523). Each cadherin domain binds three calcium
CC ions (PubMed:27161523). {ECO:0000269|PubMed:27161523,
CC ECO:0000312|PDB:5DZW}.
CC -!- MISCELLANEOUS: The protocadherins alpha are expressed from a single
CC gene cluster similarly to immunoglobulin and T-cell receptors. The N-
CC terminal region containing the 6 extracellular cadherin domains, unique
CC to each protocadherin alpha, is encoded by one of the large exons found
CC in tandem array within the gene cluster. The C-terminal region,
CC identical to all protocadherins alpha, is encoded by 3 shared exons.
CC {ECO:0000303|PubMed:11230163}.
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DR EMBL; D86916; BAA29045.1; -; mRNA.
DR EMBL; AY013762; AAK26051.1; -; mRNA.
DR EMBL; AF464178; AAM93577.1; -; Genomic_DNA.
DR EMBL; AF464180; AAM93579.1; -; mRNA.
DR EMBL; BC060211; AAH60211.1; -; mRNA.
DR EMBL; AK149282; BAE28788.1; -; mRNA.
DR CCDS; CCDS37776.1; -. [O88689-1]
DR RefSeq; NP_001167625.1; NM_001174154.2. [O88689-3]
DR RefSeq; NP_031792.1; NM_007766.2. [O88689-1]
DR PDB; 1WUZ; NMR; -; A=27-129.
DR PDB; 5DZW; X-ray; 2.43 A; A=30-450.
DR PDBsum; 1WUZ; -.
DR PDBsum; 5DZW; -.
DR AlphaFoldDB; O88689; -.
DR SMR; O88689; -.
DR BioGRID; 198893; 3.
DR CORUM; O88689; -.
DR DIP; DIP-41020N; -.
DR IntAct; O88689; 2.
DR GlyGen; O88689; 6 sites.
DR iPTMnet; O88689; -.
DR PhosphoSitePlus; O88689; -.
DR MaxQB; O88689; -.
DR PeptideAtlas; O88689; -.
DR PRIDE; O88689; -.
DR ProteomicsDB; 289318; -. [O88689-1]
DR ProteomicsDB; 289319; -. [O88689-2]
DR ProteomicsDB; 289320; -. [O88689-3]
DR DNASU; 12936; -.
DR Ensembl; ENSMUST00000115661; ENSMUSP00000111325; ENSMUSG00000103458. [O88689-3]
DR Ensembl; ENSMUST00000192295; ENSMUSP00000142103; ENSMUSG00000104252. [O88689-2]
DR Ensembl; ENSMUST00000192512; ENSMUSP00000141408; ENSMUSG00000104252. [O88689-1]
DR GeneID; 100384868; -.
DR GeneID; 12936; -.
DR KEGG; mmu:100384868; -.
DR KEGG; mmu:12936; -.
DR UCSC; uc008eox.3; mouse. [O88689-1]
DR UCSC; uc008eoy.2; mouse. [O88689-3]
DR CTD; 56144; -.
DR MGI; MGI:1298406; Pcdha4.
DR VEuPathDB; HostDB:ENSMUSG00000103458; -.
DR VEuPathDB; HostDB:ENSMUSG00000104252; -.
DR GeneTree; ENSGT00940000163846; -.
DR HOGENOM; CLU_006480_0_0_1; -.
DR InParanoid; O88689; -.
DR OMA; FIARFEI; -.
DR OrthoDB; 184745at2759; -.
DR BioGRID-ORCS; 100384868; 2 hits in 15 CRISPR screens.
DR BioGRID-ORCS; 12936; 1 hit in 37 CRISPR screens.
DR EvolutionaryTrace; O88689; -.
DR PRO; PR:O88689; -.
DR Proteomes; UP000000589; Chromosome 18.
DR RNAct; O88689; protein.
DR Bgee; ENSMUSG00000103458; Expressed in neural tube and 5 other tissues.
DR Genevisible; O88689; MM.
DR GO; GO:0005783; C:endoplasmic reticulum; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; IDA:MGI.
DR GO; GO:0045202; C:synapse; IDA:MGI.
DR GO; GO:0005509; F:calcium ion binding; IDA:UniProtKB.
DR GO; GO:0042802; F:identical protein binding; IDA:UniProtKB.
DR GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IC:UniProtKB.
DR InterPro; IPR002126; Cadherin-like_dom.
DR InterPro; IPR015919; Cadherin-like_sf.
DR InterPro; IPR031904; Cadherin_CBD.
DR InterPro; IPR020894; Cadherin_CS.
DR InterPro; IPR013164; Cadherin_N.
DR Pfam; PF00028; Cadherin; 5.
DR Pfam; PF08266; Cadherin_2; 1.
DR Pfam; PF15974; Cadherin_tail; 1.
DR PRINTS; PR00205; CADHERIN.
DR SMART; SM00112; CA; 6.
DR SUPFAM; SSF49313; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 6.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell membrane;
KW Disulfide bond; Glycoprotein; Membrane; Metal-binding; Reference proteome;
KW Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..29
FT /evidence="ECO:0000255"
FT CHAIN 30..947
FT /note="Protocadherin alpha-4"
FT /id="PRO_0000240663"
FT TOPO_DOM 30..697
FT /note="Extracellular"
FT /evidence="ECO:0000305|PubMed:27161523"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 719..947
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:9655502"
FT DOMAIN 30..133
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 134..242
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 243..350
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 351..455
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 456..565
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 573..681
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REPEAT 734..737
FT /note="PXXP 1"
FT REPEAT 774..777
FT /note="PXXP 2"
FT REPEAT 796..799
FT /note="PXXP 3"
FT REPEAT 829..832
FT /note="PXXP 4"
FT REPEAT 870..873
FT /note="PXXP 5"
FT REPEAT 888..891
FT /note="PXXP 6"
FT REGION 734..891
FT /note="6 X 4 AA repeats of P-X-X-P"
FT REGION 738..947
FT /note="Required for interaction with FYN"
FT /evidence="ECO:0000269|PubMed:9655502"
FT REGION 761..805
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 824..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 891..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 932..947
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 257
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 265
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZW"
FT CARBOHYD 438
FT /note="O-linked (Man) threonine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZW"
FT CARBOHYD 440
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZW"
FT CARBOHYD 442
FT /note="O-linked (Man) serine"
FT /evidence="ECO:0000269|PubMed:27161523,
FT ECO:0000312|PDB:5DZW"
FT CARBOHYD 548
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 96..102
FT /evidence="ECO:0000269|PubMed:15929006,
FT ECO:0000269|PubMed:27161523, ECO:0000312|PDB:1WUZ,
FT ECO:0000312|PDB:5DZW"
FT VAR_SEQ 535..795
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019413"
FT VAR_SEQ 796..947
FT /note="PRQPNPDWRYSASLRAGMHSSVHLEEAGILRAGPGGPDQQWPTVSSATPEPE
FT AGEVSPPVGAGVNSNSWTFKYGPGNPKQSGPGELPDKFIIPGSPAIISIRQEPANNQID
FT KSDFITFGKKEETKKKKKKKKGNKTQEKKEKGNSTTDNSDQ -> QAPPNTDWRFSQAQ
FT RPGTSGSQNGDETGTWPNNQFDTEMLQAMILASASEAADGSSTLGGGAGTMGLSARYGP
FT QFTLQHVPDYRQNVYIPGSNATLTNAAGKRDGKAPAGGNGNKKKSGKKEKK (in
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:12154121"
FT /id="VSP_019414"
FT VAR_SEQ 879..947
FT /note="GELPDKFIIPGSPAIISIRQEPANNQIDKSDFITFGKKEETKKKKKKKKGNK
FT TQEKKEKGNSTTDNSDQ -> EPKKQTQVSFLPRRKGEASQPRQ (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_019415"
FT STRAND 31..38
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 44..46
FT /evidence="ECO:0007829|PDB:5DZW"
FT HELIX 48..51
FT /evidence="ECO:0007829|PDB:5DZW"
FT HELIX 56..59
FT /evidence="ECO:0007829|PDB:5DZW"
FT TURN 60..63
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 65..71
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:5DZW"
FT TURN 79..82
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:5DZW"
FT HELIX 92..95
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 97..101
FT /evidence="ECO:0007829|PDB:1WUZ"
FT STRAND 103..110
FT /evidence="ECO:0007829|PDB:5DZW"
FT TURN 111..114
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 115..124
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:5DZW"
FT HELIX 164..166
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 168..172
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 176..181
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 193..196
FT /evidence="ECO:0007829|PDB:5DZW"
FT TURN 202..204
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 206..220
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 223..231
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 241..243
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 245..251
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 260..263
FT /evidence="ECO:0007829|PDB:5DZW"
FT HELIX 272..274
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 277..281
FT /evidence="ECO:0007829|PDB:5DZW"
FT HELIX 287..292
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 293..295
FT /evidence="ECO:0007829|PDB:5DZW"
FT TURN 297..299
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 301..304
FT /evidence="ECO:0007829|PDB:5DZW"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 314..324
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 326..328
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 331..340
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 349..355
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 358..360
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 368..375
FT /evidence="ECO:0007829|PDB:5DZW"
FT HELIX 380..383
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 385..389
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 396..401
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:5DZW"
FT TURN 415..417
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 420..429
FT /evidence="ECO:0007829|PDB:5DZW"
FT STRAND 436..446
FT /evidence="ECO:0007829|PDB:5DZW"
SQ SEQUENCE 947 AA; 103143 MW; 082497DBBAEFB503 CRC64;
MEFSWGSGQE SQRLLLSFLL LAIWEAGNSQ IHYSIPEEAK HGTFVGRIAQ DLGLELTELV
PRLFRVASKD RGDLLEVNLQ NGILFVNSRI DREELCGRSA ECSIHLEVIV DRPLQVFHVE
VEVRDINDNP PRFPTTQKNL FIAESRPLDT WFPLEGASDA DIGINAVLTY RLSPNDYFSL
EKPSNDERVK GLGLVLRKSL DREETPEIIL VLTVTDGGKP ELTGSVQLLI TVLDANDNAP
VFDRSLYTVK LPENVPNGTL VVKVNASDLD EGVNGDIMYS FSTDISPNVK YKFHIDPVSG
EIIVKGYIDF EECKSYEILI EGIDKGQLPL SGHCKVIVQV EDINDNVPEL EFKSLSLPIR
ENSPVGTVIA LISVSDRDTG VNGQVTCSLT SHVPFKLVST FKNYYSLVLD SALDRETTAD
YKVVVTARDG GSPSLWATAS VSVEVADVND NAPVFAQPEY TVFVKENNPP GAHIFTVSAM
DADAQENALV SYSLVERRVG ERLLSSYVSV HAESGKVFAL QPLDHEELEL LRFQVSARDA
GVPALGSNVT LQVFVLDEND NAPTLLEPEA GVSGGIVSRL VSRSVGAGHV VAKVRAVDAD
SGYNAWLSYE LQSSEGNSRS LFRVGLYTGE ISTTRILDEA DSPRQRLLVL VKDHGDPAMI
VTATVLVSLV ENGPVPKAPS RVSTSVTHSE ASLVDVNVYL IIAICAVSSL LVLTLLLYTA
LRCSTVPSES VCGPPKPVMV CSSAVGSWSY SQQRRQRVCS GEYPPKTDLM AFSPSLSDSR
DREDQLQSAE DSSGKPRQPN PDWRYSASLR AGMHSSVHLE EAGILRAGPG GPDQQWPTVS
SATPEPEAGE VSPPVGAGVN SNSWTFKYGP GNPKQSGPGE LPDKFIIPGS PAIISIRQEP
ANNQIDKSDF ITFGKKEETK KKKKKKKGNK TQEKKEKGNS TTDNSDQ
