DCC_RAT
ID DCC_RAT Reviewed; 1445 AA.
AC Q63155;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 2.
DT 25-MAY-2022, entry version 159.
DE RecName: Full=Netrin receptor DCC;
DE AltName: Full=Tumor suppressor protein DCC;
DE Flags: Precursor;
GN Name=Dcc;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH NTN1, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=8861902; DOI=10.1016/s0092-8674(00)81336-7;
RA Keino-Masu K., Masu M., Hinck L., Leonardo E.D., Chan S.S.-Y.,
RA Culotti J.G., Tessier-Lavigne M.;
RT "Deleted in colorectal cancer (DCC) encodes a netrin receptor.";
RL Cell 87:175-185(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway;
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INTERACTION WITH UNC5A; UNC5B AND UNC5C.
RX PubMed=10399920; DOI=10.1016/s0092-8674(00)80804-1;
RA Hong K., Hinck L., Nishiyama M., Poo M.-M., Tessier-Lavigne M., Stein E.;
RT "A ligand-gated association between cytoplasmic domains of UNC5 and DCC
RT family receptors converts netrin-induced growth cone attraction to
RT repulsion.";
RL Cell 97:927-941(1999).
RN [5]
RP GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-478, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=24090084; DOI=10.1021/pr400783j;
RA Parker B.L., Thaysen-Andersen M., Solis N., Scott N.E., Larsen M.R.,
RA Graham M.E., Packer N.H., Cordwell S.J.;
RT "Site-specific glycan-peptide analysis for determination of N-glycoproteome
RT heterogeneity.";
RL J. Proteome Res. 12:5791-5800(2013).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF 39-421, DISULFIDE BONDS, AND
RP GLYCOSYLATION AT ASN-60; ASN-94; ASN-299 AND ASN-318.
RA Chen Q., Liu J.-H., Wang J.-H.;
RT "Structure of DCC and the prediction of N-terminal horseshoe configuration
RT in other neural receptors.";
RL Submitted (JAN-2010) to the PDB data bank.
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) OF 1140-1166 IN COMPLEX WITH MAPK1,
RP INTERACTION WITH MAPK1, PHOSPHORYLATION AT SER-1178; THR-1187 AND SER-1267,
RP AND MUTAGENESIS OF SER-1178; THR-1187 AND SER-1267.
RX PubMed=21070949; DOI=10.1016/j.str.2010.08.011;
RA Ma W., Shang Y., Wei Z., Wen W., Wang W., Zhang M.;
RT "Phosphorylation of DCC by ERK2 is facilitated by direct docking of the
RT receptor P1 domain to the kinase.";
RL Structure 18:1502-1511(2010).
CC -!- FUNCTION: Receptor for netrin required for axon guidance. Mediates axon
CC attraction of neuronal growth cones in the developing nervous system
CC upon ligand binding. Its association with UNC5 proteins may trigger
CC signaling for axon repulsion. It also acts as a dependence receptor
CC required for apoptosis induction when not associated with netrin
CC ligand. Implicated as a tumor suppressor gene (By similarity).
CC {ECO:0000250, ECO:0000269|PubMed:8861902}.
CC -!- SUBUNIT: Interacts with the cytoplasmic part of UNC5A, UNC5B and UNC5C
CC (PubMed:10399920). Interacts with DSCAM (By similarity). Interacts with
CC PTK2/FAK1 (By similarity). Interacts with MYO10 (By similarity).
CC Interacts with MAPK1 (PubMed:21070949). Interacts with NTN1
CC (PubMed:8861902). Interacts with CBLN4; this interaction can be
CC competed by NTN1 (By similarity). Interacts with SIAH1 and SIAH2 (By
CC similarity). {ECO:0000250|UniProtKB:P43146,
CC ECO:0000250|UniProtKB:P70211, ECO:0000269|PubMed:10399920,
CC ECO:0000269|PubMed:21070949, ECO:0000269|PubMed:8861902}.
CC -!- INTERACTION:
CC Q63155; Q8CGU4: Agap2; NbExp=2; IntAct=EBI-1798965, EBI-4409108;
CC Q63155; Q63155: Dcc; NbExp=2; IntAct=EBI-1798965, EBI-1798965;
CC Q63155; P31977: Ezr; NbExp=2; IntAct=EBI-1798965, EBI-917242;
CC Q63155; P63086: Mapk1; NbExp=10; IntAct=EBI-1798965, EBI-397710;
CC Q63155; O55005: Robo1; NbExp=2; IntAct=EBI-1798965, EBI-3505237;
CC Q63155; Q9ERC8: Dscam; Xeno; NbExp=4; IntAct=EBI-1798965, EBI-1798601;
CC Q63155; P15311: EZR; Xeno; NbExp=3; IntAct=EBI-1798965, EBI-1056902;
CC Q63155; Q9HD67: MYO10; Xeno; NbExp=3; IntAct=EBI-1798965, EBI-307061;
CC Q63155; P46777: RPL5; Xeno; NbExp=4; IntAct=EBI-1798965, EBI-358018;
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:8861902}; Single-
CC pass type I membrane protein {ECO:0000269|PubMed:8861902}.
CC -!- TISSUE SPECIFICITY: Detected in embryonic spinal cord, predominantly in
CC axons of commissural neurons (at protein level). Detected in embryonic
CC spinal cord. {ECO:0000269|PubMed:8861902}.
CC -!- PTM: Ubiquitinated; mediated by SIAH1 or SIAH2 and leading to its
CC subsequent proteasomal degradation. {ECO:0000250|UniProtKB:P43146}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. DCC family.
CC {ECO:0000305}.
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DR EMBL; U68725; AAB41099.1; -; mRNA.
DR EMBL; CH473971; EDM14792.1; -; Genomic_DNA.
DR RefSeq; NP_036973.1; NM_012841.1.
DR PDB; 3LAF; X-ray; 2.40 A; A=39-421.
DR PDB; 3O71; X-ray; 1.95 A; B=1140-1166.
DR PDB; 5Z5K; X-ray; 2.49 A; A=39-418.
DR PDB; 6BZ3; X-ray; 2.50 A; B/D=1421-1443.
DR PDBsum; 3LAF; -.
DR PDBsum; 3O71; -.
DR PDBsum; 5Z5K; -.
DR PDBsum; 6BZ3; -.
DR AlphaFoldDB; Q63155; -.
DR SMR; Q63155; -.
DR DIP; DIP-46811N; -.
DR ELM; Q63155; -.
DR IntAct; Q63155; 15.
DR STRING; 10116.ENSRNOP00000063072; -.
DR GlyGen; Q63155; 7 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q63155; -.
DR PhosphoSitePlus; Q63155; -.
DR PaxDb; Q63155; -.
DR GeneID; 25311; -.
DR KEGG; rno:25311; -.
DR CTD; 1630; -.
DR RGD; 2492; Dcc.
DR eggNOG; KOG4221; Eukaryota.
DR InParanoid; Q63155; -.
DR OrthoDB; 217780at2759; -.
DR TreeFam; TF321506; -.
DR Reactome; R-RNO-373752; Netrin-1 signaling.
DR Reactome; R-RNO-418885; DCC mediated attractive signaling.
DR Reactome; R-RNO-418889; Caspase activation via Dependence Receptors in the absence of ligand.
DR EvolutionaryTrace; Q63155; -.
DR PRO; PR:Q63155; -.
DR Proteomes; UP000002494; Unplaced.
DR Proteomes; UP000234681; Chromosome 18.
DR GO; GO:0030424; C:axon; IDA:RGD.
DR GO; GO:0044295; C:axonal growth cone; IBA:GO_Central.
DR GO; GO:0009986; C:cell surface; IBA:GO_Central.
DR GO; GO:0032584; C:growth cone membrane; IDA:RGD.
DR GO; GO:0099061; C:integral component of postsynaptic density membrane; ISO:RGD.
DR GO; GO:0045121; C:membrane raft; IDA:RGD.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; ISO:RGD.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0005042; F:netrin receptor activity; IMP:RGD.
DR GO; GO:0003713; F:transcription coactivator activity; IMP:RGD.
DR GO; GO:0033564; P:anterior/posterior axon guidance; ISO:RGD.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0007411; P:axon guidance; IMP:RGD.
DR GO; GO:0098609; P:cell-cell adhesion; IBA:GO_Central.
DR GO; GO:0033563; P:dorsal/ventral axon guidance; ISO:RGD.
DR GO; GO:0001764; P:neuron migration; ISO:RGD.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IMP:RGD.
DR GO; GO:0010976; P:positive regulation of neuron projection development; IMP:RGD.
DR GO; GO:0099170; P:postsynaptic modulation of chemical synaptic transmission; ISO:RGD.
DR GO; GO:1901214; P:regulation of neuron death; ISO:RGD.
DR GO; GO:0001975; P:response to amphetamine; IEP:RGD.
DR GO; GO:0021965; P:spinal cord ventral commissure morphogenesis; ISO:RGD.
DR CDD; cd00063; FN3; 6.
DR Gene3D; 2.60.40.10; -; 10.
DR InterPro; IPR033012; DCC.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR013098; Ig_I-set.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR010560; Neogenin_C.
DR PANTHER; PTHR44170:SF8; PTHR44170:SF8; 1.
DR Pfam; PF00041; fn3; 6.
DR Pfam; PF07679; I-set; 3.
DR Pfam; PF13895; Ig_2; 1.
DR Pfam; PF06583; Neogenin_C; 1.
DR SMART; SM00060; FN3; 6.
DR SMART; SM00409; IG; 5.
DR SMART; SM00408; IGc2; 4.
DR SUPFAM; SSF48726; SSF48726; 4.
DR SUPFAM; SSF49265; SSF49265; 4.
DR PROSITE; PS50853; FN3; 6.
DR PROSITE; PS50835; IG_LIKE; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Apoptosis; Developmental protein; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Membrane; Phosphoprotein; Receptor;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix;
KW Tumor suppressor; Ubl conjugation.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..1445
FT /note="Netrin receptor DCC"
FT /id="PRO_0000416246"
FT TRANSMEM 1100..1120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 26..135
FT /note="Ig-like C2-type 1"
FT DOMAIN 139..229
FT /note="Ig-like C2-type 2"
FT DOMAIN 234..326
FT /note="Ig-like C2-type 3"
FT DOMAIN 331..416
FT /note="Ig-like C2-type 4"
FT DOMAIN 431..524
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 530..620
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 625..718
FT /note="Fibronectin type-III 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 728..821
FT /note="Fibronectin type-III 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 846..942
FT /note="Fibronectin type-III 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 947..1044
FT /note="Fibronectin type-III 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REGION 1126..1152
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1167..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1327
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1177..1220
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1178
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:21070949"
FT MOD_RES 1187
FT /note="Phosphothreonine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:21070949"
FT MOD_RES 1267
FT /note="Phosphoserine; by MAPK1"
FT /evidence="ECO:0000269|PubMed:21070949"
FT CARBOHYD 60
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.6"
FT CARBOHYD 94
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.6"
FT CARBOHYD 299
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.6"
FT CARBOHYD 318
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000269|Ref.6"
FT CARBOHYD 478
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0007744|PubMed:24090084"
FT CARBOHYD 628
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 702
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 61..117
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|Ref.6"
FT DISULFID 161..212
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|Ref.6"
FT DISULFID 261..310
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|Ref.6"
FT DISULFID 352..400
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114,
FT ECO:0000269|Ref.6"
FT MUTAGEN 1178
FT /note="S->A: Abolishes phosphorylation by MAPK1; when
FT associated with A-1187 and A-1267."
FT /evidence="ECO:0000269|PubMed:21070949"
FT MUTAGEN 1187
FT /note="T->A: Abolishes phosphorylation by MAPK1; when
FT associated with A-1178 and A-1267."
FT /evidence="ECO:0000269|PubMed:21070949"
FT MUTAGEN 1267
FT /note="S->A: Abolishes phosphorylation by MAPK1; when
FT associated with A-1178 and A-1187."
FT /evidence="ECO:0000269|PubMed:21070949"
FT STRAND 39..44
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 49..51
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 89..91
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 97..99
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 113..120
FT /evidence="ECO:0007829|PDB:3LAF"
FT HELIX 122..124
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 126..128
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 132..136
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:5Z5K"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 170..179
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 197..199
FT /evidence="ECO:0007829|PDB:3LAF"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 208..215
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 219..222
FT /evidence="ECO:0007829|PDB:5Z5K"
FT STRAND 226..231
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 238..244
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 249..252
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 257..259
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 262..267
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 270..275
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 283..290
FT /evidence="ECO:0007829|PDB:3LAF"
FT TURN 291..293
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 294..297
FT /evidence="ECO:0007829|PDB:3LAF"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 306..314
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 317..335
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 348..350
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 353..358
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 361..366
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 374..380
FT /evidence="ECO:0007829|PDB:3LAF"
FT TURN 381..383
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 384..389
FT /evidence="ECO:0007829|PDB:3LAF"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 396..404
FT /evidence="ECO:0007829|PDB:3LAF"
FT STRAND 407..416
FT /evidence="ECO:0007829|PDB:3LAF"
FT HELIX 1422..1437
FT /evidence="ECO:0007829|PDB:6BZ3"
SQ SEQUENCE 1445 AA; 157941 MW; 084F625954481988 CRC64;
MENSLGCVWV PKLAFVLFGA SLLSAHLQVT GFQIKPFTSL HFVSEPSDAV TMRGGNVLLN
CSAESDRGVP VIKWKKDGLI LALGMDDRKQ QLPNGSLLIQ NILHSRHHKP DEGLYQCEAS
LGDSGSIISR TAKVMVAGPL RFLSQTESIT AFMGDTVLLK CEVIGDPMPT IHWQKNQQDL
NPIPGDSRVV VLPSGALQIS RLQPGDSGVY RCSARNPAST RTGNEAEVRI LSDPGLHRQL
YFLQRPSNVI AIEGKDAVLE CCVSGYPPPS FTWLRGEEVI QLRSKKYSLL GGSNLLISNV
TDDDSGTYTC VVTYKNENIS ASAELTVLVP PWFLNHPSNL YAYESMDIEF ECAVSGKPVP
TVNWMKNGDV VIPSDYFQIV GGSNLRILGV VKSDEGFYQC VAENEAGNAQ SSAQLIVPKP
AIPSSSILPS APRDVVPVLV SSRFVRLSWR PPAEAKGNIQ TFTVFFSREG DNRERALNTT
QPGSLQLTVG NLKPEAMYTF RVVAYNEWGP GESSQPIKVA TQPELQVPGP VENLHAVSAS
PTSILITWEP PAYANGPVQG YRLFCTEVST GKEQNIEVDG LSYKLEGLKK FTEYTLRFLA
YNRYGPGVST DDITVVTLSD VPSAPPQNVS LEVVNSRSIK VSWLPPPSGT QNGFITGYKI
RHRKTTRRGE METLEPNNLW YLFTGLEKGS QYSFQVSAMT VNGTGPPSNW YTAETPENDL
DESQVPDQPS SLHVRPQTNC IIMSWTPPLN PNIVVRGYII GYGVGSPYAE TVRVDSKQRY
YSIERLESSS HYVISLKAFN NAGEGVPLYE SATTRSITDP TDPVDYYPLL DDFPTSGPDV
STPMLPPVGV QAVALTHEAV RVSWADNSVP KNQKTSDVRL YTVRWRTSFS ASAKYKSEDT
TSLSYTATGL KPNTMYEFSV MVTKNRRSST WSMTAHATTY EAAPTSAPKD LTVITREGKP
RAVIVSWQPP LEANGKITAY ILFYTLDKNI PIDDWIMETI SGDRLTHQIM DLSLDTMYYF
RIQARNAKGV GPLSDPILFR TLKVEHPDKM ANDQGRHGDG GYWPVDTNLI DRSTLNEPPI
GQMHPPHGSV TPQKNSNLLV ITVVTVGVLT VLVVVIVAVI CTRRSSAQQR KKRATHSASK
RKGSQKDLRP PDLWIHHEEM EMKNIEKPAG TDPAGRGSPI QSCQDLTPVS HSQSESQMGS
KSASHSGQDT EEAGSSMSTL ERSLAARRAT RTKLMIPMEA QSNNPAVVSA IPVPTLESAQ
YPGILPSPTC GYPHPQFTLR PVPFPTLSVD RGFGAGRTVS EGPTAQQQPM LPPAQPEHPS
SEEAPSRTIP TACVRPTHPL RSFANPLLPP PMSAIEPKVP YTPLLSQPGP TLPKTHVKTA
SLGLAGKARS PLLPVSVPTA PEVSEESHKP TEDPASVYEQ DDLSEQMASL EGLMKQLNAI
TGSAF
