ID   PCDH1_HUMAN             Reviewed;        1060 AA.
AC   Q08174; Q8IUP2;
DT   19-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 2.
DT   24-JAN-2024, entry version 188.
DE   RecName: Full=Protocadherin-1;
DE   AltName: Full=Cadherin-like protein 1;
DE   AltName: Full=Protocadherin-42;
DE            Short=PC42;
DE   Flags: Precursor;
GN   Name=PCDH1;
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 [LARGE SCALE GENOMIC DNA].
RX   PubMed=15372022; DOI=10.1038/nature02919;
RA   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA   Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA   She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA   Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA   Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M.,
RA   Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T.,
RA   Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A.,
RA   Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R.,
RA   Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L.,
RA   Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N.,
RA   Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J.,
RA   Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A.,
RA   Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT   "The DNA sequence and comparative analysis of human chromosome 5.";
RL   Nature 431:268-274(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC   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   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] OF 10-1060 (ISOFORM 1), NUCLEOTIDE SEQUENCE
RP   [MRNA] OF 980-1060 (ISOFORM 2), AND VARIANT PRO-25.
RC   TISSUE=Brain;
RX   PubMed=8508762; DOI=10.1002/j.1460-2075.1993.tb05878.x;
RA   Sano K., Tanihara H., Heimark R.L., Obata S., Davidson M., St John T.,
RA   Taketani S., Suzuki S.;
RT   "Protocadherins: a large family of cadherin-related molecules in central
RT   nervous system.";
RL   EMBO J. 12:2249-2256(1993).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-949 AND SER-962, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-305; ASN-813 AND ASN-818.
RC   TISSUE=Liver;
RX   PubMed=19159218; DOI=10.1021/pr8008012;
RA   Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
RT   "Glycoproteomics analysis of human liver tissue by combination of multiple
RT   enzyme digestion and hydrazide chemistry.";
RL   J. Proteome Res. 8:651-661(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-918; SER-962 AND SER-984, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1173 (ISOFORM 2), AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Liver;
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
CC   -!- FUNCTION: May be involved in cell-cell interaction processes and in
CC       cell adhesion.
CC   -!- SUBCELLULAR LOCATION: Cell junction. Cell membrane {ECO:0000305};
CC       Single-pass type I membrane protein {ECO:0000305}. Note=Found at cell-
CC       cell boundaries and probably at cell-matrix boundaries.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q08174-1; Sequence=Displayed;
CC       Name=2; Synonyms=PC42-8;
CC         IsoId=Q08174-2; Sequence=VSP_000703;
CC   -!- TISSUE SPECIFICITY: Highly expressed in the brain and neuro-glial
CC       cells.
CC   -!- DEVELOPMENTAL STAGE: Highest expression in adults.
CC   -!- CAUTION: It is uncertain whether Met-1 or Met-23 is the initiator.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA36419.1; Type=Miscellaneous discrepancy; Note=Probable cloning artifact.; Evidence={ECO:0000305};
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DR   EMBL; AC094107; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471062; EAW61902.1; -; Genomic_DNA.
DR   EMBL; BC035812; AAH35812.1; -; mRNA.
DR   EMBL; L11369; AAA36418.1; -; mRNA.
DR   EMBL; L11370; AAA36419.1; ALT_SEQ; mRNA.
DR   CCDS; CCDS4267.1; -. [Q08174-2]
DR   CCDS; CCDS43375.1; -. [Q08174-1]
DR   RefSeq; NP_001265542.1; NM_001278613.1.
DR   RefSeq; NP_001265544.1; NM_001278615.1.
DR   RefSeq; NP_002578.2; NM_002587.4. [Q08174-1]
DR   RefSeq; NP_115796.2; NM_032420.3. [Q08174-2]
DR   PDB; 6BX7; X-ray; 2.85 A; A=58-503.
DR   PDB; 6MGA; X-ray; 3.15 A; A=58-503.
DR   PDB; 6PIM; X-ray; 3.05 A; A=271-503.
DR   PDB; 6VFP; X-ray; 3.20 A; A=58-498.
DR   PDBsum; 6BX7; -.
DR   PDBsum; 6MGA; -.
DR   PDBsum; 6PIM; -.
DR   PDBsum; 6VFP; -.
DR   AlphaFoldDB; Q08174; -.
DR   EMDB; EMD-21188; -.
DR   EMDB; EMD-21189; -.
DR   EMDB; EMD-21190; -.
DR   SMR; Q08174; -.
DR   BioGRID; 111130; 110.
DR   IntAct; Q08174; 15.
DR   MINT; Q08174; -.
DR   STRING; 9606.ENSP00000287008; -.
DR   GlyCosmos; Q08174; 6 sites, No reported glycans.
DR   GlyGen; Q08174; 6 sites.
DR   iPTMnet; Q08174; -.
DR   PhosphoSitePlus; Q08174; -.
DR   SwissPalm; Q08174; -.
DR   BioMuta; PCDH1; -.
DR   DMDM; 215273864; -.
DR   CPTAC; CPTAC-1310; -.
DR   EPD; Q08174; -.
DR   jPOST; Q08174; -.
DR   MassIVE; Q08174; -.
DR   MaxQB; Q08174; -.
DR   PaxDb; 9606-ENSP00000287008; -.
DR   PeptideAtlas; Q08174; -.
DR   ProteomicsDB; 58575; -. [Q08174-1]
DR   ProteomicsDB; 58576; -. [Q08174-2]
DR   Antibodypedia; 27376; 346 antibodies from 28 providers.
DR   DNASU; 5097; -.
DR   Ensembl; ENST00000287008.8; ENSP00000287008.3; ENSG00000156453.14. [Q08174-2]
DR   Ensembl; ENST00000394536.4; ENSP00000378043.3; ENSG00000156453.14. [Q08174-1]
DR   GeneID; 5097; -.
DR   KEGG; hsa:5097; -.
DR   MANE-Select; ENST00000287008.8; ENSP00000287008.3; NM_032420.5; NP_115796.2. [Q08174-2]
DR   UCSC; uc003llp.4; human. [Q08174-1]
DR   AGR; HGNC:8655; -.
DR   CTD; 5097; -.
DR   DisGeNET; 5097; -.
DR   GeneCards; PCDH1; -.
DR   HGNC; HGNC:8655; PCDH1.
DR   HPA; ENSG00000156453; Low tissue specificity.
DR   MIM; 603626; gene.
DR   neXtProt; NX_Q08174; -.
DR   OpenTargets; ENSG00000156453; -.
DR   PharmGKB; PA32994; -.
DR   VEuPathDB; HostDB:ENSG00000156453; -.
DR   eggNOG; ENOG502QWB7; Eukaryota.
DR   GeneTree; ENSGT00940000155521; -.
DR   HOGENOM; CLU_006480_5_3_1; -.
DR   InParanoid; Q08174; -.
DR   OMA; NASYKHI; -.
DR   OrthoDB; 5353710at2759; -.
DR   PhylomeDB; Q08174; -.
DR   TreeFam; TF320624; -.
DR   PathwayCommons; Q08174; -.
DR   SignaLink; Q08174; -.
DR   BioGRID-ORCS; 5097; 69 hits in 1159 CRISPR screens.
DR   ChiTaRS; PCDH1; human.
DR   GeneWiki; PCDH1; -.
DR   GenomeRNAi; 5097; -.
DR   Pharos; Q08174; Tbio.
DR   PRO; PR:Q08174; -.
DR   Proteomes; UP000005640; Chromosome 5.
DR   RNAct; Q08174; Protein.
DR   Bgee; ENSG00000156453; Expressed in lower esophagus mucosa and 178 other cell types or tissues.
DR   ExpressionAtlas; Q08174; baseline and differential.
DR   GO; GO:0030054; C:cell junction; IDA:HPA.
DR   GO; GO:0005911; C:cell-cell junction; TAS:ProtInc.
DR   GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
DR   GO; GO:0005730; C:nucleolus; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005886; C:plasma membrane; TAS:ProtInc.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0007155; P:cell adhesion; IBA:GO_Central.
DR   GO; GO:0007267; P:cell-cell signaling; TAS:ProtInc.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   GO; GO:0007399; P:nervous system development; TAS:ProtInc.
DR   CDD; cd11304; Cadherin_repeat; 7.
DR   Gene3D; 2.60.40.60; Cadherins; 7.
DR   InterPro; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR015919; Cadherin-like_sf.
DR   InterPro; IPR020894; Cadherin_CS.
DR   InterPro; IPR013164; Cadherin_N.
DR   InterPro; IPR013585; Protocadherin.
DR   PANTHER; PTHR24028; CADHERIN-87A; 1.
DR   PANTHER; PTHR24028:SF247; PROTOCADHERIN-1; 1.
DR   Pfam; PF00028; Cadherin; 6.
DR   Pfam; PF08266; Cadherin_2; 1.
DR   Pfam; PF08374; Protocadherin; 1.
DR   PRINTS; PR00205; CADHERIN.
DR   SMART; SM00112; CA; 6.
DR   SUPFAM; SSF49313; Cadherin-like; 6.
DR   PROSITE; PS00232; CADHERIN_1; 6.
DR   PROSITE; PS50268; CADHERIN_2; 7.
DR   Genevisible; Q08174; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Calcium; Cell adhesion; Cell junction;
KW   Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW   Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..57
FT                   /evidence="ECO:0000255"
FT   CHAIN           58..1060
FT                   /note="Protocadherin-1"
FT                   /id="PRO_0000354078"
FT   TOPO_DOM        58..852
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        853..873
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        874..1060
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          58..168
FT                   /note="Cadherin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          169..280
FT                   /note="Cadherin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          281..387
FT                   /note="Cadherin 3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          396..506
FT                   /note="Cadherin 4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          507..612
FT                   /note="Cadherin 5"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          613..715
FT                   /note="Cadherin 6"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   DOMAIN          718..844
FT                   /note="Cadherin 7"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT   REGION          884..1045
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        884..898
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        919..934
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        972..991
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1002..1041
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         918
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         949
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         962
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:21406692"
FT   MOD_RES         984
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   CARBOHYD        305
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        403
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        618
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        662
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        813
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   CARBOHYD        818
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:19159218"
FT   VAR_SEQ         1034..1060
FT                   /note="VGQPFQLSTPQPLPHPYHGAIWTEVWE -> LPHRRVTFSATSQAQELQDPS
FT                   QHSYYDSGLEESETPSSKSSSGPRLGPLALPEDHYERTTPDGSIGEMEHPENDLRPLPD
FT                   VAMTGTCTRECSEFGHSDTCWMPGQSSPSRRTKSSALKLSTFVPYQDRGGQEPAGAGSP
FT                   SPPEDRNTKTAPVRLLPSYSAFSHSSHDSCKDSATLEEIPLTQTSDFPPAATPASAQTA
FT                   KREIYL (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:8508762"
FT                   /id="VSP_000703"
FT   VARIANT         15
FT                   /note="L -> F (in dbSNP:rs12517385)"
FT                   /id="VAR_047530"
FT   VARIANT         25
FT                   /note="H -> P (in dbSNP:rs12515587)"
FT                   /evidence="ECO:0000269|PubMed:8508762"
FT                   /id="VAR_047531"
FT   VARIANT         514
FT                   /note="A -> T (in dbSNP:rs3822357)"
FT                   /id="VAR_047532"
FT   CONFLICT        147
FT                   /note="G -> A (in Ref. 4; AAA36419)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        262
FT                   /note="S -> T (in Ref. 4; AAA36419)"
FT                   /evidence="ECO:0000305"
FT   STRAND          63..67
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          73..75
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   HELIX           77..79
FT                   /evidence="ECO:0007829|PDB:6VFP"
FT   STRAND          90..94
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   TURN            96..98
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          99..102
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   TURN            103..106
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          107..110
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   TURN            117..119
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   HELIX           121..123
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          128..130
FT                   /evidence="ECO:0007829|PDB:6VFP"
FT   STRAND          132..140
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          143..145
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          150..159
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          169..178
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          186..188
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   HELIX           198..200
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          201..208
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   HELIX           211..214
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          217..222
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          229..234
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   TURN            240..242
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          245..258
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          261..271
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          279..290
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          298..301
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   HELIX           310..312
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          315..321
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   HELIX           324..329
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          330..332
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   TURN            334..336
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          338..341
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   TURN            347..349
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          351..361
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          363..365
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          368..378
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          386..390
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          401..403
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          413..420
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   HELIX           425..428
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          431..434
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          439..444
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          446..448
FT                   /evidence="ECO:0007829|PDB:6MGA"
FT   STRAND          453..462
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   TURN            466..468
FT                   /evidence="ECO:0007829|PDB:6VFP"
FT   STRAND          472..479
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   STRAND          487..495
FT                   /evidence="ECO:0007829|PDB:6BX7"
FT   MOD_RES         Q08174-2:1173
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:24275569"
FT   CONFLICT        Q08174-2:1156
FT                   /note="V -> M (in Ref. 4; AAA36418)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   1060 AA;  114743 MW;  0F4F24F3EE607D04 CRC64;
     MDSGAGGRRC PEAALLILGP PRMEHLRHSP GPGGQRLLLP SMLLALLLLL APSPGHATRV
     VYKVPEEQPP NTLIGSLAAD YGFPDVGHLY KLEVGAPYLR VDGKTGDIFT TETSIDREGL
     RECQNQLPGD PCILEFEVSI TDLVQNGSPR LLEGQIEVQD INDNTPNFAS PVITLAIPEN
     TNIGSLFPIP LASDRDAGPN GVASYELQAG PEAQELFGLQ VAEDQEEKQP QLIVMGNLDR
     ERWDSYDLTI KVQDGGSPPR ASSALLRVTV LDTNDNAPKF ERPSYEAELS ENSPIGHSVI
     QVKANDSDQG ANAEIEYTFH QAPEVVRRLL RLDRNTGLIT VQGPVDREDL STLRFSVLAK
     DRGTNPKSAR AQVVVTVKDM NDNAPTIEIR GIGLVTHQDG MANISEDVAE ETAVALVQVS
     DRDEGENAAV TCVVAGDVPF QLRQASETGS DSKKKYFLQT TTPLDYEKVK DYTIEIVAVD
     SGNPPLSSTN SLKVQVVDVN DNAPVFTQSV TEVAFPENNK PGEVIAEITA SDADSGSNAE
     LVYSLEPEPA AKGLFTISPE TGEIQVKTSL DREQRESYEL KVVAADRGSP SLQGTATVLV
     NVLDCNDNDP KFMLSGYNFS VMENMPALSP VGMVTVIDGD KGENAQVQLS VEQDNGDFVI
     QNGTGTILSS LSFDREQQST YTFQLKAVDG GVPPRSAYVG VTINVLDEND NAPYITAPSN
     TSHKLLTPQT RLGETVSQVA AEDFDSGVNA ELIYSIAGGN PYGLFQIGSH SGAITLEKEI
     ERRHHGLHRL VVKVSDRGKP PRYGTALVHL YVNETLANRT LLETLLGHSL DTPLDIDIAG
     DPEYERSKQR GNILFGVVAG VVAVALLIAL AVLVRYCRQR EAKSGYQAGK KETKDLYAPK
     PSGKASKGNK SKGKKSKSPK PVKPVEDEDE AGLQKSLKFN LMSDAPGDSP RIHLPLNYPP
     GSPDLGRHYR SNSPLPSIQL QPQSPSASKK HQVVQDLPPA NTFVGTGDTT STGSEQYSDY
     SYRTNPPKYP SKQVGQPFQL STPQPLPHPY HGAIWTEVWE
//