PC11X_HUMAN
ID PC11X_HUMAN Reviewed; 1347 AA.
AC Q9BZA7; A6NIQ4; Q2TJH0; Q2TJH1; Q2TJH3; Q5JVZ0; Q70LR8; Q70LS7; Q70LS8;
AC Q70LS9; Q70LT7; Q70LT8; Q70LT9; Q70LU0; Q70LU1; Q96RV4; Q96RW0; Q9BZA6;
AC Q9H4E0; Q9P2M0; Q9P2X5;
DT 18-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 165.
DE RecName: Full=Protocadherin-11 X-linked;
DE Short=Protocadherin-11;
DE AltName: Full=Protocadherin on the X chromosome;
DE Short=PCDH-X;
DE AltName: Full=Protocadherin-S;
DE Flags: Precursor;
GN Name=PCDH11X; Synonyms=KIAA1326, PCDH11, PCDHX;
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 7), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=10644456; DOI=10.1006/geno.1999.6042;
RA Yoshida K., Sugano S.;
RT "Identification of a novel protocadherin gene (PCDH11) on the human XY
RT homology region in Xq21.3.";
RL Genomics 62:540-543(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND TISSUE SPECIFICITY.
RC TISSUE=Brain;
RX PubMed=11003707; DOI=10.1007/s003350010177;
RA Blanco P., Sargent C.A., Boucher C., Mitchell M., Affara N.;
RT "Conservation of PCDHX in mammals; expression of human X/Y genes
RT predominantly in brain.";
RL Mamm. Genome 11:906-914(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
RX PubMed=12815422; DOI=10.1038/nature01722;
RA Skaletsky H., Kuroda-Kawaguchi T., Minx P.J., Cordum H.S., Hillier L.W.,
RA Brown L.G., Repping S., Pyntikova T., Ali J., Bieri T., Chinwalla A.,
RA Delehaunty A., Delehaunty K., Du H., Fewell G., Fulton L., Fulton R.,
RA Graves T.A., Hou S.-F., Latrielle P., Leonard S., Mardis E., Maupin R.,
RA McPherson J., Miner T., Nash W., Nguyen C., Ozersky P., Pepin K., Rock S.,
RA Rohlfing T., Scott K., Schultz B., Strong C., Tin-Wollam A., Yang S.-P.,
RA Waterston R.H., Wilson R.K., Rozen S., Page D.C.;
RT "The male-specific region of the human Y chromosome is a mosaic of discrete
RT sequence classes.";
RL Nature 423:825-837(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 5).
RA Kools P.F.J., van Roy F.;
RT "Identification and cloning of a human chromosome X-linked protocadherin
RT gene with seven extracellular domains and an unusual large cytoplasmic
RT domain.";
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 4; 5; 6 AND 8).
RC TISSUE=Fetal brain;
RA Vanhalst K., Kools P., Staes K., van Roy F., Redies C.;
RT "Delta-protocadherins: a subfamily of protocadherins expressed
RT differentially in the mouse nervous system.";
RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15772651; DOI=10.1038/nature03440;
RA Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D.,
RA Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L.,
RA Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.,
RA Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A.,
RA Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P.,
RA Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D.,
RA Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D.,
RA Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L.,
RA Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P.,
RA Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G.,
RA Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J.,
RA Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D.,
RA Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L.,
RA Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z.,
RA Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S.,
RA Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S.,
RA Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O.,
RA Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H.,
RA Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T.,
RA Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L.,
RA Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R.,
RA Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y.,
RA Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K.,
RA Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J.,
RA Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L.,
RA Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S.,
RA Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A.,
RA Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L.,
RA Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D.,
RA Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H.,
RA McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S.,
RA Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C.,
RA Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S.,
RA Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V.,
RA Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K.,
RA Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K.,
RA Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D.,
RA Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R.,
RA Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B.,
RA Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C.,
RA d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q.,
RA Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N.,
RA Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A.,
RA Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J.,
RA Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A.,
RA Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F.,
RA Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L.,
RA Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S.,
RA Rogers J., Bentley D.R.;
RT "The DNA sequence of the human X chromosome.";
RL Nature 434:325-337(2005).
RN [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-1011; 1049-1114 AND 1124-1347, NUCLEOTIDE
RP SEQUENCE [MRNA] OF 181-1347 (ISOFORM 7), AND ALTERNATIVE SPLICING.
RX PubMed=14727141; DOI=10.1007/s00335-003-3028-7;
RA Blanco-Arias P., Sargent C.A., Affara N.A.;
RT "Protocadherin X (PCDHX) and Y (PCDHY) genes; multiple mRNA isoforms
RT encoding variant signal peptides and cytoplasmic domains.";
RL Mamm. Genome 15:41-52(2004).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 924-1347.
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI. The
RT complete sequences of 150 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [9]
RP VARIANT [LARGE SCALE ANALYSIS] GLY-42.
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: Potential calcium-dependent cell-adhesion protein.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass type I
CC membrane protein {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=8;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q9BZA7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9BZA7-2; Sequence=VSP_017980, VSP_017983;
CC Name=3;
CC IsoId=Q9BZA7-3; Sequence=VSP_017984;
CC Name=4;
CC IsoId=Q9BZA7-4; Sequence=VSP_017984, VSP_017987;
CC Name=5;
CC IsoId=Q9BZA7-5; Sequence=VSP_017979;
CC Name=6;
CC IsoId=Q9BZA7-6; Sequence=VSP_017985, VSP_017986;
CC Name=7; Synonyms=Protocadherin-Xa;
CC IsoId=Q9BZA7-7; Sequence=VSP_017981, VSP_017982;
CC Name=8;
CC IsoId=Q9BZA7-8; Sequence=VSP_017987;
CC -!- TISSUE SPECIFICITY: Expressed strongly in fetal brain and brain
CC (cortex, amygdala, thalamus, substantia nigra, hippocampus, caudate
CC nucleus and corpus callosum). Expressed at low level in testis.
CC {ECO:0000269|PubMed:10644456, ECO:0000269|PubMed:11003707}.
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DR EMBL; AB026187; BAA90765.1; -; mRNA.
DR EMBL; AJ276804; CAC13123.1; -; mRNA.
DR EMBL; AF332218; AAK13470.1; -; mRNA.
DR EMBL; AF332219; AAK13471.1; -; mRNA.
DR EMBL; AF206516; AAK82655.1; -; mRNA.
DR EMBL; AF217288; AAK82656.1; -; mRNA.
DR EMBL; AY861432; AAX56122.1; -; mRNA.
DR EMBL; AY861433; AAX56123.1; -; mRNA.
DR EMBL; AY861434; AAX56124.1; -; mRNA.
DR EMBL; AY861435; AAX56125.1; -; mRNA.
DR EMBL; AC004388; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL121869; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133274; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ564931; CAD92410.1; -; mRNA.
DR EMBL; AJ564932; CAD92411.1; -; mRNA.
DR EMBL; AJ564933; CAD92412.1; -; mRNA.
DR EMBL; AJ564934; CAD92413.1; -; mRNA.
DR EMBL; AJ564935; CAD92414.1; -; mRNA.
DR EMBL; AJ564936; CAD92415.1; -; mRNA.
DR EMBL; AJ564942; CAD92421.1; -; mRNA.
DR EMBL; AJ564945; CAD92424.1; -; mRNA.
DR EMBL; AJ564946; CAD92425.1; -; mRNA.
DR EMBL; AJ564947; CAD92426.1; -; mRNA.
DR EMBL; AB037747; BAA92564.1; -; mRNA.
DR CCDS; CCDS14461.1; -. [Q9BZA7-1]
DR CCDS; CCDS14462.1; -. [Q9BZA7-3]
DR CCDS; CCDS55458.1; -. [Q9BZA7-6]
DR CCDS; CCDS55459.1; -. [Q9BZA7-8]
DR CCDS; CCDS55460.1; -. [Q9BZA7-4]
DR CCDS; CCDS55461.1; -. [Q9BZA7-5]
DR RefSeq; NP_001161832.1; NM_001168360.1. [Q9BZA7-8]
DR RefSeq; NP_001161833.1; NM_001168361.1. [Q9BZA7-6]
DR RefSeq; NP_001161834.1; NM_001168362.1. [Q9BZA7-5]
DR RefSeq; NP_001161835.1; NM_001168363.1. [Q9BZA7-4]
DR RefSeq; NP_116750.1; NM_032968.4. [Q9BZA7-1]
DR RefSeq; NP_116751.1; NM_032969.4. [Q9BZA7-3]
DR RefSeq; XP_011529216.1; XM_011530914.2. [Q9BZA7-1]
DR RefSeq; XP_016884911.1; XM_017029422.1. [Q9BZA7-2]
DR AlphaFoldDB; Q9BZA7; -.
DR SMR; Q9BZA7; -.
DR BioGRID; 118142; 6.
DR IntAct; Q9BZA7; 4.
DR STRING; 9606.ENSP00000362186; -.
DR GlyConnect; 2065; 1 N-Linked glycan (1 site).
DR GlyGen; Q9BZA7; 6 sites, 2 N-linked glycans (1 site).
DR iPTMnet; Q9BZA7; -.
DR PhosphoSitePlus; Q9BZA7; -.
DR BioMuta; PCDH11X; -.
DR DMDM; 74761344; -.
DR EPD; Q9BZA7; -.
DR jPOST; Q9BZA7; -.
DR MassIVE; Q9BZA7; -.
DR PaxDb; Q9BZA7; -.
DR PeptideAtlas; Q9BZA7; -.
DR PRIDE; Q9BZA7; -.
DR ProteomicsDB; 79788; -. [Q9BZA7-1]
DR ProteomicsDB; 79789; -. [Q9BZA7-2]
DR ProteomicsDB; 79790; -. [Q9BZA7-3]
DR ProteomicsDB; 79791; -. [Q9BZA7-4]
DR ProteomicsDB; 79792; -. [Q9BZA7-5]
DR ProteomicsDB; 79793; -. [Q9BZA7-6]
DR ProteomicsDB; 79794; -. [Q9BZA7-7]
DR ProteomicsDB; 79795; -. [Q9BZA7-8]
DR Antibodypedia; 28445; 102 antibodies from 18 providers.
DR DNASU; 27328; -.
DR Ensembl; ENST00000361655.6; ENSP00000355105.2; ENSG00000102290.23. [Q9BZA7-4]
DR Ensembl; ENST00000373088.5; ENSP00000362180.1; ENSG00000102290.23. [Q9BZA7-5]
DR Ensembl; ENST00000373094.5; ENSP00000362186.1; ENSG00000102290.23. [Q9BZA7-1]
DR Ensembl; ENST00000373097.5; ENSP00000362189.1; ENSG00000102290.23. [Q9BZA7-3]
DR Ensembl; ENST00000406881.3; ENSP00000384758.1; ENSG00000102290.23. [Q9BZA7-8]
DR Ensembl; ENST00000504220.6; ENSP00000423762.1; ENSG00000102290.23. [Q9BZA7-6]
DR Ensembl; ENST00000682573.1; ENSP00000507225.1; ENSG00000102290.23. [Q9BZA7-1]
DR GeneID; 27328; -.
DR KEGG; hsa:27328; -.
DR MANE-Select; ENST00000682573.1; ENSP00000507225.1; NM_032968.5; NP_116750.1.
DR UCSC; uc004efk.3; human. [Q9BZA7-1]
DR CTD; 27328; -.
DR DisGeNET; 27328; -.
DR GeneCards; PCDH11X; -.
DR HGNC; HGNC:8656; PCDH11X.
DR HPA; ENSG00000102290; Group enriched (brain, ovary).
DR MIM; 300246; gene.
DR neXtProt; NX_Q9BZA7; -.
DR OpenTargets; ENSG00000102290; -.
DR PharmGKB; PA32996; -.
DR VEuPathDB; HostDB:ENSG00000102290; -.
DR eggNOG; ENOG502QPMK; Eukaryota.
DR GeneTree; ENSGT00940000158335; -.
DR HOGENOM; CLU_006480_5_2_1; -.
DR InParanoid; Q9BZA7; -.
DR OMA; IHTRQVM; -.
DR PhylomeDB; Q9BZA7; -.
DR TreeFam; TF320624; -.
DR PathwayCommons; Q9BZA7; -.
DR SignaLink; Q9BZA7; -.
DR SIGNOR; Q9BZA7; -.
DR BioGRID-ORCS; 27328; 21 hits in 685 CRISPR screens.
DR ChiTaRS; PCDH11X; human.
DR GeneWiki; PCDH11X; -.
DR GenomeRNAi; 27328; -.
DR Pharos; Q9BZA7; Tbio.
DR PRO; PR:Q9BZA7; -.
DR Proteomes; UP000005640; Chromosome X.
DR RNAct; Q9BZA7; protein.
DR Bgee; ENSG00000102290; Expressed in cortical plate and 60 other tissues.
DR Genevisible; Q9BZA7; HS.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
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:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
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 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; SSF49313; 6.
DR PROSITE; PS00232; CADHERIN_1; 5.
DR PROSITE; PS50268; CADHERIN_2; 7.
PE 2: Evidence at transcript level;
KW Alternative splicing; Calcium; Cell adhesion; Cell membrane; Glycoprotein;
KW Membrane; Reference proteome; Repeat; Signal; Transmembrane;
KW Transmembrane helix.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..1347
FT /note="Protocadherin-11 X-linked"
FT /id="PRO_0000232758"
FT TOPO_DOM 24..812
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 813..833
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 834..1347
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 26..139
FT /note="Cadherin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 140..249
FT /note="Cadherin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 250..355
FT /note="Cadherin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 362..466
FT /note="Cadherin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 467..570
FT /note="Cadherin 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 571..673
FT /note="Cadherin 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT DOMAIN 677..795
FT /note="Cadherin 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00043"
FT REGION 1057..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1097..1116
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1326..1347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 48
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 54
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 344
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 553
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 773
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT VAR_SEQ 1012..1048
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.4, ECO:0000303|Ref.5"
FT /id="VSP_017979"
FT VAR_SEQ 1012..1025
FT /note="PMKEVVRSCTPMKE -> TDSRTSTIEICSEI (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11003707"
FT /id="VSP_017980"
FT VAR_SEQ 1012..1021
FT /note="PMKEVVRSCT -> VGIQVSNTTF (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:10644456,
FT ECO:0000303|PubMed:14727141"
FT /id="VSP_017981"
FT VAR_SEQ 1022..1347
FT /note="Missing (in isoform 7)"
FT /evidence="ECO:0000303|PubMed:10644456,
FT ECO:0000303|PubMed:14727141"
FT /id="VSP_017982"
FT VAR_SEQ 1026..1347
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:11003707"
FT /id="VSP_017983"
FT VAR_SEQ 1039..1048
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:12815422, ECO:0000303|Ref.5"
FT /id="VSP_017984"
FT VAR_SEQ 1049..1065
FT /note="SQRRVTFHLPEGSQESS -> TVLTSSSPSAMTLSYLD (in isoform
FT 6)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_017985"
FT VAR_SEQ 1066..1347
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_017986"
FT VAR_SEQ 1116..1123
FT /note="Missing (in isoform 8 and isoform 4)"
FT /evidence="ECO:0000303|Ref.5"
FT /id="VSP_017987"
FT VARIANT 42
FT /note="D -> G (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs1451414636)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036109"
FT VARIANT 1018
FT /note="R -> Q (in dbSNP:rs4252205)"
FT /id="VAR_048575"
FT CONFLICT 242..244
FT /note="TND -> PNA (in Ref. 4; AAK82655/AAK82656)"
FT /evidence="ECO:0000305"
FT CONFLICT 252
FT /note="T -> P (in Ref. 4; AAK82655/AAK82656)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1347 AA; 147558 MW; 0227FA6C521FDA84 CRC64;
MDLLSGTYIF AVLLACVVFH SGAQEKNYTI REEMPENVLI GDLLKDLNLS LIPNKSLTTA
MQFKLVYKTG DVPLIRIEED TGEIFTTGAR IDREKLCAGI PRDEHCFYEV EVAILPDEIF
RLVKIRFLIE DINDNAPLFP ATVINISIPE NSAINSKYTL PAAVDPDVGI NGVQNYELIK
SQNIFGLDVI ETPEGDKMPQ LIVQKELDRE EKDTYVMKVK VEDGGFPQRS STAILQVSVT
DTNDNHPVFK ETEIEVSIPE NAPVGTSVTQ LHATDADIGE NAKIHFSFSN LVSNIARRLF
HLNATTGLIT IKEPLDREET PNHKLLVLAS DGGLMPARAM VLVNVTDVND NVPSIDIRYI
VNPVNDTVVL SENIPLNTKI ALITVTDKDA DHNGRVTCFT DHEIPFRLRP VFSNQFLLET
AAYLDYESTK EYAIKLLAAD AGKPPLNQSA MLFIKVKDEN DNAPVFTQSF VTVSIPENNS
PGIQLTKVSA MDADSGPNAK INYLLGPDAP PEFSLDCRTG MLTVVKKLDR EKEDKYLFTI
LAKDNGVPPL TSNVTVFVSI IDQNDNSPVF THNEYNFYVP ENLPRHGTVG LITVTDPDYG
DNSAVTLSIL DENDDFTIDS QTGVIRPNIS FDREKQESYT FYVKAEDGGR VSRSSSAKVT
INVVDVNDNK PVFIVPPSNC SYELVLPSTN PGTVVFQVIA VDNDTGMNAE VRYSIVGGNT
RDLFAIDQET GNITLMEKCD VTDLGLHRVL VKANDLGQPD SLFSVVIVNL FVNESVTNAT
LINELVRKST EAPVTPNTEI ADVSSPTSDY VKILVAAVAG TITVVVVIFI TAVVRCRQAP
HLKAAQKNKQ NSEWATPNPE NRQMIMMKKK KKKKKHSPKN LLLNFVTIEE TKADDVDSDG
NRVTLDLPID LEEQTMGKYN WVTTPTTFKP DSPDLARHYK SASPQPAFQI QPETPLNSKH
HIIQELPLDN TFVACDSISK CSSSSSDPYS VSDCGYPVTT FEVPVSVHTR PPMKEVVRSC
TPMKESTTME IWIHPQPQRK SEGKVAGKSQ RRVTFHLPEG SQESSSDGGL GDHDAGSLTS
TSHGLPLGYP QEEYFDRATP SNRTEGDGNS DPESTFIPGL KKAAEITVQP TVEEASDNCT
QECLIYGHSD ACWMPASLDH SSSSQAQASA LCHSPPLSQA STQHHSPRVT QTIALCHSPP
VTQTIALCHS PPPIQVSALH HSPPLVQATA LHHSPPSAQA SALCYSPPLA QAAAISHSSP
LPQVIALHRS QAQSSVSLQQ GWVQGADGLC SVDQGVQGSA TSQFYTMSER LHPSDDSIKV
IPLTTFTPRQ QARPSRGDSP IMEEHPL
