PKHA7_MOUSE
ID PKHA7_MOUSE Reviewed; 1118 AA.
AC Q3UIL6; B6RSP2; B6RSP3; Q3TUE4; Q5XG70; Q8BYE3;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 2.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=Pleckstrin homology domain-containing family A member 7;
DE Short=PH domain-containing family A member 7;
DE AltName: Full=Heart adapter protein 1;
GN Name=Plekha7; Synonyms=Hadp1;
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] (ISOFORMS 2 AND 6).
RC STRAIN=C57BL/6J;
RA Wythe J.D., Urness L.D., Jones C.A., Jurynec M., Grunwald D.J.,
RA MacRae C.A., Li D.Y.;
RT "HADP1, a novel pleckstrin homology domain protein, is required for cardiac
RT contractility in zebrafish.";
RL Submitted (JAN-2008) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Head, Stomach, and Thymus;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC STRAIN=FVB/N; TISSUE=Mammary tumor;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-542 AND SER-609, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=16452087; DOI=10.1074/mcp.t500041-mcp200;
RA Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT "Comprehensive identification of phosphorylation sites in postsynaptic
RT density preparations.";
RL Mol. Cell. Proteomics 5:914-922(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-542; SER-601;
RP SER-609; SER-900 AND SER-904, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-1226 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-990
RP (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1180 (ISOFORM
RP 6), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533; SER-542; SER-601;
RP SER-609; SER-864; SER-868; SER-900 AND SER-904, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-1226 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-990 (ISOFORM 4), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
RP SER-1180 (ISOFORM 6), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=30463011; DOI=10.1016/j.celrep.2018.10.088;
RA Shah J., Rouaud F., Guerrera D., Vasileva E., Popov L.M., Kelley W.L.,
RA Rubinstein E., Carette J.E., Amieva M.R., Citi S.;
RT "A Dock-and-Lock Mechanism Clusters ADAM10 at Cell-Cell Junctions to
RT Promote alpha-Toxin Cytotoxicity.";
RL Cell Rep. 25:2132-2147(2018).
CC -!- FUNCTION: Required for zonula adherens biogenesis and maintenance. Acts
CC via its interaction with CAMSAP3, which anchors microtubules at their
CC minus-ends to zonula adherens, leading to the recruitment of KIFC3
CC kinesin to the junctional site (By similarity). Mediates docking of
CC ADAM10 to zonula adherens through a PDZD11-dependent interaction with
CC the ADAM10-binding protein TSPAN33 (PubMed:30463011).
CC {ECO:0000250|UniProtKB:Q6IQ23, ECO:0000269|PubMed:30463011}.
CC -!- SUBUNIT: Interacts with CAMSAP3 and CTNND1 (By similarity). Interacts
CC (via WW domains) with TSPAN33 (via cytoplasmic domain) and with PDZD11;
CC the interaction with TSPAN33 is dependent on PDZD11 being bound to
CC PLEKHA7 and facilitates the docking of ADAM10 to zonula adherens
CC through interaction of TSPAN33 with ADAM10 (PubMed:30463011).
CC {ECO:0000250|UniProtKB:Q6IQ23, ECO:0000269|PubMed:30463011}.
CC -!- SUBCELLULAR LOCATION: Cell junction, adherens junction
CC {ECO:0000269|PubMed:30463011}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome {ECO:0000250|UniProtKB:Q6IQ23}.
CC Note=Localizes to zonula adherens, recruited via its interaction with
CC CTNND1. {ECO:0000250|UniProtKB:Q6IQ23}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q3UIL6-1; Sequence=Displayed;
CC Name=2; Synonyms=HADP1a;
CC IsoId=Q3UIL6-2; Sequence=VSP_025596;
CC Name=3;
CC IsoId=Q3UIL6-3; Sequence=VSP_025595;
CC Name=4;
CC IsoId=Q3UIL6-4; Sequence=VSP_025593, VSP_025596;
CC Name=5;
CC IsoId=Q3UIL6-5; Sequence=VSP_044626, VSP_044627;
CC Name=6; Synonyms=HADP1b;
CC IsoId=Q3UIL6-6; Sequence=VSP_039544, VSP_025596;
CC -!- TISSUE SPECIFICITY: Expressed in kidney and lung (at protein level).
CC {ECO:0000269|PubMed:30463011}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAE36027.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE36027.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; EU380771; ACB38003.1; -; mRNA.
DR EMBL; EU380772; ACB38004.1; -; mRNA.
DR EMBL; AK040271; BAC30557.1; -; mRNA.
DR EMBL; AK146866; BAE27490.1; -; mRNA.
DR EMBL; AK160810; BAE36027.1; ALT_FRAME; mRNA.
DR EMBL; BC084587; AAH84587.1; -; mRNA.
DR CCDS; CCDS40099.1; -. [Q3UIL6-4]
DR CCDS; CCDS80791.1; -. [Q3UIL6-3]
DR CCDS; CCDS85395.1; -. [Q3UIL6-5]
DR CCDS; CCDS85396.1; -. [Q3UIL6-6]
DR CCDS; CCDS85397.1; -. [Q3UIL6-2]
DR RefSeq; NP_001292114.1; NM_001305185.1. [Q3UIL6-2]
DR RefSeq; NP_001292115.1; NM_001305186.1. [Q3UIL6-6]
DR RefSeq; NP_001292118.1; NM_001305189.1. [Q3UIL6-3]
DR RefSeq; NP_001292119.1; NM_001305190.1. [Q3UIL6-5]
DR RefSeq; NP_766331.1; NM_172743.3. [Q3UIL6-4]
DR AlphaFoldDB; Q3UIL6; -.
DR SMR; Q3UIL6; -.
DR BioGRID; 231441; 2.
DR IntAct; Q3UIL6; 1.
DR STRING; 10090.ENSMUSP00000081714; -.
DR iPTMnet; Q3UIL6; -.
DR PhosphoSitePlus; Q3UIL6; -.
DR EPD; Q3UIL6; -.
DR jPOST; Q3UIL6; -.
DR MaxQB; Q3UIL6; -.
DR PaxDb; Q3UIL6; -.
DR PeptideAtlas; Q3UIL6; -.
DR PRIDE; Q3UIL6; -.
DR ProteomicsDB; 289902; -. [Q3UIL6-1]
DR ProteomicsDB; 289903; -. [Q3UIL6-2]
DR ProteomicsDB; 289904; -. [Q3UIL6-3]
DR ProteomicsDB; 289905; -. [Q3UIL6-4]
DR ProteomicsDB; 289906; -. [Q3UIL6-5]
DR ProteomicsDB; 289907; -. [Q3UIL6-6]
DR Antibodypedia; 42457; 124 antibodies from 19 providers.
DR DNASU; 233765; -.
DR Ensembl; ENSMUST00000084664; ENSMUSP00000081714; ENSMUSG00000045659. [Q3UIL6-4]
DR Ensembl; ENSMUST00000181981; ENSMUSP00000138766; ENSMUSG00000045659. [Q3UIL6-3]
DR Ensembl; ENSMUST00000181998; ENSMUSP00000138575; ENSMUSG00000045659. [Q3UIL6-2]
DR Ensembl; ENSMUST00000182487; ENSMUSP00000138214; ENSMUSG00000045659. [Q3UIL6-1]
DR Ensembl; ENSMUST00000182511; ENSMUSP00000138544; ENSMUSG00000045659. [Q3UIL6-5]
DR Ensembl; ENSMUST00000182834; ENSMUSP00000138257; ENSMUSG00000045659. [Q3UIL6-6]
DR GeneID; 233765; -.
DR KEGG; mmu:233765; -.
DR UCSC; uc009jiy.2; mouse. [Q3UIL6-4]
DR UCSC; uc009jiz.3; mouse. [Q3UIL6-2]
DR UCSC; uc009jja.1; mouse. [Q3UIL6-6]
DR UCSC; uc009jjc.2; mouse. [Q3UIL6-1]
DR CTD; 144100; -.
DR MGI; MGI:2445094; Plekha7.
DR VEuPathDB; HostDB:ENSMUSG00000045659; -.
DR eggNOG; KOG0940; Eukaryota.
DR GeneTree; ENSGT00940000155817; -.
DR HOGENOM; CLU_008216_0_0_1; -.
DR InParanoid; Q3UIL6; -.
DR OMA; NAWNEYT; -.
DR OrthoDB; 71844at2759; -.
DR PhylomeDB; Q3UIL6; -.
DR TreeFam; TF329090; -.
DR BioGRID-ORCS; 233765; 0 hits in 25 CRISPR screens.
DR ChiTaRS; Plekha7; mouse.
DR PRO; PR:Q3UIL6; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q3UIL6; protein.
DR Bgee; ENSMUSG00000045659; Expressed in placenta labyrinth and 219 other tissues.
DR ExpressionAtlas; Q3UIL6; baseline and differential.
DR Genevisible; Q3UIL6; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005911; C:cell-cell junction; IDA:ARUK-UCL.
DR GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0046930; C:pore complex; IMP:UniProtKB.
DR GO; GO:0005915; C:zonula adherens; ISS:UniProtKB.
DR GO; GO:0070097; F:delta-catenin binding; ISS:UniProtKB.
DR GO; GO:0044331; P:cell-cell adhesion mediated by cadherin; IMP:ARUK-UCL.
DR GO; GO:0090136; P:epithelial cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0046931; P:pore complex assembly; IMP:UniProtKB.
DR GO; GO:0045218; P:zonula adherens maintenance; ISS:UniProtKB.
DR CDD; cd13248; PH_PEPP1_2_3; 1.
DR CDD; cd00201; WW; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR001849; PH_domain.
DR InterPro; IPR040392; PKHA4-7_PH.
DR InterPro; IPR001202; WW_dom.
DR InterPro; IPR036020; WW_dom_sf.
DR Pfam; PF00169; PH; 1.
DR SMART; SM00233; PH; 1.
DR SMART; SM00456; WW; 2.
DR SUPFAM; SSF51045; SSF51045; 2.
DR PROSITE; PS50003; PH_DOMAIN; 1.
DR PROSITE; PS01159; WW_DOMAIN_1; 1.
DR PROSITE; PS50020; WW_DOMAIN_2; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Coiled coil; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1118
FT /note="Pleckstrin homology domain-containing family A
FT member 7"
FT /id="PRO_0000287693"
FT DOMAIN 8..41
FT /note="WW 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 53..86
FT /note="WW 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00224"
FT DOMAIN 163..281
FT /note="PH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00145"
FT REGION 100..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 334..512
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 528..629
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 535..693
FT /note="Interaction with CTNND1"
FT /evidence="ECO:0000250"
FT REGION 839..873
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 886..968
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1003..1024
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 697..798
FT /evidence="ECO:0000255"
FT COILED 1064..1091
FT /evidence="ECO:0000255"
FT COMPBIAS 111..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 451..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 496..512
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 564..582
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 583..597
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 915..939
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..968
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 533
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 542
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 566
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ23"
FT MOD_RES 601
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 605
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ23"
FT MOD_RES 609
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16452087,
FT ECO:0007744|PubMed:17242355, ECO:0007744|PubMed:21183079"
FT MOD_RES 857
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ23"
FT MOD_RES 864
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 867
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ23"
FT MOD_RES 868
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 900
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 904
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 983
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6IQ23"
FT VAR_SEQ 1..236
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_025593"
FT VAR_SEQ 1..105
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_025595"
FT VAR_SEQ 1..73
FT /note="MAAAVGRDTLPEHWSYGVCRDGRVFFINDQLRCTTWLHPRTGEPVNSGHMIR
FT SDLPRGWEEGFTEEGASFFID -> MEPWRCPPRDARPAALGFWGEPLAVCS (in
FT isoform 6)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_039544"
FT VAR_SEQ 1..62
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_044626"
FT VAR_SEQ 63..73
FT /note="FTEEGASFFID -> MSLRSTWATVC (in isoform 5)"
FT /evidence="ECO:0000305"
FT /id="VSP_044627"
FT VAR_SEQ 1116..1118
FT /note="SVC -> SWKREQEFDLQLLERAAQGDRKDKEEGWLKVQATPVMELDLEPQD
FT YDLDISRELSKPEKVSIPERYVELDPEEPPSLEELQARYQKAEKIRNILARSSMCNLQP
FT LGQDRNSLADLDSQLQEQERIINISYALASEASKRSKQVAAQAITDP (in isoform
FT 2, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:16141072, ECO:0000303|Ref.1"
FT /id="VSP_025596"
FT MOD_RES Q3UIL6-2:1226
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UIL6-4:990
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES Q3UIL6-6:1180
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1118 AA; 126742 MW; 6CCCE91B582ED368 CRC64;
MAAAVGRDTL PEHWSYGVCR DGRVFFINDQ LRCTTWLHPR TGEPVNSGHM IRSDLPRGWE
EGFTEEGASF FIDHNQQTTT FRHPVTGQFS SENSEYVLRE EPHPHMSKPE RNQRPSSMVS
ETSTAGTTST LEAKPGPKIV KSSSKVHSFG KRDQAIRRNL NVPVVVRGWL HKQDSSGMRL
WKRRWFVLAD YCLFYYKDSR EEAVLGSIPL PSYVISPVAP EDRISRKYSF KAVHTGMRAL
IYSTTTAGSQ MEHSGMRTYY FSADTLEDMN AWVRAMNQAA QVLSRSSLRR DVDKVERQAM
PQANHTDACQ ECGHVGPGHS RDCPRRGYED SYGFNRREQE EERFRAQRDP LEGRRDRSKA
RSPYLPAEED ALFVDLPGGP RGQQAQPQRA EKNGVPPYGL GEQNGTNGYQ RTAPPRANPE
KHSQRKTGLA QAEHWTKAQK GDGRSLPLDQ TLPRQGPSQP LSFPENYQSL PKSTRHLSGS
SSPPPRNLPS DYKYAQDRAS HLKMSSEERR AHRDGTVWQL YEWQQRQQFR HGSPTAPIGA
GSPEFTEQGR SRSLLEVPRS ISVPPSPSDI PPPGPPRPFP PRRPHTPAER VTVKPPEQRR
SVDISLGGSP RKARGHAAKN SSHVDRRSMP SMGYMTHTVS APSLHGKSAD DTYLQLKKDL
EYLDLKMTGR DLLKDRSLKP MKIAESDIDV KLSIFCEQDR ILQDLEDKIR ALKENKDQLE
SVLEVLHRQT EQYRDQPQHL EKITCQQRLL QEDLVHIRAE LCRESTEMEN AWNEYLKLEK
DVEQLKQTLQ EQHRRAFFFQ EKSQIQKDLW RIEDVMAGLS ANKENYRVLV GSVKNPERKT
VPLFPHPSVP SLSPTESKPA LQPSPPTSPV RTPLEVRLFP QLQTYVPYRP HPPQLRKVMS
PLQSPTKAKP QAEDEAPPRP PLPELYSPED QPPAVPPLPR EATIIRHTSV RGLKRQSDER
KRDREQGQCV NGDLKVELRS YVSEPELASL SGDVPQPSLS LVGSESRYQT LPGRGLSGST
SRLQQSSTIA PYVTLRRGLN AENSSATFSR PKSALERLYS GDHQRGKMSA EEQLERMKRH
QKALVRERKR TLSQGEKTGL LSARYLSQPL PGDLGSVC
