NPHP1_MOUSE
ID NPHP1_MOUSE Reviewed; 687 AA.
AC Q9QY53; Q9D7G8; Q9QZP0; Q9WUZ2;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Nephrocystin-1;
GN Name=Nphp1; Synonyms=Nph1;
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], TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Diaphragm;
RX PubMed=10665934; DOI=10.1681/asn.v112270;
RA Otto E., Kispert A., Schaetzle S., Lescher B., Rensing C., Hildebrandt F.;
RT "Nephrocystin: gene expression and sequence conservation between human,
RT mouse, and Caenorhabditis elegans.";
RL J. Am. Soc. Nephrol. 11:270-282(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH BCAR1, AND SUBCELLULAR
RP LOCATION.
RC TISSUE=Embryo;
RX PubMed=10739664; DOI=10.1006/excr.2000.4822;
RA Donaldson J.C., Dempsey P.J., Reddy S., Bouton A.H., Coffey R.J.,
RA Hanks S.K.;
RT "Crk-associated substrate p130(Cas) interacts with nephrocystin and both
RT proteins localize to cell-cell contacts of polarized epithelial cells.";
RL Exp. Cell Res. 256:168-178(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Silbermann F., Benessy F., Saunier S., Mollet G., Antignac C.;
RT "Identification of the mouse Nph1 gene.";
RL Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 569-687.
RC STRAIN=C57BL/6J; TISSUE=Tongue;
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 [5]
RP FUNCTION, AND INTERACTION WITH PTK2B; BCAR1 AND TENSIN.
RX PubMed=11493697; DOI=10.1073/pnas.171269898;
RA Benzing T., Gerke P., Hoepker K., Hildebrandt F., Kim E., Walz G.;
RT "Nephrocystin interacts with Pyk2, p130(Cas), and tensin and triggers
RT phosphorylation of Pyk2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:9784-9789(2001).
RN [6]
RP INTERACTION WITH FLNA, SUBCELLULAR LOCATION, AND DOMAIN.
RX PubMed=12006559; DOI=10.1074/jbc.m111697200;
RA Donaldson J.C., Dise R.S., Ritchie M.D., Hanks S.K.;
RT "Nephrocystin-conserved domains involved in targeting to epithelial cell-
RT cell junctions, interaction with filamins, and establishing cell
RT polarity.";
RL J. Biol. Chem. 277:29028-29035(2002).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16885411; DOI=10.1681/asn.2005121351;
RA Fliegauf M., Horvath J., von Schnakenburg C., Olbrich H., Mueller D.,
RA Thumfart J., Schermer B., Pazour G.J., Neumann H.P., Zentgraf H.,
RA Benzing T., Omran H.;
RT "Nephrocystin specifically localizes to the transition zone of renal and
RT respiratory cilia and photoreceptor connecting cilia.";
RL J. Am. Soc. Nephrol. 17:2424-2433(2006).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=18477472; DOI=10.1016/j.bbrc.2008.05.016;
RA Eley L., Moochhala S.H., Simms R., Hildebrandt F., Sayer J.A.;
RT "Nephrocystin-1 interacts directly with Ack1 and is expressed in human
RT collecting duct.";
RL Biochem. Biophys. Res. Commun. 371:877-882(2008).
RN [9]
RP FUNCTION, DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=18684731; DOI=10.1093/hmg/ddn231;
RA Jiang S.T., Chiou Y.Y., Wang E., Lin H.K., Lee S.P., Lu H.Y., Wang C.K.,
RA Tang M.J., Li H.;
RT "Targeted disruption of Nphp1 causes male infertility due to defects in the
RT later steps of sperm morphogenesis in mice.";
RL Hum. Mol. Genet. 17:3368-3379(2008).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=19208653; DOI=10.1093/hmg/ddp068;
RA Jiang S.T., Chiou Y.Y., Wang E., Chien Y.L., Ho H.H., Tsai F.J., Lin C.Y.,
RA Tsai S.P., Li H.;
RT "Essential role of nephrocystin in photoreceptor intraflagellar transport
RT in mouse.";
RL Hum. Mol. Genet. 18:1566-1577(2009).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [12]
RP INTERACTION WITH PKD1.
RX PubMed=20856870; DOI=10.1371/journal.pone.0012719;
RA Wodarczyk C., Distefano G., Rowe I., Gaetani M., Bricoli B., Muorah M.,
RA Spitaleri A., Mannella V., Ricchiuto P., Pema M., Castelli M.,
RA Casanova A.E., Mollica L., Banzi M., Boca M., Antignac C., Saunier S.,
RA Musco G., Boletta A.;
RT "Nephrocystin-1 forms a complex with polycystin-1 via a polyproline
RT motif/SH3 domain interaction and regulates the apoptotic response in
RT mammals.";
RL PLoS ONE 5:E12719-E12719(2010).
RN [13]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=21565611; DOI=10.1016/j.cell.2011.04.019;
RA Sang L., Miller J.J., Corbit K.C., Giles R.H., Brauer M.J., Otto E.A.,
RA Baye L.M., Wen X., Scales S.J., Kwong M., Huntzicker E.G., Sfakianos M.K.,
RA Sandoval W., Bazan J.F., Kulkarni P., Garcia-Gonzalo F.R., Seol A.D.,
RA O'Toole J.F., Held S., Reutter H.M., Lane W.S., Rafiq M.A., Noor A.,
RA Ansar M., Devi A.R., Sheffield V.C., Slusarski D.C., Vincent J.B.,
RA Doherty D.A., Hildebrandt F., Reiter J.F., Jackson P.K.;
RT "Mapping the NPHP-JBTS-MKS protein network reveals ciliopathy disease genes
RT and pathways.";
RL Cell 145:513-528(2011).
RN [14]
RP INTERACTION WITH ANKS3.
RX PubMed=25671767; DOI=10.1038/ki.2015.17;
RA Yakulov T.A., Yasunaga T., Ramachandran H., Engel C., Mueller B., Hoff S.,
RA Dengjel J., Lienkamp S.S., Walz G.;
RT "Anks3 interacts with nephronophthisis proteins and is required for normal
RT renal development.";
RL Kidney Int. 87:1191-1200(2015).
RN [15]
RP INTERACTION WITH SPATA7, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=29899041; DOI=10.1083/jcb.201712117;
RA Dharmat R., Eblimit A., Robichaux M.A., Zhang Z., Nguyen T.T., Jung S.Y.,
RA He F., Jain A., Li Y., Qin J., Overbeek P., Roepman R., Mardon G.,
RA Wensel T.G., Chen R.;
RT "SPATA7 maintains a novel photoreceptor-specific zone in the distal
RT connecting cilium.";
RL J. Cell Biol. 217:2851-2865(2018).
CC -!- FUNCTION: Together with BCAR1 it may play a role in the control of
CC epithelial cell polarity. Involved in the organization of apical
CC junctions in kidney cells, together with NPHP4 and RPGRIP1L/NPHP8
CC (PubMed:21565611). Does not seem to be strictly required for
CC ciliogenesis (PubMed:19208653). Seems to help to recruit PTK2B/PYK2 to
CC cell matrix adhesions, thereby initiating phosphorylation of PTK2B/PYK2
CC and PTK2B/PYK2-dependent signaling (PubMed:11493697). May play a role
CC in the regulation of intraflagellar transport (IFT) during cilia
CC assembly (PubMed:19208653). Required for normal retina development
CC (PubMed:19208653). In connecting photoreceptor cilia influences the
CC movement of some IFT proteins such as IFT88 and WDR19
CC (PubMed:19208653). Involved in spermatogenesis; required for the
CC differentiation of early elongating spermatids into spermatozoa
CC (PubMed:18684731). {ECO:0000269|PubMed:11493697,
CC ECO:0000269|PubMed:18684731, ECO:0000269|PubMed:19208653,
CC ECO:0000269|PubMed:21565611}.
CC -!- SUBUNIT: Interacts with INVS and NPHP3 (By similarity). Interacts with
CC Crk-associated substrate BCAR1 (PubMed:10739664, PubMed:11493697).
CC Interacts with NPHP4 (By similarity). Interacts with PTK2B/PYK2 and
CC tensin (PubMed:11493697). Interacts with AHI1 and TNK2 (By similarity).
CC Interacts with NPHP4 in a complex containing NPHP1, NPHP4 and
CC RPGRIP1L/NPHP8 (By similarity). Interacts with IQCB1; the interaction
CC likely requires additional interactors (By similarity). Interacts (via
CC SH3 domain) with PKD1 (PubMed:20856870). Interacts with KIF7 (By
CC similarity). Interacts with ANKS3 (PubMed:25671767). Interacts with
CC SPATA7 (PubMed:29899041). Interacts with FLNA (PubMed:12006559).
CC {ECO:0000250|UniProtKB:O15259, ECO:0000269|PubMed:10739664,
CC ECO:0000269|PubMed:11493697, ECO:0000269|PubMed:12006559,
CC ECO:0000269|PubMed:20856870, ECO:0000269|PubMed:25671767,
CC ECO:0000269|PubMed:29899041}.
CC -!- INTERACTION:
CC Q9QY53; Q61140: Bcar1; NbExp=2; IntAct=EBI-77230, EBI-77088;
CC Q9QY53; P59240: Nphp4; NbExp=8; IntAct=EBI-77230, EBI-4281265;
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000269|PubMed:12006559,
CC ECO:0000269|PubMed:18477472}. Cell junction, adherens junction
CC {ECO:0000250|UniProtKB:Q9TU19}. Cell projection, cilium
CC {ECO:0000269|PubMed:16885411, ECO:0000269|PubMed:19208653,
CC ECO:0000269|PubMed:29899041}. Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000269|PubMed:19208653}. Cell junction, tight junction
CC {ECO:0000269|PubMed:10739664}. Note=In the retinal photoreceptor cell
CC layer, localizes at the connecting cilium (PubMed:19208653,
CC PubMed:29899041). Colocalizes with E-cadherin and BCAR1 at or near the
CC cell-cell adherens junctions (PubMed:10739664). Localizes to
CC respiratory cilia axoneme (PubMed:16885411). Localized to the
CC transition zone of respiratory cilia (PubMed:16885411). Localized to
CC the transition zone of photoreceptor-connecting cilia and renal
CC monocilia (PubMed:16885411). In cultured renal cells, it localizes
CC diffusely in the cytoplasm but, as cells approach confluence, it
CC accumulates at basolateral tight junctions (PubMed:21565611).
CC {ECO:0000269|PubMed:10739664, ECO:0000269|PubMed:16885411,
CC ECO:0000269|PubMed:19208653, ECO:0000269|PubMed:21565611,
CC ECO:0000269|PubMed:29899041}.
CC -!- TISSUE SPECIFICITY: Expressed in the retina (at protein level)
CC (PubMed:16885411, PubMed:19208653, PubMed:29899041). Expressed in the
CC testis (at protein level) (PubMed:10665934). Widespread expression,
CC with weak expression in skeletal muscle, kidney, thyroid, ovary, lung,
CC prostate, thymus, uterus, heart, and liver (PubMed:10665934). Lowest
CC levels in brain and spleen (PubMed:10665934).
CC {ECO:0000269|PubMed:10665934, ECO:0000269|PubMed:16885411,
CC ECO:0000269|PubMed:19208653, ECO:0000269|PubMed:29899041}.
CC -!- DEVELOPMENTAL STAGE: Widespread and uniform expression in whole embryo
CC at all development stages (PubMed:10665934). Expressed in cell stages
CC of the first meiotic division and thereafter (PubMed:10665934).
CC Initially expressed at day 14 with consistent expression thereafter to
CC day 365 (PubMed:18684731). {ECO:0000269|PubMed:10665934,
CC ECO:0000269|PubMed:18684731}.
CC -!- DOMAIN: The SH3 domain mediates the stable interaction with Cas and is
CC involved in establishing tight junctions in epithelial cells.
CC {ECO:0000269|PubMed:12006559}.
CC -!- DISRUPTION PHENOTYPE: Mice are viable without renal manifestations of
CC nephronophthisis (PubMed:18684731). Male mice are infertile with
CC oligoteratozoospermia (PubMed:18684731). Spermatogenesis is blocked at
CC the early stages of spermatid elongation, with degenerating spermatids
CC sloughing off into the lumen (PubMed:18684731). Early elongating
CC spermatids are detached from Sertoli cells and show a failure of sperm
CC head and tail morphogenesis and an abnormal F-actin distribution
CC (PubMed:18684731). Severe retinal degradation with mislocalized
CC rhodopsin, disorganized outer segments, restricted expression of
CC transducin to the inner segment and abnormal intraflagellar transport
CC (IFT) of IFT57 (PubMed:19208653). {ECO:0000269|PubMed:18684731,
CC ECO:0000269|PubMed:19208653}.
CC -!- SIMILARITY: Belongs to the nephrocystin-1 family. {ECO:0000305}.
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DR EMBL; AF127180; AAF22134.1; -; mRNA.
DR EMBL; AF176210; AAD54311.1; -; mRNA.
DR EMBL; AJ243223; CAB45687.1; -; mRNA.
DR EMBL; AK009252; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_058598.1; NM_016902.4.
DR AlphaFoldDB; Q9QY53; -.
DR SMR; Q9QY53; -.
DR BioGRID; 207511; 56.
DR CORUM; Q9QY53; -.
DR IntAct; Q9QY53; 45.
DR MINT; Q9QY53; -.
DR STRING; 10090.ENSMUSP00000028857; -.
DR iPTMnet; Q9QY53; -.
DR PhosphoSitePlus; Q9QY53; -.
DR MaxQB; Q9QY53; -.
DR PaxDb; Q9QY53; -.
DR PRIDE; Q9QY53; -.
DR ProteomicsDB; 293951; -.
DR DNASU; 53885; -.
DR GeneID; 53885; -.
DR KEGG; mmu:53885; -.
DR CTD; 4867; -.
DR MGI; MGI:1858233; Nphp1.
DR eggNOG; ENOG502QU7K; Eukaryota.
DR InParanoid; Q9QY53; -.
DR OrthoDB; 676699at2759; -.
DR Reactome; R-MMU-5620912; Anchoring of the basal body to the plasma membrane.
DR BioGRID-ORCS; 53885; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Nphp1; mouse.
DR PRO; PR:Q9QY53; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q9QY53; protein.
DR GO; GO:0005912; C:adherens junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0097546; C:ciliary base; IDA:MGI.
DR GO; GO:0035869; C:ciliary transition zone; IDA:MGI.
DR GO; GO:0005929; C:cilium; IDA:MGI.
DR GO; GO:0005737; C:cytoplasm; IDA:CACAO.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0031514; C:motile cilium; ISS:UniProtKB.
DR GO; GO:0032391; C:photoreceptor connecting cilium; IDA:UniProtKB.
DR GO; GO:0120206; C:photoreceptor distal connecting cilium; IDA:MGI.
DR GO; GO:0030030; P:cell projection organization; IMP:UniProtKB.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; IGI:UniProtKB.
DR GO; GO:1903348; P:positive regulation of bicellular tight junction assembly; ISO:MGI.
DR GO; GO:0008104; P:protein localization; IGI:UniProtKB.
DR GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IBA:GO_Central.
DR GO; GO:0060041; P:retina development in camera-type eye; IMP:UniProtKB.
DR GO; GO:0048515; P:spermatid differentiation; IMP:UniProtKB.
DR CDD; cd11770; SH3_Nephrocystin; 1.
DR InterPro; IPR039687; NPHP1.
DR InterPro; IPR030642; NPHP1_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR15176:SF1; PTHR15176:SF1; 1.
DR Pfam; PF00018; SH3_1; 1.
DR PRINTS; PR00452; SH3DOMAIN.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW Cell junction; Cell projection; Cilium; Cilium biogenesis/degradation;
KW Coiled coil; Cytoplasm; Cytoskeleton; Differentiation; Phosphoprotein;
KW Reference proteome; SH3 domain; Spermatogenesis; Tight junction.
FT CHAIN 1..687
FT /note="Nephrocystin-1"
FT /id="PRO_0000159586"
FT DOMAIN 155..215
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 111..154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..237
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 10..30
FT /evidence="ECO:0000255"
FT COILED 40..106
FT /evidence="ECO:0000255"
FT COMPBIAS 118..141
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..237
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 46
FT /note="Phosphotyrosine; by FAK2"
FT /evidence="ECO:0000250|UniProtKB:O15259"
FT MOD_RES 304
FT /note="Phosphotyrosine; by FAK2"
FT /evidence="ECO:0000250|UniProtKB:O15259"
FT CONFLICT 46
FT /note="Y -> C (in Ref. 3; CAB45687)"
FT /evidence="ECO:0000305"
FT CONFLICT 90
FT /note="E -> G (in Ref. 3; CAB45687)"
FT /evidence="ECO:0000305"
FT CONFLICT 210
FT /note="L -> W (in Ref. 3; CAB45687)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="D -> DGEED (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 296
FT /note="Missing (in Ref. 3; CAB45687)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="R -> K (in Ref. 3; CAB45687)"
FT /evidence="ECO:0000305"
FT CONFLICT 477
FT /note="V -> A (in Ref. 3; CAB45687)"
FT /evidence="ECO:0000305"
FT CONFLICT 549
FT /note="R -> K (in Ref. 3; CAB45687)"
FT /evidence="ECO:0000305"
FT CONFLICT 569..582
FT /note="PLLLEQPDVMDALR -> MNGALCCPLSLQEK (in Ref. 4)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 687 AA; 77035 MW; FAA10B044F5CE678 CRC64;
MLARRPRDPL QALRRRGQEL KLQVDSLVTE SQLTGALEPS KRREIYQRCI QLKQAVDENK
NTLQKLNKAD EAAPVGNYEQ RKEEEHSLLE KLACQLQELA VSISRKDALK VEAHSDKEED
DTTEDDEEET GGEEEESEGD GEGKQEQASP KQAETETVTY IALGDFAAQQ TGDLTFKKGD
VLHIIEKKPD GWWLAKDAEG VEGLIPRTYL EPYNKEDKLE SSEGSEEGGE EDGEEDVEVV
DETADGAQVK QRTDSHWSAV RKAISEQINT VDVLATMGAI PAGFRPSTLS QLLDEAGNQF
RASYFLQPEL TTSQLAFRDL TWDAKAGTIM SRPSRVSLIL TLWSCKMIPL PGTSIQVLSR
HIRLCLFDGS KVLSNIHTVR AVWQPKKPKT WTFSPQVTGI LPCLLDGDCF IRSNSSTPDL
GILFELGISY IRNSTGERGE LSCGWVFLKL FDASGVPIPA KTYELFLNGG TPYEKGVEVD
PSVSRRAQGS VFRQMISVRR QPQLLVKLRS LNRRSRAMLS LLPETLVGSM CSAHLLIFYR
QILGDVLLRD RTNLQSADLI SHPVLATFPL LLEQPDVMDA LRSSWSEKES TLKRAEKRDK
ELLKAEFLLV YHDCVLPLLH STLLPPFRWA EEETEAARWK AIADFLKQSR ENEGSLKALL
SPDGVHKPFD LSEQTFDFLG EIRKNSG
