NPHP1_CANLF
ID NPHP1_CANLF Reviewed; 565 AA.
AC Q9TU19;
DT 16-NOV-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 25-MAY-2022, entry version 103.
DE RecName: Full=Nephrocystin-1;
DE Flags: Fragment;
GN Name=NPHP1; Synonyms=NPH1;
OS Canis lupus familiaris (Dog) (Canis familiaris).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX NCBI_TaxID=9615;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=Cocker spaniel; TISSUE=Kidney;
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 [2]
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).
CC -!- FUNCTION: Together with BCAR1 it may play a role in the control of
CC epithelial cell polarity (By similarity). Involved in the organization
CC of apical junctions in kidney cells together with NPHP4 and
CC RPGRIP1L/NPHP8 (By similarity). Does not seem to be strictly required
CC for ciliogenesis (By similarity). Seems to help to recruit PTK2B/PYK2
CC to cell matrix adhesions, thereby initiating phosphorylation of
CC PTK2B/PYK2 and PTK2B/PYK2-dependent signaling (By similarity). May play
CC a role in the regulation of intraflagellar transport (IFT) during cilia
CC assembly (By similarity). Required for normal retina development (By
CC similarity). In connecting photoreceptor cilia influences the movement
CC of some IFT proteins such as IFT88 and WDR19. Involved in
CC spermatogenesis (By similarity). {ECO:0000250|UniProtKB:Q9QY53}.
CC -!- SUBUNIT: Interacts with Crk-associated substrate BCAR1, NPHP4,
CC PTK2B/PYK2 and tensin. Interacts with INVS and NPHP3. Interacts with
CC AHI1 and TNK2 (By similarity). Interacts with NPHP4 in a complex
CC containing NPHP1, NPHP4 and RPGRIP1L/NPHP8 (By similarity). Interacts
CC with IQCB1; the interaction likely requires additional interactors (By
CC similarity). Interacts with KIF7 (By similarity). Interacts with ANKS3
CC (By similarity). Interacts with SPATA7 (By similarity). Interacts with
CC FLNA (By similarity). {ECO:0000250|UniProtKB:O15259,
CC ECO:0000250|UniProtKB:Q9QY53}.
CC -!- SUBCELLULAR LOCATION: Cell junction {ECO:0000250|UniProtKB:Q9QY53}.
CC Cell junction, adherens junction {ECO:0000250|UniProtKB:Q9QY53}. Cell
CC projection, cilium {ECO:0000269|PubMed:16885411}. Cytoplasm,
CC cytoskeleton, cilium axoneme {ECO:0000250|UniProtKB:O15259}. Cell
CC junction, tight junction {ECO:0000250|UniProtKB:Q9QY53}. Note=In the
CC retinal photoreceptor cell layer, localizes at the connecting cilium
CC (By similarity). Colocalizes with E-cadherin and BCAR1 at or near the
CC cell-cell adherens junctions (By similarity). Localizes to respiratory
CC cilia axoneme (By similarity). Localized to the transition zone of
CC respiratory cilia (By similarity). Localized to the transition zone of
CC photoreceptor-connecting cilia and renal monocilia (By similarity). In
CC cultured renal cells, it localizes diffusely in the cytoplasm but, as
CC cells approach confluence, it accumulates to basolateral tight
CC junctions (By similarity). {ECO:0000250|UniProtKB:Q9QY53}.
CC -!- TISSUE SPECIFICITY: Expressed in renal cells (at protein level).
CC {ECO:0000269|PubMed:10739664, ECO:0000269|PubMed:16885411}.
CC -!- DOMAIN: The SH3 domain mediates the stable interaction with Cas.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the nephrocystin-1 family. {ECO:0000305}.
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DR EMBL; AF177536; AAD54337.1; -; mRNA.
DR AlphaFoldDB; Q9TU19; -.
DR SMR; Q9TU19; -.
DR IntAct; Q9TU19; 1.
DR STRING; 9615.ENSCAFP00000010483; -.
DR PaxDb; Q9TU19; -.
DR eggNOG; ENOG502QU7K; Eukaryota.
DR InParanoid; Q9TU19; -.
DR Proteomes; UP000002254; Unplaced.
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:0005929; C:cilium; IBA:GO_Central.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-KW.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0030030; P:cell projection organization; IEA:UniProtKB-KW.
DR GO; GO:0090251; P:protein localization involved in establishment of planar polarity; IBA:GO_Central.
DR GO; GO:0007283; P:spermatogenesis; IEA:UniProtKB-KW.
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 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..565
FT /note="Nephrocystin-1"
FT /id="PRO_0000159584"
FT DOMAIN 40..100
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..46
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 95..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 2..48
FT /evidence="ECO:0000255"
FT COMPBIAS 1..30
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..121
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 14
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O15259"
FT MOD_RES 182
FT /note="Phosphotyrosine; by FAK2"
FT /evidence="ECO:0000250|UniProtKB:O15259"
FT MOD_RES 554
FT /note="Phosphotyrosine; by SRC"
FT /evidence="ECO:0000250|UniProtKB:O15259"
FT NON_TER 1
SQ SEQUENCE 565 AA; 63961 MW; 10C2433F4951E88A CRC64;
GEEEDEEEEE EEESEEGGGE EEESEEEEEE KQENESHHQA TSKEYIAVGD FTAQQAGDLT
FKKREILLII EKKPDGWWIA KNAKGNKGLI PRTYVEPYNK EEGQDTSEEE DSEEDVEVGD
QTAGGEEVKQ RTDSHWSAVQ KAISEQINTV DVLTTMGAIP AGFRPSTLFQ LLEEGNQFRA
SYFLQPELTP SQLAFRDLMW DAKTGTIRSR PSRVSFILTL WSCKMIPLPG TSIQVLSRHV
RLCIFDGNKV LSNIHTVRAT WQSKKPKTWT FSPQVTGILP CLLDGDCFIR SNSSSPDLGI
LFELGISYIR NSTGERGELS CGWVFLKLFD ASGIPIPAKT YELFLNGGTP YEKGVEVDPS
VSRRAYGSVF HQMMTMRRQP QLLVKLRSLN RRSRDLLSLL PETLIGSMCT IHLLIFYRQI
LGDVLLKDRT SMQSADLISN PVLATFPKLL EQPDMMDALR SSWAEKESTL KRSEKRDKEF
LKAMFLLVYH DCVVPLLHST LLPPFRWAEE ETEAARWKVI ADFLKQNQEN GGALQALLSP
DGVHEPFDIS EQTYDLLGEI RKNVA
