INADL_RAT
ID INADL_RAT Reviewed; 1836 AA.
AC F1MAD2;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2015, sequence version 2.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=InaD-like protein {ECO:0000250|UniProtKB:Q8NI35};
DE Short=Inadl protein {ECO:0000250|UniProtKB:Q8NI35};
DE AltName: Full=Channel-interacting PDZ domain-containing protein {ECO:0000250|UniProtKB:Q63ZW7};
DE AltName: Full=Pals1-associated tight junction protein {ECO:0000250|UniProtKB:Q63ZW7};
DE AltName: Full=Protein associated to tight junctions {ECO:0000250|UniProtKB:Q8NI35};
GN Name=Patj {ECO:0000312|RGD:1565362};
GN Synonyms=Cipp {ECO:0000250|UniProtKB:Q63ZW7},
GN Inadl {ECO:0000250|UniProtKB:Q8NI35};
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116 {ECO:0000312|Proteomes:UP000002494};
RN [1] {ECO:0000312|Proteomes:UP000002494}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Brown Norway {ECO:0000312|Proteomes:UP000002494};
RX PubMed=15057822; DOI=10.1038/nature02426;
RA Gibbs R.A., Weinstock G.M., Metzker M.L., Muzny D.M., Sodergren E.J.,
RA Scherer S., Scott G., Steffen D., Worley K.C., Burch P.E., Okwuonu G.,
RA Hines S., Lewis L., Deramo C., Delgado O., Dugan-Rocha S., Miner G.,
RA Morgan M., Hawes A., Gill R., Holt R.A., Adams M.D., Amanatides P.G.,
RA Baden-Tillson H., Barnstead M., Chin S., Evans C.A., Ferriera S.,
RA Fosler C., Glodek A., Gu Z., Jennings D., Kraft C.L., Nguyen T.,
RA Pfannkoch C.M., Sitter C., Sutton G.G., Venter J.C., Woodage T., Smith D.,
RA Lee H.-M., Gustafson E., Cahill P., Kana A., Doucette-Stamm L.,
RA Weinstock K., Fechtel K., Weiss R.B., Dunn D.M., Green E.D.,
RA Blakesley R.W., Bouffard G.G., De Jong P.J., Osoegawa K., Zhu B., Marra M.,
RA Schein J., Bosdet I., Fjell C., Jones S., Krzywinski M., Mathewson C.,
RA Siddiqui A., Wye N., McPherson J., Zhao S., Fraser C.M., Shetty J.,
RA Shatsman S., Geer K., Chen Y., Abramzon S., Nierman W.C., Havlak P.H.,
RA Chen R., Durbin K.J., Egan A., Ren Y., Song X.-Z., Li B., Liu Y., Qin X.,
RA Cawley S., Cooney A.J., D'Souza L.M., Martin K., Wu J.Q.,
RA Gonzalez-Garay M.L., Jackson A.R., Kalafus K.J., McLeod M.P.,
RA Milosavljevic A., Virk D., Volkov A., Wheeler D.A., Zhang Z., Bailey J.A.,
RA Eichler E.E., Tuzun E., Birney E., Mongin E., Ureta-Vidal A., Woodwark C.,
RA Zdobnov E., Bork P., Suyama M., Torrents D., Alexandersson M., Trask B.J.,
RA Young J.M., Huang H., Wang H., Xing H., Daniels S., Gietzen D., Schmidt J.,
RA Stevens K., Vitt U., Wingrove J., Camara F., Mar Alba M., Abril J.F.,
RA Guigo R., Smit A., Dubchak I., Rubin E.M., Couronne O., Poliakov A.,
RA Huebner N., Ganten D., Goesele C., Hummel O., Kreitler T., Lee Y.-A.,
RA Monti J., Schulz H., Zimdahl H., Himmelbauer H., Lehrach H., Jacob H.J.,
RA Bromberg S., Gullings-Handley J., Jensen-Seaman M.I., Kwitek A.E.,
RA Lazar J., Pasko D., Tonellato P.J., Twigger S., Ponting C.P., Duarte J.M.,
RA Rice S., Goodstadt L., Beatson S.A., Emes R.D., Winter E.E., Webber C.,
RA Brandt P., Nyakatura G., Adetobi M., Chiaromonte F., Elnitski L.,
RA Eswara P., Hardison R.C., Hou M., Kolbe D., Makova K., Miller W.,
RA Nekrutenko A., Riemer C., Schwartz S., Taylor J., Yang S., Zhang Y.,
RA Lindpaintner K., Andrews T.D., Caccamo M., Clamp M., Clarke L., Curwen V.,
RA Durbin R.M., Eyras E., Searle S.M., Cooper G.M., Batzoglou S., Brudno M.,
RA Sidow A., Stone E.A., Payseur B.A., Bourque G., Lopez-Otin C., Puente X.S.,
RA Chakrabarti K., Chatterji S., Dewey C., Pachter L., Bray N., Yap V.B.,
RA Caspi A., Tesler G., Pevzner P.A., Haussler D., Roskin K.M., Baertsch R.,
RA Clawson H., Furey T.S., Hinrichs A.S., Karolchik D., Kent W.J.,
RA Rosenbloom K.R., Trumbower H., Weirauch M., Cooper D.N., Stenson P.D.,
RA Ma B., Brent M., Arumugam M., Shteynberg D., Copley R.R., Taylor M.S.,
RA Riethman H., Mudunuri U., Peterson J., Guyer M., Felsenfeld A., Old S.,
RA Mockrin S., Collins F.S.;
RT "Genome sequence of the Brown Norway rat yields insights into mammalian
RT evolution.";
RL Nature 428:493-521(2004).
RN [2] {ECO:0007744|PubMed:22673903}
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
RN [3] {ECO:0000305}
RP TISSUE SPECIFICITY.
RX PubMed=18621709; DOI=10.1073/pnas.0801527105;
RA Wong E.W., Mruk D.D., Lee W.M., Cheng C.Y.;
RT "Par3/Par6 polarity complex coordinates apical ectoplasmic specialization
RT and blood-testis barrier restructuring during spermatogenesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:9657-9662(2008).
RN [4] {ECO:0000305}
RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 1-68 IN COMPLEX WITH MOUSE LIN7B
RP AND HUMAN PALS1.
RX PubMed=22337881; DOI=10.1074/jbc.m111.321216;
RA Zhang J., Yang X., Wang Z., Zhou H., Xie X., Shen Y., Long J.;
RT "Structure of an L27 domain heterotrimer from cell polarity complex
RT Patj/Pals1/Mals2 reveals mutually independent L27 domain assembly mode.";
RL J. Biol. Chem. 287:11132-11140(2012).
CC -!- FUNCTION: Scaffolding protein that facilitates the localization of
CC proteins to the cell membrane (By similarity). Required for the correct
CC formation of tight junctions and epithelial apico-basal polarity (By
CC similarity). Positively regulates epithelial cell microtubule
CC elongation and cell migration, possibly via facilitating localization
CC of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of migrating cells (By
CC similarity). Plays a role in the correct reorientation of the
CC microtubule-organizing center during epithelial migration (By
CC similarity). May regulate the surface expression and/or function of
CC ASIC3 in sensory neurons (By similarity). May recruit ARHGEF18 to
CC apical cell-cell boundaries (By similarity).
CC {ECO:0000250|UniProtKB:E2QYC9, ECO:0000250|UniProtKB:Q63ZW7,
CC ECO:0000250|UniProtKB:Q8NI35}.
CC -!- SUBUNIT: Forms a ternary complex with PALS1 and CRB1 (By similarity).
CC Component of a complex whose core is composed of ARHGAP17, AMOT, PALS1,
CC INADL/PATJ and PARD3/PAR3 (By similarity). Forms a heterotrimeric
CC complex composed of MMP5, LIN7B and PATJ; the N-terminal L27 domain of
CC PALS1 interacts with the L27 domain of PATJ and the C-terminal L27
CC domain of PALS1 interacts with the L27 domain of LIN7B
CC (PubMed:22337881). Component of a complex composed of CRB3, PALS1 and
CC PATJ (By similarity). Interacts (via N-terminus) with PALS1/PALS (via
CC PDZ domain) (By similarity). Interacts with TJP3/ZO-3 and
CC CLDN1/claudin-1 (By similarity). Interacts with ASIC3, KCNJ10, KCNJ15,
CC GRIN2A, GRIN2B, GRIN2C, GRIN2D, NLGN2, and HTR2A (By similarity).
CC Interacts with MPP7 (By similarity). Directly interacts with HTR4 (By
CC similarity). Interacts (via PDZ domain 8) with WWC1 (via the ADDV
CC motif) (By similarity). Interacts with SLC6A4 (By similarity).
CC Interacts (via C-terminus) with ARHGEF18 (By similarity). Interacts
CC with NPHP1 (By similarity). Interacts with PARD3/PAR3 (By similarity).
CC {ECO:0000250|UniProtKB:A0A5F4CJZ2, ECO:0000250|UniProtKB:E2QYC9,
CC ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35,
CC ECO:0000269|PubMed:22337881}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000250|UniProtKB:Q8NI35}. Apical cell membrane
CC {ECO:0000250|UniProtKB:Q8NI35}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:Q8NI35}. Cytoplasm, perinuclear region
CC {ECO:0000250|UniProtKB:Q63ZW7}. Note=Localizes to the apical region at
CC the start of epithelial cell polarization then locates to tight
CC junctions as polarization is completed (By similarity). Localized in
CC the paranodal region of myelinating Schwann cells (By similarity).
CC Localized to the leading edge of the actin cortex of migrating
CC epithelia cells (By similarity). {ECO:0000250|UniProtKB:E2QYC9,
CC ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35}.
CC -!- TISSUE SPECIFICITY: Abundantly expressed in germ cells, also expressed
CC in testes and seminiferous tubules, with faint expression in Sertoli
CC cells (at protein level). {ECO:0000269|PubMed:18621709}.
CC -!- DOMAIN: The L27 domain (also called Maguk recruitment domain) is
CC required for interaction with PALS1 and CRB3, and PALS1 localization to
CC tight junctions. {ECO:0000250|UniProtKB:Q8NI35}.
CC -!- DOMAIN: The PDZ domain 6 mediates interaction with the C-terminus of
CC TJP3 and is crucial for localization to the tight junctions (By
CC similarity). The PDZ domain 8 interacts with CLDN1 but is not required
CC for proper localization (By similarity).
CC {ECO:0000250|UniProtKB:Q8NI35}.
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DR EMBL; AABR07049320; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07049321; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07049322; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07049323; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07049324; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07049325; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AABR07049326; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR RefSeq; NP_536323.1; NM_080398.1.
DR RefSeq; XP_006238486.1; XM_006238424.3.
DR PDB; 3UIT; X-ray; 2.05 A; A/B/C/D=1-68.
DR PDBsum; 3UIT; -.
DR AlphaFoldDB; F1MAD2; -.
DR SMR; F1MAD2; -.
DR CORUM; F1MAD2; -.
DR STRING; 10116.ENSRNOP00000010211; -.
DR iPTMnet; F1MAD2; -.
DR PhosphoSitePlus; F1MAD2; -.
DR PaxDb; F1MAD2; -.
DR PRIDE; F1MAD2; -.
DR Ensembl; ENSRNOT00000010211; ENSRNOP00000010211; ENSRNOG00000007551.
DR GeneID; 140581; -.
DR KEGG; rno:140581; -.
DR CTD; 10207; -.
DR RGD; 1565362; Patj.
DR eggNOG; KOG0708; Eukaryota.
DR eggNOG; KOG3528; Eukaryota.
DR GeneTree; ENSGT00940000155136; -.
DR HOGENOM; CLU_002378_1_0_1; -.
DR InParanoid; F1MAD2; -.
DR OMA; ESHYILH; -.
DR OrthoDB; 1419918at2759; -.
DR TreeFam; TF330709; -.
DR PRO; PR:F1MAD2; -.
DR Proteomes; UP000002494; Chromosome 5.
DR Bgee; ENSRNOG00000007551; Expressed in cerebellum and 18 other tissues.
DR Genevisible; F1MAD2; RN.
DR GO; GO:0045177; C:apical part of cell; ISO:RGD.
DR GO; GO:0016324; C:apical plasma membrane; ISS:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; ISO:RGD.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; ISO:RGD.
DR GO; GO:0032991; C:protein-containing complex; IDA:RGD.
DR GO; GO:0035003; C:subapical complex; ISO:RGD.
DR GO; GO:0070160; C:tight junction; ISS:UniProtKB.
DR GO; GO:0035089; P:establishment of apical/basal cell polarity; ISS:UniProtKB.
DR GO; GO:0120192; P:tight junction assembly; ISS:UniProtKB.
DR Gene3D; 2.30.42.10; -; 10.
DR InterPro; IPR015132; L27_2.
DR InterPro; IPR004172; L27_dom.
DR InterPro; IPR036892; L27_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF09045; L27_2; 1.
DR Pfam; PF00595; PDZ; 10.
DR SMART; SM00569; L27; 1.
DR SMART; SM00228; PDZ; 10.
DR SUPFAM; SSF101288; SSF101288; 1.
DR SUPFAM; SSF50156; SSF50156; 10.
DR PROSITE; PS51022; L27; 1.
DR PROSITE; PS50106; PDZ; 10.
PE 1: Evidence at protein level;
KW 3D-structure; Cell junction; Cell membrane; Cytoplasm; Membrane;
KW Phosphoprotein; Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1836
FT /note="InaD-like protein"
FT /id="PRO_0000447579"
FT DOMAIN 1..65
FT /note="L27"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00365"
FT DOMAIN 134..221
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 248..328
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 365..453
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 555..641
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 687..773
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1074..1166
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1245..1328
FT /note="PDZ 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1472..1555
FT /note="PDZ 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1568..1650
FT /note="PDZ 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1709..1795
FT /note="PDZ 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 456..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1173..1232
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1341..1448
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1657..1678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1813..1836
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1173..1191
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1364..1384
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1405..1448
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1822..1836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 455
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZW7"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI35"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZW7"
FT MOD_RES 647
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZW7"
FT MOD_RES 1217
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZW7"
FT MOD_RES 1545
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI35"
FT HELIX 11..26
FT /evidence="ECO:0007829|PDB:3UIT"
FT HELIX 32..43
FT /evidence="ECO:0007829|PDB:3UIT"
FT HELIX 45..56
FT /evidence="ECO:0007829|PDB:3UIT"
SQ SEQUENCE 1836 AA; 199468 MW; BB8000DE4468A966 CRC64;
MPENPAAEKM QVLQVLDRLR GKLQEKGDTT QNEKLSAFYE TLKSPLFNQI LTLQQSIKQL
KGQLSHIPSD CSANFDFSRK GLLVFTDGSI TNGNAHRPCS SITASESLPW TQRSGNEDFT
SVIQQMAQGR HIEYIDIERP STGGLGFSVV ALRSQSLGLI DIFVKEVHPG SVADRDQRLK
ENDQILAIND TPLDQNISHQ QAIALLQQAT GSLRLVVARE VGHTQSRTST SSADTTLPET
VRWGHTEDVE LINDGSGLGF GIVGGKSSGV VVRTIVPGGL ADRDGRLQTG DHILKIGSTN
VQGMTSEQVA QVLRNCGNSV RMLVARDPVG EIAVTPPTPA SLPVALPVVA TRTLGSDSSP
FETYNVELVK KDGQSLGIRI VGYVGTAHPG EASGIYVKSI IPGSAAYHNG QIQVNDKIVA
VDGVNIQGFA NQDVVEVLRN AGQVVHLTLV RRKTSLSASP FEQPSSREAV AEPPEVPELT
GSLKPETNSR MEAEEIGERL DNLRKDTVQA LEKPDVYPED IPGCPENELK SRWENLLGPD
YEVMVATLDT QIADDEELQK YSKLLPIHTL RLGMEVDSFD GHHYISSIAP GGPVDTLNLL
QPEDELLEVN GVQLYGKSRR EAVSFLKEVP PPFTLVCCRR LFDDEASVDE PRTVEPSLLE
AEVDRSVDVS TEDDDGELAL WSPEVKTVEL VKDCKGLGFS ILDYQDPLDP MRSVIVIRSL
VADGVAERSG ELLPGDRLVS VNEFSLDNAT LAEAVEVLKA VPPGVVHLGI CKPLVEEEKE
EKEEHFIFHS NNNGDNSESP ETVHEIHSSL ILEAPQGFRD EPYLEELVDE PFLDLGKSLQ
FQQKDMDSSS EAWEMHEFLS PRLERRGEER EMLVDEEYEI YQDRLRDMEA HPPPPHIREP
TSASPRLDLQ AGPQWLHADL SGGEILECHD TESMMTAYPQ EMQDYSFSTT DMMKETFGLD
SRPPMPSSEG NGQHGRFDDL EHLHSLVSHG LDLGMMTPSD LQGPGVLVDL PAVTQRREQE
ELPLYRLPSA RVVTKPSSHV GMVSSRHANA ACELPEREEG EGEETPNFSH WGPPRIVEIF
REPNVSLGIS IVGGQTVIKR LKNGEELKGI FIKQVLEDSP AGKTKALKTG DKILEVSGVD
LQNASHAEAV EAIKSAGNPV VFVVQSLSST PRVIPSVNNK GKTPPQNQDQ NTQEKKAKRH
GTAPPPMKLP PPYRAPSADT EESEEDSALT DKKIRQRYAD LPGELHIIEL EKDKNGLGLS
LAGNKDRSRM SIFVVGINPD GPAAADGRMR VGDELLEINN QILYGRSHQN ASAIIKTAPT
RVKLVFIRNE DAVNQMAVAP FPVPSHSPSP VEDLGGTEPV SSEEDSSVDA KPLPERESSK
PEDLTQAVDD SMVAEQEKAS ESPDSAARQM KQPGYSAQVS SSSQEIPSAP APLCQSTHAD
VTGSGNFQAP LSVDPAPLSV DPATCPIVPG QEMIIEISKG RSGLGLSIVG GKDTPLDAIV
IHEVYEEGAA ARDGRLWAGD QILEVNGVDL RSSSHEEAIT ALRQTPQKVR LVIYRDEAQY
RDEENLEVFL VDLQKKTGRG LGLSIVGKRS GSGVFISDIV KGGAADLDGR LIRGDQILSV
NGEDVRQASQ ETVATILKCV QGLVQLEIGR LRAGSWASSR KTSQNSQGDQ HSAHSSCRPS
FAPVITSLQN LVGTKRSSDP PQKCTEEEPR TVEIIRELSD ALGVSIAGGK GSPLGDIPIF
IAMIQANGVA ARTQKLKVGD RIVSINGQPL DGLSHTDAVN LLKNAFGRII LQVVADTNIS
AIATQLEMMS AGSQLGSPTA DRHPQDPEEL LQRTAD
