INADL_CANLF
ID INADL_CANLF Reviewed; 1828 AA.
AC E2QYC9;
DT 02-DEC-2020, integrated into UniProtKB/Swiss-Prot.
DT 11-DEC-2019, sequence version 3.
DT 03-AUG-2022, entry version 65.
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:0000250|UniProtKB:Q8NI35};
GN Synonyms=CIPP {ECO:0000250|UniProtKB:Q63ZW7},
GN INADL {ECO:0000250|UniProtKB:Q8NI35};
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 {ECO:0000312|Proteomes:UP000002254};
RN [1] {ECO:0000312|Proteomes:UP000002254}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Boxer {ECO:0000312|Proteomes:UP000002254};
RX PubMed=16341006; DOI=10.1038/nature04338;
RA Lindblad-Toh K., Wade C.M., Mikkelsen T.S., Karlsson E.K., Jaffe D.B.,
RA Kamal M., Clamp M., Chang J.L., Kulbokas E.J. III, Zody M.C., Mauceli E.,
RA Xie X., Breen M., Wayne R.K., Ostrander E.A., Ponting C.P., Galibert F.,
RA Smith D.R., deJong P.J., Kirkness E.F., Alvarez P., Biagi T., Brockman W.,
RA Butler J., Chin C.-W., Cook A., Cuff J., Daly M.J., DeCaprio D., Gnerre S.,
RA Grabherr M., Kellis M., Kleber M., Bardeleben C., Goodstadt L., Heger A.,
RA Hitte C., Kim L., Koepfli K.-P., Parker H.G., Pollinger J.P.,
RA Searle S.M.J., Sutter N.B., Thomas R., Webber C., Baldwin J., Abebe A.,
RA Abouelleil A., Aftuck L., Ait-Zahra M., Aldredge T., Allen N., An P.,
RA Anderson S., Antoine C., Arachchi H., Aslam A., Ayotte L., Bachantsang P.,
RA Barry A., Bayul T., Benamara M., Berlin A., Bessette D., Blitshteyn B.,
RA Bloom T., Blye J., Boguslavskiy L., Bonnet C., Boukhgalter B., Brown A.,
RA Cahill P., Calixte N., Camarata J., Cheshatsang Y., Chu J., Citroen M.,
RA Collymore A., Cooke P., Dawoe T., Daza R., Decktor K., DeGray S.,
RA Dhargay N., Dooley K., Dooley K., Dorje P., Dorjee K., Dorris L.,
RA Duffey N., Dupes A., Egbiremolen O., Elong R., Falk J., Farina A., Faro S.,
RA Ferguson D., Ferreira P., Fisher S., FitzGerald M., Foley K., Foley C.,
RA Franke A., Friedrich D., Gage D., Garber M., Gearin G., Giannoukos G.,
RA Goode T., Goyette A., Graham J., Grandbois E., Gyaltsen K., Hafez N.,
RA Hagopian D., Hagos B., Hall J., Healy C., Hegarty R., Honan T., Horn A.,
RA Houde N., Hughes L., Hunnicutt L., Husby M., Jester B., Jones C., Kamat A.,
RA Kanga B., Kells C., Khazanovich D., Kieu A.C., Kisner P., Kumar M.,
RA Lance K., Landers T., Lara M., Lee W., Leger J.-P., Lennon N., Leuper L.,
RA LeVine S., Liu J., Liu X., Lokyitsang Y., Lokyitsang T., Lui A.,
RA Macdonald J., Major J., Marabella R., Maru K., Matthews C., McDonough S.,
RA Mehta T., Meldrim J., Melnikov A., Meneus L., Mihalev A., Mihova T.,
RA Miller K., Mittelman R., Mlenga V., Mulrain L., Munson G., Navidi A.,
RA Naylor J., Nguyen T., Nguyen N., Nguyen C., Nguyen T., Nicol R., Norbu N.,
RA Norbu C., Novod N., Nyima T., Olandt P., O'Neill B., O'Neill K., Osman S.,
RA Oyono L., Patti C., Perrin D., Phunkhang P., Pierre F., Priest M.,
RA Rachupka A., Raghuraman S., Rameau R., Ray V., Raymond C., Rege F.,
RA Rise C., Rogers J., Rogov P., Sahalie J., Settipalli S., Sharpe T.,
RA Shea T., Sheehan M., Sherpa N., Shi J., Shih D., Sloan J., Smith C.,
RA Sparrow T., Stalker J., Stange-Thomann N., Stavropoulos S., Stone C.,
RA Stone S., Sykes S., Tchuinga P., Tenzing P., Tesfaye S., Thoulutsang D.,
RA Thoulutsang Y., Topham K., Topping I., Tsamla T., Vassiliev H.,
RA Venkataraman V., Vo A., Wangchuk T., Wangdi T., Weiand M., Wilkinson J.,
RA Wilson A., Yadav S., Yang S., Yang X., Young G., Yu Q., Zainoun J.,
RA Zembek L., Zimmer A., Lander E.S.;
RT "Genome sequence, comparative analysis and haplotype structure of the
RT domestic dog.";
RL Nature 438:803-819(2005).
RN [2] {ECO:0000305}
RP IDENTIFICATION IN A COMPLEX WITH PALS1 AND CRB3, AND SUBCELLULAR LOCATION.
RX PubMed=12527193; DOI=10.1016/s0378111902010843;
RA Makarova O., Roh M.H., Liu C.-J., Laurinec S., Margolis B.;
RT "Mammalian Crumbs3 is a small transmembrane protein linked to protein
RT associated with Lin-7 (Pals1).";
RL Gene 302:21-29(2003).
RN [3] {ECO:0000305}
RP SUBCELLULAR LOCATION.
RX PubMed=12771187; DOI=10.1242/jcs.00500;
RA Roh M.H., Fan S., Liu C.-J., Margolis B.;
RT "The Crumbs3-Pals1 complex participates in the establishment of polarity in
RT mammalian epithelial cells.";
RL J. Cell Sci. 116:2895-2906(2003).
RN [4] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PALS1 AND CRB3, AND SUBCELLULAR LOCATION.
RX PubMed=15738264; DOI=10.1083/jcb.200408064;
RA Shin K., Straight S., Margolis B.;
RT "PATJ regulates tight junction formation and polarity in mammalian
RT epithelial cells.";
RL J. Cell Biol. 168:705-711(2005).
RN [5] {ECO:0000305}
RP FUNCTION, INTERACTION WITH PARD3, AND SUBCELLULAR LOCATION.
RX PubMed=17235357; DOI=10.1038/sj.embor.7400890;
RA Shin K., Wang Q., Margolis B.;
RT "PATJ regulates directional migration of mammalian epithelial cells.";
RL EMBO Rep. 8:158-164(2007).
CC -!- FUNCTION: Scaffolding protein that facilitates the localization of
CC proteins to the cell membrane (PubMed:17235357). Required for the
CC correct formation of tight junctions and epithelial apico-basal
CC polarity (PubMed:15738264). Positively regulates epithelial cell
CC microtubule elongation and cell migration, possibly via facilitating
CC localization of PRKCI/aPKC and PAR3D/PAR3 at the leading edge of
CC migrating cells (PubMed:17235357). Plays a role in the correct
CC reorientation of the microtubule-organizing center during epithelial
CC migration (PubMed:17235357). May regulate the surface expression and/or
CC function of ASIC3 in sensory neurons (By similarity). May recruit
CC ARHGEF18 to apical cell-cell boundaries (By similarity).
CC {ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35,
CC ECO:0000269|PubMed:15738264, ECO:0000269|PubMed:17235357}.
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 (By similarity).
CC Component of a complex composed of CRB3, PALS1 and PATJ
CC (PubMed:12527193, PubMed:15738264). Interacts (via N-terminus) with
CC PALS1/PALS (via PDZ domain) (PubMed:15738264). Interacts with TJP3/ZO-3
CC and CLDN1/claudin-1 (By similarity). Interacts with ASIC3, KCNJ10,
CC KCNJ15, GRIN2A, GRIN2B, GRIN2C, GRIN2D, NLGN2, and HTR2A (By
CC similarity). Interacts with MPP7 (By similarity). Directly interacts
CC with HTR4 (By similarity). Interacts (via PDZ domain 8) with WWC1 (via
CC the ADDV 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
CC (PubMed:17235357). {ECO:0000250|UniProtKB:F1MAD2,
CC ECO:0000250|UniProtKB:Q63ZW7, ECO:0000250|UniProtKB:Q8NI35,
CC ECO:0000269|PubMed:12527193, ECO:0000269|PubMed:15738264,
CC ECO:0000269|PubMed:17235357}.
CC -!- SUBCELLULAR LOCATION: Cell junction, tight junction
CC {ECO:0000269|PubMed:12527193, ECO:0000269|PubMed:12771187,
CC ECO:0000269|PubMed:15738264}. Apical cell membrane
CC {ECO:0000269|PubMed:15738264}; 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 (PubMed:15738264). 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 (PubMed:17235357). {ECO:0000250|UniProtKB:Q63ZW7,
CC ECO:0000269|PubMed:15738264, ECO:0000269|PubMed:17235357}.
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; AAEX03003771; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX03003772; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX03003773; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AAEX03003774; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR AlphaFoldDB; E2QYC9; -.
DR SMR; E2QYC9; -.
DR CORUM; E2QYC9; -.
DR eggNOG; KOG0708; Eukaryota.
DR eggNOG; KOG3528; Eukaryota.
DR HOGENOM; CLU_002378_1_0_1; -.
DR OMA; ESHYILH; -.
DR TreeFam; TF330709; -.
DR Proteomes; UP000002254; Chromosome 5.
DR Bgee; ENSCAFG00000018822; Expressed in cerebellum and 46 other tissues.
DR GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
DR GO; GO:0005923; C:bicellular tight junction; IEA:UniProtKB-SubCell.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0070160; C:tight junction; IDA:UniProtKB.
DR GO; GO:0035089; P:establishment of apical/basal cell polarity; IMP:UniProtKB.
DR GO; GO:0031023; P:microtubule organizing center organization; IMP:UniProtKB.
DR GO; GO:0010634; P:positive regulation of epithelial cell migration; IMP:UniProtKB.
DR GO; GO:0070507; P:regulation of microtubule cytoskeleton organization; IMP:UniProtKB.
DR GO; GO:0032880; P:regulation of protein localization; IMP:UniProtKB.
DR GO; GO:0120192; P:tight junction assembly; IMP: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 Cell junction; Cell membrane; Cytoplasm; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Tight junction.
FT CHAIN 1..1828
FT /note="InaD-like protein"
FT /id="PRO_0000451409"
FT DOMAIN 5..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 553..639
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 686..758
FT /note="PDZ 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1070..1162
FT /note="PDZ 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1241..1324
FT /note="PDZ 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1464..1547
FT /note="PDZ 8"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1560..1642
FT /note="PDZ 9"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1703..1789
FT /note="PDZ 10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1168..1220
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1333..1362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1645..1669
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1805..1828
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1168..1182
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1334..1356
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 459
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI35"
FT MOD_RES 522
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZW7"
FT MOD_RES 645
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZW7"
FT MOD_RES 1211
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q63ZW7"
FT MOD_RES 1535
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NI35"
SQ SEQUENCE 1828 AA; 199664 MW; B2B6D87C02900653 CRC64;
MPENPAPDKL QVLQVLDRLK MKLQEKGDTS QNEKLSLFYE TLQSPLFNQI LTLQQSIKQL
KGQLSHIPSD CSTNFDFSRK GLLVFTDSAI TNGNAQRPSN NLTVSGLFPW TPKSGNEDFN
SVIQQMAQGR QIEYIDIERP STGGLGFSVV ALRSQNLGEV DIFVKEVQPG SIADRDQRLR
ENDQILAINH TPLDQNISHQ QAIALLQQTT GSLHLVVARE PVHTKSRTSI NLTDTTMPET
VHWGHIEDVE LINDGSGLGF GIVGGKSSGV VVRTIVPGGL ADRDGRLQTG DHILKIGDTD
VQGMTSEQVA QVLRNCGNSV RMLVARDPVG ETSVTPPTPA ALPVALPAVA NRSPSTDSSL
YETYGVELIK KDGQSLGIRI VGYIGTAHTG EASGIYVKSI IPGSAAYHNG QIQVNDKIVA
VDGVNIQGFT NQDVVEVLRN AGQVVHLTLV RRKMCSSTSP LERSSDRGTV VEPSGTPARY
VTGAVETETN LDGGDEETEE RMDNLKNDNI QALEKLERVP DSPENELKSR WENLLGPDYE
VMVATLDTQI ADDAELQKYS KLLPIHTLRL GMEVDSFDGH HYISSIAPGG PVDALNLLQP
EDELLEVNGV QLYGKSRREA VSFLKEVPPP FTLVCCRRLF DDEASVDEPR TTETLLPEME
ADHNVDINTE EEEEEELALW SPEVKIVELV KDHKGLGFSI LDYQDPLDPT RSVIVIRSLV
ANGVAEKGGE LLPGDRLVSV NEYCLENTTL AEAVEVLKAV PPGIVHLGVC KPLVDNDKEE
ESHYILHSNN NEDETELSET IHDINSSLIL EAPKGFRDEP YYKEELVDEP FLDLGKAFQS
QQKEIDNSKE AWEMQEFLPP RLQEMGEERE MLVDEECDLY QDHFQSMDLY PSSHLQEAAP
VSSVKELHFG TQWLHDSEPP ELQEARSMMN MYSQETQQYG YSTENMIKEN FGIDSLPSIS
SSEGNSQQGR FDDLENLNSL TKSSLDLGMM IPNDVQGPGM LVELPAVAQR REQEDLPLYQ
LPRTRVVSKA SAYTGASSSR YTAGACELPE REEGEGEETP NFSHWGPPRI VEIFREPNVS
LGISIVGGQT VIKRLKNGEE LKGIFIKQVL EDSPAGKTNA LKTGDKILEV SGVDLQNASH
REAVEAIKNA GNPVVFVVQS LSSTPRVIPS VHNKANKIAN NQDQNTEEKK EKRQGTPPPP
MKLPPPYKAP SDDSDENEEE YAFTNKKIRQ RYADLPGELH IIELEKDKNG LGLSLAGNKD
RSRMSIFVVG INPEGPAATD GRMRIGDELL EINNQILYGR SHQNASAVIK TAPSKVKLVF
IRNEDAVNQM AVAPFPVPSS SPSSLEDQSG TEPVSSEEDG SLEVGIKQLP ENESSKLEDI
SQVAGQGMVA GQQKALDCPT DNAVSQMKPQ KYSTKVSFSS QEIPLAPAPS YHSTDVDFTS
YGGFQAPLSV DPATCPIVPG QEMIIEISKG RSGLGLSIVG GRDTPLDAIV IHEVYEEGAA
ARDGRLWAGD QILEVNGIDL RSASHEEAIT ALRQTPQKVR LVVYRDEAHY RDEENLEIFP
VDLQKKAGRG LGLSIVGKRN GSGVFISDIV KGGAADLDRR LIQGDQILSV NGEDMRNASQ
ETVATVLKCA QGLVQLEIGR LRAGSWTSSR KTSQNSQGSQ HSTHSSFHPS LAPVITSLQN
LVGTKRATDP SLKSSGMDMG PRTVEIIREL SDALGISIAG GKGSPLGDIP IFIAMIQASG
VAARTQKLKV GDRIVSINGQ PLDGLSHADV VNLLKNAYGR IILQVVADTN ISAIATQLEN
MSTGYHLGSP TAEHHPEDTE EPLQMTAG
