LRIT1_RAT
ID LRIT1_RAT Reviewed; 623 AA.
AC Q9JMH2;
DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot.
DT 03-NOV-2009, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Leucine-rich repeat, immunoglobulin-like domain and transmembrane domain-containing protein 1;
DE AltName: Full=Leucine-rich repeat-containing protein 21;
DE AltName: Full=Photoreceptor-associated LRR superfamily protein;
DE AltName: Full=Retina-specific protein PAL;
DE Flags: Precursor;
GN Name=Lrit1; Synonyms=Lrrc21, Pal;
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|EMBL:BAA95680.1};
RN [1] {ECO:0000305}
RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, SUBCELLULAR LOCATION, TISSUE
RP SPECIFICITY, AND DEVELOPMENTAL STAGE.
RC TISSUE=Retina {ECO:0000312|EMBL:BAA95680.1};
RX PubMed=10777785; DOI=10.1523/jneurosci.20-09-03206.2000;
RA Gomi F., Imaizumi K., Yoneda T., Taniguchi M., Mori Y., Miyoshi K.,
RA Hitomi J., Fujikado T., Tano Y., Tohyama M.;
RT "Molecular cloning of a novel membrane glycoprotein, Pal, specifically
RT expressed in photoreceptor cells of the retina and containing leucine-rich
RT repeat.";
RL J. Neurosci. 20:3206-3213(2000).
CC -!- FUNCTION: Possible role in phototransduction.
CC {ECO:0000303|PubMed:10777785}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10777785}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000269|PubMed:10777785}; Single-pass type I membrane protein
CC {ECO:0000269|PubMed:10777785}.
CC -!- TISSUE SPECIFICITY: Retina, outer segments of photoreceptor cells.
CC {ECO:0000269|PubMed:10777785}.
CC -!- DEVELOPMENTAL STAGE: No expression at 1 day old. Expressed at 7 days
CC old, increased expression at 14 and 56 days old.
CC {ECO:0000269|PubMed:10777785}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA95680.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB028461; BAA95680.1; ALT_INIT; mRNA.
DR RefSeq; NP_647547.2; NM_139331.2.
DR AlphaFoldDB; Q9JMH2; -.
DR SMR; Q9JMH2; -.
DR STRING; 10116.ENSRNOP00000017773; -.
DR GlyGen; Q9JMH2; 3 sites.
DR PhosphoSitePlus; Q9JMH2; -.
DR PaxDb; Q9JMH2; -.
DR Ensembl; ENSRNOT00000017773; ENSRNOP00000017773; ENSRNOG00000012790.
DR GeneID; 246214; -.
DR KEGG; rno:246214; -.
DR UCSC; RGD:628607; rat.
DR CTD; 26103; -.
DR RGD; 628607; Lrit1.
DR eggNOG; KOG0619; Eukaryota.
DR eggNOG; KOG3510; Eukaryota.
DR GeneTree; ENSGT00940000156033; -.
DR HOGENOM; CLU_019650_0_0_1; -.
DR InParanoid; Q9JMH2; -.
DR OrthoDB; 316687at2759; -.
DR PhylomeDB; Q9JMH2; -.
DR TreeFam; TF330861; -.
DR PRO; PR:Q9JMH2; -.
DR Proteomes; UP000002494; Chromosome 16.
DR Genevisible; Q9JMH2; RN.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IDA:UniProtKB.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR Gene3D; 3.80.10.10; -; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR000372; LRRNT.
DR Pfam; PF00041; fn3; 1.
DR Pfam; PF13855; LRR_8; 1.
DR SMART; SM00409; IG; 1.
DR SMART; SM00408; IGc2; 1.
DR SMART; SM00369; LRR_TYP; 4.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR SUPFAM; SSF49265; SSF49265; 1.
DR PROSITE; PS50853; FN3; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
DR PROSITE; PS51450; LRR; 4.
PE 1: Evidence at protein level;
KW Disulfide bond; Endoplasmic reticulum; Glycoprotein; Immunoglobulin domain;
KW Leucine-rich repeat; Membrane; Reference proteome; Repeat; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..623
FT /note="Leucine-rich repeat, immunoglobulin-like domain and
FT transmembrane domain-containing protein 1"
FT /id="PRO_0000014837"
FT TOPO_DOM 22..526
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT TRANSMEM 527..547
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 548..623
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..59
FT /note="LRRNT"
FT REPEAT 60..81
FT /note="LRR 1"
FT REPEAT 84..105
FT /note="LRR 2"
FT REPEAT 108..128
FT /note="LRR 3"
FT REPEAT 132..153
FT /note="LRR 4"
FT REPEAT 156..177
FT /note="LRR 5"
FT DOMAIN 201..253
FT /note="LRRCT"
FT DOMAIN 266..332
FT /note="Ig-like C2-type"
FT DOMAIN 430..518
FT /note="Fibronectin type-III"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT REPEAT 525..548
FT /note="LRR 6"
FT CARBOHYD 156
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 296
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 455
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 275..328
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 623 AA; 68417 MW; 78D82B09D3DC8275 CRC64;
MWVALGMLWL LALGGPHQAW SFCPSQCSCS LHILSDGSKA RTVVCSDPDL TLPPASIPPD
TCKLRLERTA IRRVPGETFR PLSRLEQLWL PYNALSELST LMLRGLRRLR ELRLPGNHLV
TFPWAALKDT PQLQLLDLQA NRLSTLPPEA VHFLENLTFL DLSNNQLMRL PEELLDTWAH
LKTGPYLSSR RTRLVLGLQD NPWVCDCRLY DLVHLLDGWA SNLIFIEARL RCGSPRSLAG
VAFSQLELRK CQSPELRPGV TSIISPLGST VLLRCGATGI PGPEMSWRRA NGRPLNGTVH
QEVSSDGSSW TLLDLPVVSL FDSGDYICQA KNFLGASETL ISLIVTEPQT STEYTGIPGA
LWARTGEGAE AAAYNNKLVA RHVPHVPEPV ALATKPSVPS IKEELPLQNF QMDVPGEFSR
EPSEHQETQM VRSLKVVGDT YHSVSLVWKA PQAGNTTAFS VLYAVFGQRD MRRMTVEAGK
TSVTIEGLAP KTKYVACVCV RGLVPTKEQC VIFSTDEVVD AEGTQRLINM VVISVAAIIA
LPPTLLVCCG ALRRRCHKCR AGGSAEASGA YVNLERLGHS EDGSEELSRS SLSEADRLLS
ARSSLDSQVL GVRGGRRINE YFC
