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Database: UniProt
Entry: G1KUK5_ANOCA
LinkDB: G1KUK5_ANOCA
Original site: G1KUK5_ANOCA 
ID   G1KUK5_ANOCA            Unreviewed;      1053 AA.
AC   G1KUK5;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 2.
DT   27-MAR-2024, entry version 84.
DE   SubName: Full=Leucine rich repeats and immunoglobulin like domains 2 {ECO:0000313|Ensembl:ENSACAP00000017670.3};
GN   Name=LRIG2 {ECO:0000313|Ensembl:ENSACAP00000017670.3};
OS   Anolis carolinensis (Green anole) (American chameleon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Lepidosauria; Squamata; Bifurcata; Unidentata; Episquamata; Toxicofera;
OC   Iguania; Dactyloidae; Anolis.
OX   NCBI_TaxID=28377 {ECO:0000313|Ensembl:ENSACAP00000017670.3, ECO:0000313|Proteomes:UP000001646};
RN   [1] {ECO:0000313|Ensembl:ENSACAP00000017670.3, ECO:0000313|Proteomes:UP000001646}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JBL SC #1 {ECO:0000313|Ensembl:ENSACAP00000017670.3,
RC   ECO:0000313|Proteomes:UP000001646};
RG   The Genome Sequencing Platform;
RA   Di Palma F., Alfoldi J., Heiman D., Young S., Grabherr M., Johnson J.,
RA   Lander E.S., Lindblad-Toh K.;
RT   "The Genome Sequence of Anolis carolinensis (Green Anole Lizard).";
RL   Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSACAP00000017670.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   RefSeq; XP_003220507.2; XM_003220459.3.
DR   AlphaFoldDB; G1KUK5; -.
DR   STRING; 28377.ENSACAP00000017670; -.
DR   Ensembl; ENSACAT00000018018.4; ENSACAP00000017670.3; ENSACAG00000017947.4.
DR   GeneID; 100560844; -.
DR   KEGG; acs:100560844; -.
DR   CTD; 9860; -.
DR   eggNOG; KOG4194; Eukaryota.
DR   GeneTree; ENSGT00940000158791; -.
DR   HOGENOM; CLU_000288_18_24_1; -.
DR   InParanoid; G1KUK5; -.
DR   OrthoDB; 5405965at2759; -.
DR   TreeFam; TF325380; -.
DR   Proteomes; UP000001646; Chromosome 4.
DR   Bgee; ENSACAG00000017947; Expressed in hemipenis and 13 other cell types or tissues.
DR   GO; GO:0031012; C:extracellular matrix; IBA:GO_Central.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0030426; C:growth cone; IEA:Ensembl.
DR   GO; GO:0097708; C:intracellular vesicle; IEA:Ensembl.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005102; F:signaling receptor binding; IEA:Ensembl.
DR   GO; GO:0060384; P:innervation; IEA:Ensembl.
DR   GO; GO:0006509; P:membrane protein ectodomain proteolysis; IEA:Ensembl.
DR   GO; GO:0048681; P:negative regulation of axon regeneration; IEA:Ensembl.
DR   GO; GO:0051045; P:negative regulation of membrane protein ectodomain proteolysis; IEA:Ensembl.
DR   GO; GO:2000010; P:positive regulation of protein localization to cell surface; IEA:Ensembl.
DR   GO; GO:0034394; P:protein localization to cell surface; IEA:Ensembl.
DR   GO; GO:2001222; P:regulation of neuron migration; IEA:Ensembl.
DR   GO; GO:0010640; P:regulation of platelet-derived growth factor receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0007605; P:sensory perception of sound; IEA:Ensembl.
DR   CDD; cd05763; IgI_LRIG1-like; 1.
DR   Gene3D; 2.60.40.10; Immunoglobulins; 3.
DR   Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 2.
DR   InterPro; IPR000483; Cys-rich_flank_reg_C.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR013098; Ig_I-set.
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   PANTHER; PTHR45842:SF19; LEUCINE-RICH REPEATS AND IMMUNOGLOBULIN-LIKE DOMAINS PROTEIN 2; 1.
DR   PANTHER; PTHR45842; SYNAPTIC ADHESION-LIKE MOLECULE SALM; 1.
DR   Pfam; PF07679; I-set; 2.
DR   Pfam; PF13927; Ig_3; 1.
DR   Pfam; PF13855; LRR_8; 3.
DR   Pfam; PF01463; LRRCT; 1.
DR   PRINTS; PR00019; LEURICHRPT.
DR   SMART; SM00409; IG; 3.
DR   SMART; SM00408; IGc2; 3.
DR   SMART; SM00365; LRR_SD22; 7.
DR   SMART; SM00369; LRR_TYP; 11.
DR   SMART; SM00082; LRRCT; 1.
DR   SUPFAM; SSF48726; Immunoglobulin; 3.
DR   SUPFAM; SSF52058; L domain-like; 1.
DR   PROSITE; PS50835; IG_LIKE; 3.
DR   PROSITE; PS51450; LRR; 5.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001646};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..25
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           26..1053
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003413126"
FT   TRANSMEM        792..818
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          487..586
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          591..680
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          685..759
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   REGION          848..877
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        848..874
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1053 AA;  117816 MW;  7087CE0237E63B32 CRC64;
     MRWRRGFPPR PIGLLFVLLL QRAAGEACAP AGPCSCRRGV LDCSRLRATG RSVEPGLLLP
     LPPDTTALDL SHNHLSSSNW SIDSSGQKLQ EVKMNYNELT DIPCFGELTS NITLLSLVHN
     TIPEIVPEQL QLFVSLENLD LSSNLISEIK ISSFPRMQLK YLNLSNNRIT TLEAGCFDNL
     SSSLIVVKLN KNRISVIPPK TFRLPHVQYL ELKRNRIKII DSLTFQGLDS LKSLKMQRNG
     ISRLMDGAFF GLDNMEELEL EHNNLTEVNK GWLYGLRTLQ QLYVSQNAIN KIGPDAWEFC
     QRLSELDLSY NQLTRLDEFA FVGLNLLERL NLSDNRISHI ADGVFKGLSN LQTLDLRNNE
     ISWAIEDSNE AFVGLERLNK LILQGNQIKS ITKRAFFGLQ VLEYLDLNNN AIMSIQENAF
     SQPLKELVLN TSSLLCDCQL KWLLQWLTQS NLQDTVNVIC AHPERLAGQS ILTVNPEDFV
     CDDFPKPQIR THPETAIALR GTNVTLTCKA VSSSDLPMST TWRKDSEILY DADIETFVRY
     QQQDGEVLEY TSILHVFNVN FTDEGKYQCI ISNHFGSNYS NKAKLTVNEL PSFIKTPMDL
     TIRTRAMAKL ECAAEGHPPP QISWQKDGGT DFPAARERRM HVMPEDDVFF IANVKIEDMG
     IYSCMAQNVA GGISANATLT VLETPSFVRP LEDRTVAQGE TAVLQCIASG SPAPRLNWTK
     DDGPLTVTER HFFAAANQLL IIVDAGLEDA GKYTCVMSNT LGTVRGHIYL YVISSPNCDS
     SQSGIGIEED GWTTVGIVII VVVCCVVGTS LVWVIVIYHM RRKSEDYSIT NTEEVNLPAD
     IPSYLSSQGT LSEPQEGYSN SEAGSNQQLM PPSSGYVHKG TDGGTAQLVI CSDCYDNANI
     YSRTREYCPY AYVTEDDPLD QTLSNLMVQM SKEPYPVCPQ HEATTLDGLP GDRDMSVFLN
     NQDRLHEKKP CPQPCNTDPF RLSLWGVNKD LGLLHPCFSP QPKTHDVPHV LLSEGIAETG
     QEQVISPRSH HKLHEHNFDF DRTQNLQEHH EAT
//
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