ID M7BZ18_CHEMY Unreviewed; 361 AA.
AC M7BZ18;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Chondroadherin {ECO:0000313|EMBL:EMP42474.1};
GN ORFNames=UY3_00261 {ECO:0000313|EMBL:EMP42474.1};
OS Chelonia mydas (Green sea-turtle) (Chelonia agassizi).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Testudinata; Testudines; Cryptodira; Durocryptodira;
OC Americhelydia; Chelonioidea; Cheloniidae; Chelonia.
OX NCBI_TaxID=8469 {ECO:0000313|EMBL:EMP42474.1, ECO:0000313|Proteomes:UP000031443};
RN [1] {ECO:0000313|Proteomes:UP000031443}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23624526; DOI=10.1038/ng.2615;
RA Wang Z., Pascual-Anaya J., Zadissa A., Li W., Niimura Y., Huang Z., Li C.,
RA White S., Xiong Z., Fang D., Wang B., Ming Y., Chen Y., Zheng Y.,
RA Kuraku S., Pignatelli M., Herrero J., Beal K., Nozawa M., Li Q., Wang J.,
RA Zhang H., Yu L., Shigenobu S., Wang J., Liu J., Flicek P., Searle S.,
RA Wang J., Kuratani S., Yin Y., Aken B., Zhang G., Irie N.;
RT "The draft genomes of soft-shell turtle and green sea turtle yield insights
RT into the development and evolution of the turtle-specific body plan.";
RL Nat. Genet. 45:701-706(2013).
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000256|ARBA:ARBA00004246}. Cell membrane
CC {ECO:0000256|ARBA:ARBA00004162}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004162}. Endoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004586}. Membrane
CC {ECO:0000256|ARBA:ARBA00004167}; Single-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004167}.
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DR EMBL; KB472301; EMP42474.1; -; Genomic_DNA.
DR RefSeq; XP_007052820.1; XM_007052758.1.
DR AlphaFoldDB; M7BZ18; -.
DR STRING; 8469.M7BZ18; -.
DR GeneID; 102936694; -.
DR KEGG; cmy:102936694; -.
DR CTD; 1101; -.
DR eggNOG; KOG0619; Eukaryota.
DR OrthoDB; 3851278at2759; -.
DR Proteomes; UP000031443; Unassembled WGS sequence.
DR Gene3D; 3.80.10.10; Ribonuclease Inhibitor; 1.
DR InterPro; IPR000483; Cys-rich_flank_reg_C.
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 PANTHER; PTHR45712; AGAP008170-PA; 1.
DR PANTHER; PTHR45712:SF22; LEUCINE RICH REPEAT FAMILY PROTEIN; 1.
DR Pfam; PF13855; LRR_8; 3.
DR Pfam; PF01463; LRRCT; 1.
DR Pfam; PF01462; LRRNT; 1.
DR SMART; SM00369; LRR_TYP; 9.
DR SMART; SM00082; LRRCT; 1.
DR SMART; SM00013; LRRNT; 1.
DR SUPFAM; SSF52058; L domain-like; 1.
DR PROSITE; PS51450; LRR; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Endoplasmic reticulum {ECO:0000256|ARBA:ARBA00022824};
KW Leucine-rich repeat {ECO:0000256|ARBA:ARBA00022614};
KW Membrane {ECO:0000256|ARBA:ARBA00022475};
KW Reference proteome {ECO:0000313|Proteomes:UP000031443};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Secreted {ECO:0000256|ARBA:ARBA00022525};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..361
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004080496"
FT DOMAIN 23..57
FT /note="LRRNT"
FT /evidence="ECO:0000259|SMART:SM00013"
FT DOMAIN 302..349
FT /note="LRRCT"
FT /evidence="ECO:0000259|SMART:SM00082"
SQ SEQUENCE 361 AA; 40570 MW; 1761142C28A60222 CRC64;
MDRSAFFLSL LSLLVCLPPI LQACPSSCHC HGGELQHVIC DNVGLKKIPK VSEQTRLLNL
QRNNFPVLPT NAFREMKGLV SLHLQHSQIK EISSGAFRGL KQLVYLYLSN NDISIIKMGA
FDDLSELTYL YMDHNKISDL PKGLLSPLIN LFILQLGSNK IRELRSGAFS GAKDLRWLYL
SDNSLSSVQP GALDDVENLA VFHLDKNQLS TYPVAAMSKL RVVEDLKLSH NPMKVIPDYA
FQSFGRYMET LSLDNMGLEK FSDKAFAGVT TLKTVHIENN RLNQLPGNFP FSSLENLTLS
NNPWHCSCQL AALRKWLESS RSRPDAVCAS PSQYRGQQIR DTAALRSCKL PTRRPRKGNR
H
//
