ID   LAYN_CRIGR              Reviewed;         374 AA.
AC   Q9Z209;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Layilin;
DE   Flags: Precursor;
GN   Name=LAYN;
OS   Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC   Cricetidae; Cricetinae; Cricetulus.
OX   NCBI_TaxID=10029;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP   INTERACTION WITH TLN1.
RX   PubMed=9786953; DOI=10.1083/jcb.143.2.429;
RA   Borowsky M.L., Hynes R.O.;
RT   "Layilin, a novel talin-binding transmembrane protein homologous with C-
RT   type lectins, is localized in membrane ruffles.";
RL   J. Cell Biol. 143:429-442(1998).
CC   -!- FUNCTION: Receptor for hyaluronate. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts with NF2 and RDX (By similarity). Interacts with
CC       TLN1. {ECO:0000250, ECO:0000269|PubMed:9786953}.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
CC       membrane protein {ECO:0000305}. Note=Colocalizes with TLN1 at the
CC       membrane ruffles. {ECO:0000269|PubMed:9786953}.
CC   -!- TISSUE SPECIFICITY: Widely expressed. Abundant in the ovary.
CC       {ECO:0000269|PubMed:9786953}.
CC   -!- DOMAIN: The C-terminal domain interacts with the N-terminal domain of
CC       RDX. {ECO:0000250}.
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DR   EMBL; AF093673; AAC68695.1; -; mRNA.
DR   RefSeq; NP_001233610.1; NM_001246681.1.
DR   AlphaFoldDB; Q9Z209; -.
DR   SMR; Q9Z209; -.
DR   STRING; 10029.NP_001233610.1; -.
DR   PRIDE; Q9Z209; -.
DR   GeneID; 100689416; -.
DR   KEGG; cge:100689416; -.
DR   CTD; 143903; -.
DR   eggNOG; KOG4297; Eukaryota.
DR   OrthoDB; 1005951at2759; -.
DR   GO; GO:0009986; C:cell surface; IDA:HGNC-UCL.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0001726; C:ruffle; IDA:HGNC-UCL.
DR   GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.100.10; -; 1.
DR   InterPro; IPR001304; C-type_lectin-like.
DR   InterPro; IPR016186; C-type_lectin-like/link_sf.
DR   InterPro; IPR016187; CTDL_fold.
DR   Pfam; PF00059; Lectin_C; 1.
DR   SMART; SM00034; CLECT; 1.
DR   SUPFAM; SSF56436; SSF56436; 1.
DR   PROSITE; PS50041; C_TYPE_LECTIN_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Lectin; Membrane; Phosphoprotein; Repeat;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000255"
FT   CHAIN           25..374
FT                   /note="Layilin"
FT                   /id="PRO_0000262507"
FT   TOPO_DOM        25..221
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        222..242
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        243..374
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          37..177
FT                   /note="C-type lectin"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   REPEAT          333..337
FT                   /note="1-1"
FT   REPEAT          343..347
FT                   /note="1-2"
FT   REPEAT          349..352
FT                   /note="2-1"
FT   REPEAT          364..368
FT                   /note="1-3"
FT   REPEAT          370..373
FT                   /note="2-2"
FT   REGION          184..212
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          323..367
FT                   /note="Interaction with NF2"
FT                   /evidence="ECO:0000250"
FT   REGION          330..374
FT                   /note="Interaction with TLN1"
FT                   /evidence="ECO:0000269|PubMed:9786953"
FT   REGION          333..368
FT                   /note="3 X 5 AA repeats of E-S-G-X-V"
FT   REGION          349..373
FT                   /note="2 X 4 AA repeats of N-X-I-Y"
FT   MOD_RES         279
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C351"
FT   MOD_RES         292
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q8C351"
FT   CARBOHYD        109
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        63..176
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
FT   DISULFID        142..168
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00040"
SQ   SEQUENCE   374 AA;  42436 MW;  298A8BA24FB04E1C CRC64;
     MQPGPALQAV LLAVLLSEPR SSKGRLLSGQ LVCRGGTRRP CYKVIYFHDA FQRLNFEEAK
     EACRRDGGQL VSIETEDEQR LIEKFIENLL ASDGDFWIGL RRLEVKQVNN TACQDLYAWT
     DGSTSQFRNW YVDEPSCGSE VCVVMYHQPS APPGIGGSYM FQWNDDRCNM KNNFICKYAD
     EKPSTTPSIR PGGEATEPPT PVLPEETQKE DTKETFKESR EAALNLAYIL IPSIPLFLLL
     VVTSAACWVW ICRRRKQEQP DPTTKEQHTI WPTPHQENSP NLDVYNVIRK QSEADLTEPR
     PDLKNISFRV CSSEAPPDDI SCDYDNMAVN PSESGFVTLA SMESGFVTND IYEFSPDRMG
     RSKESGWVEN EIYY