CLM9_BOVIN
ID CLM9_BOVIN Reviewed; 255 AA.
AC A5D7B2;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=CMRF35-like molecule 9;
DE Short=CLM-9;
DE AltName: Full=CD300 antigen-like family member G;
DE AltName: CD_antigen=CD300g;
DE Flags: Precursor;
GN Name=CD300LG; Synonyms=CLM9;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Ascending colon;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Receptor which may mediate L-selectin-dependent lymphocyte
CC rollings. Binds SELL in a calcium dependent manner. Binds lymphocyte
CC (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Apical cell membrane
CC {ECO:0000250|UniProtKB:Q1ERP8}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q1ERP8}. Basolateral cell membrane
CC {ECO:0000250|UniProtKB:Q1ERP8}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q1ERP8}. Endosome, multivesicular body membrane
CC {ECO:0000250|UniProtKB:Q1ERP8}; Single-pass type I membrane protein
CC {ECO:0000250|UniProtKB:Q1ERP8}. Note=Transcytoses across the cytoplasm.
CC {ECO:0000250|UniProtKB:Q1ERP8}.
CC -!- DOMAIN: Ig-like V-type domain mediates binding to lymphocyte.
CC {ECO:0000250}.
CC -!- PTM: O-glycosylated with sialylated oligosaccharides. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the CD300 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI40493.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; BC140492; AAI40493.1; ALT_INIT; mRNA.
DR RefSeq; XP_005195820.2; XM_005195763.3.
DR RefSeq; XP_005221013.1; XM_005220956.3.
DR AlphaFoldDB; A5D7B2; -.
DR SMR; A5D7B2; -.
DR STRING; 9913.ENSBTAP00000009774; -.
DR PaxDb; A5D7B2; -.
DR Ensembl; ENSBTAT00000009774; ENSBTAP00000009774; ENSBTAG00000007434.
DR Ensembl; ENSBTAT00000066872; ENSBTAP00000068066; ENSBTAG00000007434.
DR GeneID; 615388; -.
DR KEGG; bta:615388; -.
DR CTD; 146894; -.
DR VEuPathDB; HostDB:ENSBTAG00000007434; -.
DR VGNC; VGNC:27024; CD300LG.
DR eggNOG; ENOG502SURU; Eukaryota.
DR GeneTree; ENSGT00940000162429; -.
DR HOGENOM; CLU_051023_1_0_1; -.
DR InParanoid; A5D7B2; -.
DR OrthoDB; 1494510at2759; -.
DR TreeFam; TF334441; -.
DR Proteomes; UP000009136; Chromosome 19.
DR Bgee; ENSBTAG00000007434; Expressed in bone marrow and 100 other tissues.
DR ExpressionAtlas; A5D7B2; baseline and differential.
DR GO; GO:0016324; C:apical plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016323; C:basolateral plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0032585; C:multivesicular body membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IBA:GO_Central.
DR GO; GO:0002376; P:immune system process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.10; -; 1.
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; IPR013106; Ig_V-set.
DR Pfam; PF07686; V-set; 1.
DR SMART; SM00409; IG; 1.
DR SUPFAM; SSF48726; SSF48726; 1.
DR PROSITE; PS50835; IG_LIKE; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Disulfide bond; Endosome; Glycoprotein; Immunity;
KW Immunoglobulin domain; Membrane; Receptor; Reference proteome; Signal;
KW Transmembrane; Transmembrane helix.
FT SIGNAL 1..17
FT /evidence="ECO:0000250"
FT CHAIN 18..255
FT /note="CMRF35-like molecule 9"
FT /id="PRO_0000306111"
FT TOPO_DOM 18..170
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..255
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 18..118
FT /note="Ig-like V-type"
FT REGION 130..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 206..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 131..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 206..230
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 125
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 131
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 132
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 138
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 142
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 146
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 147
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 148
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT CARBOHYD 149
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 152
FT /note="O-linked (GalNAc...) threonine"
FT /evidence="ECO:0000255"
FT CARBOHYD 153
FT /note="O-linked (GalNAc...) serine"
FT /evidence="ECO:0000255"
FT DISULFID 37..104
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
SQ SEQUENCE 255 AA; 27988 MW; 9FE30A61AAB5F1D0 CRC64;
MRPLLMLWGC LVLPGYGSVV NPKEISGFEG DTVSLQCTYE EELKKHQKYW CREAGLFISR
CTGTVFSGEY GQEGRVSVHD NPRENRFTVI LRNLTLKDRG KYLCGVKRLG FDKTMSVSLL
VFPGTSLHPA TSPPAGISQP ATQLDSTSTE DTSFVPSSSS KSRVSIPLIR ILAPVLVLLA
LLLATGLAAL GNYMFQRREK AQLASETQKK DKVHLSHLTS EDDEASWRDP KGDMTPASTL
PMSGDEPGFS KFSSV
