CLTRN_BOVIN
ID CLTRN_BOVIN Reviewed; 222 AA.
AC Q0VCT4;
DT 10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Collectrin;
DE AltName: Full=Transmembrane protein 27;
DE Flags: Precursor;
GN Name=CLTRN; Synonyms=TMEM27;
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=Fetal cerebellum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays an important role in amino acid transport by acting as
CC binding partner of amino acid transporters SLC6A18 and SLC6A19,
CC regulating their trafficking on the cell surface and their activity (By
CC similarity). May also play a role in trafficking of amino acid
CC transporters SLC3A1 and SLC7A9 to the renal cortical cell membrane (By
CC similarity). Regulator of SNARE complex function (By similarity).
CC Stimulator of beta cell replication (By similarity).
CC {ECO:0000250|UniProtKB:Q9ESG4}.
CC -!- SUBUNIT: Monomer. Homodimer; dimerization prevents CLTRN cleavage by
CC BACE2 (By similarity). Interacts with SLC6A18; this interaction
CC regulates the trafficking of SLC6A18 to the cell membrane and its amino
CC acid transporter activity. Interacts with SLC6A19; this interaction
CC regulates the trafficking of SLC6A19 to the cell membrane and its amino
CC acid transporter activity (By similarity). Interacts with SNAPIN (By
CC similarity). {ECO:0000250|UniProtKB:Q9ESG4,
CC ECO:0000250|UniProtKB:Q9HBJ8}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9ESG4};
CC Single-pass type I membrane protein {ECO:0000255}. Note=Localizes to
CC the brush border membranes of cells in the proximal tubules of kidney.
CC Colocalized with SLC6A19 in the early proximal S1 tubule.
CC {ECO:0000250|UniProtKB:Q9ESG4}.
CC -!- DOMAIN: The cleavage site containing the double Phe-Phe motif acts as
CC negative regulator of shedding by BACE2.
CC {ECO:0000250|UniProtKB:Q9HBJ8}.
CC -!- PTM: Glycosylated. Glycosylation is required for plasma membrane
CC localization and for its cleavage by BACE2.
CC {ECO:0000250|UniProtKB:Q9HBJ8}.
CC -!- PTM: Proteolytically processed in pancreatic beta cells by BACE2
CC leading to the generation and extracellular release of soluble CLTRN,
CC and a corresponding cell-associated C-terminal fragment which is later
CC cleaved by gamma-secretase. This shedding process inactivates CLTRN (By
CC similarity). Three cleavage sites have been identified for BACE2, two
CC clustered sites after Phe-116 and Leu-118 and a more membrane proximal
CC site at Phe-125; the preferred BACE2 cleavage site seems to be between
CC Phe-125 and Leu-126, Phe-116 and Leu-118 act as alternative sites (By
CC similarity). {ECO:0000250|UniProtKB:Q9ESG4,
CC ECO:0000250|UniProtKB:Q9HBJ8}.
CC -!- SIMILARITY: Belongs to the CLTRN family. {ECO:0000305}.
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DR EMBL; BC120016; AAI20017.1; -; mRNA.
DR RefSeq; NP_001069071.1; NM_001075603.1.
DR AlphaFoldDB; Q0VCT4; -.
DR SMR; Q0VCT4; -.
DR STRING; 9913.ENSBTAP00000041744; -.
DR PaxDb; Q0VCT4; -.
DR PRIDE; Q0VCT4; -.
DR Ensembl; ENSBTAT00000063008; ENSBTAP00000055619; ENSBTAG00000048296.
DR GeneID; 513188; -.
DR KEGG; bta:513188; -.
DR CTD; 57393; -.
DR VEuPathDB; HostDB:ENSBTAG00000048296; -.
DR eggNOG; ENOG502RWVW; Eukaryota.
DR GeneTree; ENSGT00940000160862; -.
DR HOGENOM; CLU_108544_1_0_1; -.
DR InParanoid; Q0VCT4; -.
DR OMA; CKPDAQN; -.
DR OrthoDB; 1212584at2759; -.
DR Proteomes; UP000009136; Chromosome X.
DR Bgee; ENSBTAG00000048296; Expressed in metanephros cortex and 107 other tissues.
DR ExpressionAtlas; Q0VCT4; baseline and differential.
DR GO; GO:0031526; C:brush border membrane; IEA:Ensembl.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IEA:Ensembl.
DR GO; GO:0017156; P:calcium-ion regulated exocytosis; IEA:Ensembl.
DR GO; GO:0035773; P:insulin secretion involved in cellular response to glucose stimulus; IEA:Ensembl.
DR GO; GO:0051957; P:positive regulation of amino acid transport; IBA:GO_Central.
DR GO; GO:1905737; P:positive regulation of L-proline import across plasma membrane; IEA:Ensembl.
DR GO; GO:0022898; P:regulation of transmembrane transporter activity; IEA:Ensembl.
DR GO; GO:0035493; P:SNARE complex assembly; IEA:Ensembl.
DR InterPro; IPR042944; Collectrin.
DR InterPro; IPR031588; Collectrin_dom.
DR PANTHER; PTHR46884; PTHR46884; 1.
DR Pfam; PF16959; Collectrin; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Glycoprotein; Membrane; Phosphoprotein; Reference proteome;
KW Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..14
FT /evidence="ECO:0000255"
FT CHAIN 15..222
FT /note="Collectrin"
FT /id="PRO_0000363766"
FT TOPO_DOM 15..141
FT /note="Extracellular"
FT /evidence="ECO:0000250|UniProtKB:Q9HBJ8"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..222
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:Q9HBJ8"
FT SITE 125..126
FT /note="Cleavage by BACE2"
FT /evidence="ECO:0000250|UniProtKB:Q9HBJ8"
FT MOD_RES 214
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESG4"
FT MOD_RES 220
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9ESG4"
FT CARBOHYD 76
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 93
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 222 AA; 25288 MW; B970E50779556B04 CRC64;
MLWLLFFLVT AIHADLCRPD AENAFKVRLS IRTALGDKAY AWDANEEYLF KAMVAFSMRK
VPNRETTEIS HVLLCNVTQR VSFWFVVTDP SRNHTLPAVE VQSAIRMNRN RINNAFFLND
QTLEFLRIPS TLAPPTDPSV PIWIIIFGVI FCIVLVATML LIISGIRQHR RKNKGPSEME
DSEDKCENVI TIENGIPCDP LDMKGGHIND AFVTEDERLT PL
