TCAF2_BOVIN
ID TCAF2_BOVIN Reviewed; 914 AA.
AC A6QLU7;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 25-MAY-2022, entry version 53.
DE RecName: Full=TRPM8 channel-associated factor 2 {ECO:0000250|UniProtKB:A6NFQ2};
DE AltName: Full=TRP channel-associated factor 2 {ECO:0000250|UniProtKB:A6NFQ2};
GN Name=TCAF2 {ECO:0000250|UniProtKB:A6NFQ2}; Synonyms=FAM115C, FAM139A;
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=Basal ganglia;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Negatively regulates the plasma membrane cation channel TRPM8
CC activity. Involved in the recruitment of TRPM8 to the cell surface.
CC Promotes prostate cancer cell migration stimulation in a TRPM8-
CC dependent manner. {ECO:0000250|UniProtKB:A6NFQ2}.
CC -!- SUBUNIT: Interacts with TRPM8 (via N-terminus and C-terminus domains);
CC the interaction inhibits TRPM8 channel activity. Interacts with TRPV6.
CC {ECO:0000250|UniProtKB:A6NFQ2}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:A6NFQ2}.
CC Note=Colocalizes with TRPM8 on the plasma membrane.
CC {ECO:0000250|UniProtKB:A6NFQ2}.
CC -!- SIMILARITY: Belongs to the TCAF family. {ECO:0000305}.
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DR EMBL; BC148091; AAI48092.1; -; mRNA.
DR RefSeq; NP_001095394.1; NM_001101924.1.
DR AlphaFoldDB; A6QLU7; -.
DR SMR; A6QLU7; -.
DR STRING; 9913.ENSBTAP00000007200; -.
DR MEROPS; M98.A03; -.
DR PaxDb; A6QLU7; -.
DR PRIDE; A6QLU7; -.
DR GeneID; 510320; -.
DR KEGG; bta:510320; -.
DR CTD; 285966; -.
DR eggNOG; ENOG502QQUS; Eukaryota.
DR InParanoid; A6QLU7; -.
DR OrthoDB; 1049811at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0044325; F:transmembrane transporter binding; IBA:GO_Central.
DR GO; GO:0010360; P:negative regulation of anion channel activity; IBA:GO_Central.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IBA:GO_Central.
DR GO; GO:0010359; P:regulation of anion channel activity; IBA:GO_Central.
DR Gene3D; 1.10.390.30; -; 1.
DR InterPro; IPR029062; Class_I_gatase-like.
DR InterPro; IPR035423; M60-like_N.
DR InterPro; IPR042279; Pep_M60_3.
DR InterPro; IPR031161; Peptidase_M60_dom.
DR Pfam; PF17291; M60-like_N; 1.
DR Pfam; PF13402; Peptidase_M60; 1.
DR SMART; SM01276; M60-like; 1.
DR SUPFAM; SSF52317; SSF52317; 1.
DR PROSITE; PS51723; PEPTIDASE_M60; 1.
PE 2: Evidence at transcript level;
KW Cell membrane; Membrane; Reference proteome; Transport.
FT CHAIN 1..914
FT /note="TRPM8 channel-associated factor 2"
FT /id="PRO_0000320186"
FT DOMAIN 541..840
FT /note="Peptidase M60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01060"
SQ SEQUENCE 914 AA; 99893 MW; F8AE65D670EAA3D5 CRC64;
MATTPAAAFE ALMDGVTSWE LPEGPVPSEL LLTGEAAFPV MVNDKGQVLI AASFYGRGRL
VVVSHEGYLL DAGLARFLLN AVRWLSPSPG APVGVHPSLA SLAHILEGSG VEAQVHPEPA
EPLGVYCISA YNDTMTAELI QFVKRGGGLL IGGQAWHWAS QHGSDQVLSE FPGNQVTSVA
GVYFTDTYGV KGRFKVSKKV PKIPLQVRCG EDLRQDQQQL LEGISELDIG TKGLPSQLLV
HGALAFPLGL DASLRCFLAA ARYGRGRVVL AAHEGMLSAP SLGPFLLNAV RWLAKGQTGK
VGVNTSLEKL HTLLLEHGLE CSLEPHLTSG VCVYCCTAYS DKEAKQLQEF VAEGGGLLIG
GHAWWWASQN PGRSALADFP GNVILNSFGL SILPWTLDPG CFPVPSADSL NYHFRKALSE
FQATLNLEGG NLEKNWLAKL RVDGAAFLQI PAEGVPAYAS LHRLLRKQLR LRLSGFPAVS
RENPVAGDSC EAVVLCLATE LARSGTDCSE LAQGLGAWSC SSNLCPSEHT VEINARNPSD
DAWMSTGLNL PNGQLTEVCL CEAAACAGLK LQIGCHTDNL MSASKLSRAP VVTHQCHMDR
TEQLVSNLWG GLLYVIVPTG CNLGPMSITI KRAVPAPYYK LGETSLEAWR SCIQESPAPW
GELATDNIIL TVPTADLRAL EDPEPLLRLW DEMMEAIARL AAQPFPFRRP ERIVADVQIS
AGWMHSGYPI MCHLESVSEL IDETGMRSRG LWGPVHELGH NQQREQWEFP PHTTEATCNL
WSVYVHETVL GIPRAQAHPA LSPPERENRI KTHLEKGAPL CDWKVWTALE TYLQLQEAFG
WEPFTQLFAE YQTLSDIPND NPGKMNLWVR KFSEKVQKNL APFFEAWGWP VEKEVASSLA
CLPEWEENPM RMYI