TCAF2_MOUSE
ID TCAF2_MOUSE Reviewed; 919 AA.
AC Q921K8; Q6KAN8; Q922C4;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2001, sequence version 1.
DT 03-AUG-2022, entry version 112.
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, ECO:0000312|MGI:MGI:2385258};
GN Synonyms=Fam115c, Fam139a;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15449545; DOI=10.1093/dnares/11.2.127;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Kitamura H., Nakagawa T., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of FLJ genes: the
RT complete nucleotide sequences of 110 mouse FLJ-homologous cDNAs identified
RT by screening of terminal sequences of cDNA clones randomly sampled from
RT size-fractionated libraries.";
RL DNA Res. 11:127-135(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brown adipose tissue, Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD21419.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AK131169; BAD21419.1; ALT_INIT; mRNA.
DR EMBL; BC008555; AAH08555.1; -; mRNA.
DR EMBL; BC011487; AAH11487.1; -; mRNA.
DR CCDS; CCDS20075.1; -.
DR RefSeq; NP_666286.1; NM_146174.1.
DR AlphaFoldDB; Q921K8; -.
DR BioGRID; 231291; 1.
DR STRING; 10090.ENSMUSP00000031879; -.
DR MEROPS; M98.A03; -.
DR iPTMnet; Q921K8; -.
DR PhosphoSitePlus; Q921K8; -.
DR MaxQB; Q921K8; -.
DR PaxDb; Q921K8; -.
DR PeptideAtlas; Q921K8; -.
DR PRIDE; Q921K8; -.
DR ProteomicsDB; 254674; -.
DR Ensembl; ENSMUST00000031879; ENSMUSP00000031879; ENSMUSG00000029851.
DR GeneID; 232748; -.
DR KEGG; mmu:232748; -.
DR UCSC; uc009brn.1; mouse.
DR CTD; 285966; -.
DR MGI; MGI:2385258; Tcaf2.
DR VEuPathDB; HostDB:ENSMUSG00000029851; -.
DR eggNOG; ENOG502S2AP; Eukaryota.
DR GeneTree; ENSGT00390000017365; -.
DR HOGENOM; CLU_011215_0_0_1; -.
DR InParanoid; Q921K8; -.
DR OMA; WASQHGR; -.
DR OrthoDB; 1049811at2759; -.
DR PhylomeDB; Q921K8; -.
DR TreeFam; TF331520; -.
DR BioGRID-ORCS; 232748; 2 hits in 71 CRISPR screens.
DR ChiTaRS; Tcaf2; mouse.
DR PRO; PR:Q921K8; -.
DR Proteomes; UP000000589; Chromosome 6.
DR RNAct; Q921K8; protein.
DR Bgee; ENSMUSG00000029851; Expressed in parotid gland and 162 other tissues.
DR Genevisible; Q921K8; MM.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR GO; GO:0002244; P:hematopoietic progenitor cell differentiation; IGI:MGI.
DR GO; GO:0010360; P:negative regulation of anion channel activity; ISO:MGI.
DR GO; GO:0030335; P:positive regulation of cell migration; ISO:MGI.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; ISO:MGI.
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 1: Evidence at protein level;
KW Cell membrane; Membrane; Reference proteome; Transport.
FT CHAIN 1..919
FT /note="TRPM8 channel-associated factor 2"
FT /id="PRO_0000320188"
FT DOMAIN 543..842
FT /note="Peptidase M60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01060"
FT CONFLICT 16
FT /note="V -> M (in Ref. 2; AAH08555)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="A -> V (in Ref. 2; AAH08555)"
FT /evidence="ECO:0000305"
FT CONFLICT 91
FT /note="T -> A (in Ref. 2; AAH08555)"
FT /evidence="ECO:0000305"
FT CONFLICT 137
FT /note="K -> E (in Ref. 2; AAH08555)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="A -> T (in Ref. 2; AAH08555)"
FT /evidence="ECO:0000305"
FT CONFLICT 453
FT /note="A -> T (in Ref. 2; AAH08555)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 919 AA; 101598 MW; 1B0819C108C8A5CF CRC64;
MATTPDAAFE ALMNGVTSWD LPKEFTPSEL LLIGEAAFPV MVNDKGQVLI AVSFYGQGRL
VVVSHESYLM HAGLAPFLLN AVSWLCPSPG TPIEVHSSLA SLVNILRGSG INALVQPEPG
EALGVYCIDA YNDTLTKKLV QFVKRGGGLL IGGQAWNWAS QHGSDKVLFS FPGNKVTSVA
GVYFTDVYGD INRFKVSKKI PKIPLYIRCW EELRHDQDQL LDGISMLDVR TGGVPSQLLV
HGSLAFPLGL DNSFLSCFLA AAHYGRGRVV LAAHEAMLCA PKMEPFLLNA IRWLSRGQED
NIGVNTRLKN LNSLLLKHGL KCSLESHLTD DMCVYCCAAY SDQEAKKIQE FVAEGGGLLI
GGQSWWWASQ NPGSSALGSF PGNVILNTFG LSILPRTVSP GCFPILHIDI RNYHFRGALS
EFQAMLNHKE GNLEKRYSGK LGVDGAGFLQ IPAQGVPAYL SVHRILRKIL RQAGLPAVSK
SNPVSSHSYE AAILQLATEL AHSGSDCSQI AHNLSSQTCS SNLSSSEHPI TVEINGTNPG
DRDVWMSTGL YLLEGQSTEI SVSEPAASAG LKVQIGCHTD DLTFAIKLFR APVVTYQCCM
NRTQRSVSCL WGGLLYIIVP KGCQLGPVSV TITNAVPAPY YKLGKTSLEE WKSCIQKNLG
PWGELATDNV ILTVPTASLK TLENPEPLLQ LWDEMMQAVA RLASQPFPFQ RPERIVADVQ
LSAGWMHSGY PIMCHMESVQ ELVSLANIRS KGLWGPIHEL GHNQQCRGWE FPPHTTEATC
NLWSVYVHET VLGIPRAQAH PQLKPEEREK RIKEHLQKGA PLQNWNVWTA LETYLQLQEV
FGWEPFITLF AEYQTIFYIP EDNECKMNIW LKLFSEKVQK NLVPFFEAWG WPIQKDVAED
LACYPSWEDH PLRMYMGSE
