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TCAF1_MOUSE
ID   TCAF1_MOUSE             Reviewed;         924 AA.
AC   Q8BNE1; Q6A005; Q80VG2; Q8BPR4; Q8BTD3; Q8C8Q5; Q8CEM1; Q8CET9; Q8K2D7;
AC   Q9D223;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 124.
DE   RecName: Full=TRPM8 channel-associated factor 1 {ECO:0000250|UniProtKB:Q9Y4C2};
DE   AltName: Full=TRP channel-associated factor 1 {ECO:0000250|UniProtKB:Q9Y4C2};
GN   Name=Tcaf1 {ECO:0000250|UniProtKB:Q9Y4C2, ECO:0000312|MGI:MGI:1914665};
GN   Synonyms=Fam115a, Kiaa0738;
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] (ISOFORM 2).
RX   PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA   Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA   Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA   Nagase T., Ohara O., Koga H.;
RT   "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT   The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT   identified by screening of terminal sequences of cDNA clones randomly
RT   sampled from size-fractionated libraries.";
RL   DNA Res. 11:205-218(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
RC   STRAIN=C57BL/6J;
RC   TISSUE=Eye, Head, Hypothalamus, Pancreas, Retina, and Spinal ganglion;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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).
CC   -!- FUNCTION: Positively 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 inhibition in a TRPM8-dependent
CC       manner. {ECO:0000250|UniProtKB:Q9Y4C2}.
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:Q9Y4C2}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9Y4C2}.
CC       Note=Colocalizes with TRPM8 on the plasma membrane.
CC       {ECO:0000250|UniProtKB:Q9Y4C2}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8BNE1-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8BNE1-2; Sequence=VSP_031634;
CC       Name=3;
CC         IsoId=Q8BNE1-3; Sequence=VSP_031632, VSP_031634;
CC       Name=4;
CC         IsoId=Q8BNE1-4; Sequence=VSP_031633;
CC   -!- DOMAIN: The C-terminal region is necessary for the channel activity
CC       stimulation. {ECO:0000250|UniProtKB:Q9Y4C2}.
CC   -!- SIMILARITY: Belongs to the TCAF family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAD32291.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AK173013; BAD32291.1; ALT_INIT; mRNA.
DR   EMBL; AK004097; BAC25066.1; -; mRNA.
DR   EMBL; AK014379; BAC25433.1; -; mRNA.
DR   EMBL; AK019001; BAC25574.1; -; mRNA.
DR   EMBL; AK020704; BAB32184.1; -; mRNA.
DR   EMBL; AK044692; BAC32035.1; -; mRNA.
DR   EMBL; AK053509; BAC35410.1; -; mRNA.
DR   EMBL; AK083917; BAC39061.1; -; mRNA.
DR   EMBL; AK132148; BAE20997.1; -; mRNA.
DR   EMBL; BC031718; AAH31718.1; -; mRNA.
DR   EMBL; BC043304; AAH43304.1; -; mRNA.
DR   CCDS; CCDS20076.1; -. [Q8BNE1-2]
DR   RefSeq; NP_084206.1; NM_029930.2. [Q8BNE1-2]
DR   RefSeq; XP_006506814.1; XM_006506751.3.
DR   RefSeq; XP_006506815.1; XM_006506752.3. [Q8BNE1-1]
DR   RefSeq; XP_006506816.1; XM_006506753.3. [Q8BNE1-1]
DR   RefSeq; XP_006506817.1; XM_006506754.3. [Q8BNE1-1]
DR   RefSeq; XP_006506818.1; XM_006506755.2.
DR   RefSeq; XP_006506819.1; XM_006506756.2. [Q8BNE1-2]
DR   RefSeq; XP_017177319.1; XM_017321830.1.
DR   AlphaFoldDB; Q8BNE1; -.
DR   BioGRID; 218771; 3.
DR   IntAct; Q8BNE1; 1.
DR   STRING; 10090.ENSMUSP00000036379; -.
DR   MEROPS; M98.A03; -.
DR   iPTMnet; Q8BNE1; -.
DR   PhosphoSitePlus; Q8BNE1; -.
DR   MaxQB; Q8BNE1; -.
DR   PaxDb; Q8BNE1; -.
DR   PeptideAtlas; Q8BNE1; -.
DR   PRIDE; Q8BNE1; -.
DR   ProteomicsDB; 262956; -. [Q8BNE1-1]
DR   ProteomicsDB; 262957; -. [Q8BNE1-2]
DR   ProteomicsDB; 262958; -. [Q8BNE1-3]
DR   ProteomicsDB; 262959; -. [Q8BNE1-4]
DR   Antibodypedia; 66174; 33 antibodies from 11 providers.
DR   DNASU; 77574; -.
DR   Ensembl; ENSMUST00000045054; ENSMUSP00000046137; ENSMUSG00000036667. [Q8BNE1-2]
DR   Ensembl; ENSMUST00000045140; ENSMUSP00000036379; ENSMUSG00000036667. [Q8BNE1-2]
DR   Ensembl; ENSMUST00000121083; ENSMUSP00000114036; ENSMUSG00000036667. [Q8BNE1-2]
DR   GeneID; 77574; -.
DR   KEGG; mmu:77574; -.
DR   UCSC; uc009bro.1; mouse. [Q8BNE1-1]
DR   UCSC; uc009bru.1; mouse. [Q8BNE1-4]
DR   CTD; 9747; -.
DR   MGI; MGI:1914665; Tcaf1.
DR   VEuPathDB; HostDB:ENSMUSG00000036667; -.
DR   eggNOG; ENOG502S2AP; Eukaryota.
DR   GeneTree; ENSGT00390000017365; -.
DR   HOGENOM; CLU_011215_0_0_1; -.
DR   InParanoid; Q8BNE1; -.
DR   OMA; MQIPSSW; -.
DR   OrthoDB; 1049811at2759; -.
DR   PhylomeDB; Q8BNE1; -.
DR   TreeFam; TF331520; -.
DR   BioGRID-ORCS; 77574; 1 hit in 73 CRISPR screens.
DR   ChiTaRS; Tcaf1; mouse.
DR   PRO; PR:Q8BNE1; -.
DR   Proteomes; UP000000589; Chromosome 6.
DR   RNAct; Q8BNE1; protein.
DR   Bgee; ENSMUSG00000036667; Expressed in superior cervical ganglion and 220 other tissues.
DR   Genevisible; Q8BNE1; MM.
DR   GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR   GO; GO:0044325; F:transmembrane transporter binding; ISO:MGI.
DR   GO; GO:0030336; P:negative regulation of cell migration; ISO:MGI.
DR   GO; GO:1901529; P:positive regulation of anion channel activity; 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   2: Evidence at transcript level;
KW   Alternative splicing; Cell membrane; Membrane; Reference proteome;
KW   Transport.
FT   CHAIN           1..924
FT                   /note="TRPM8 channel-associated factor 1"
FT                   /id="PRO_0000320183"
FT   DOMAIN          542..841
FT                   /note="Peptidase M60"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01060"
FT   VAR_SEQ         1..424
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031632"
FT   VAR_SEQ         208..924
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031633"
FT   VAR_SEQ         923..924
FT                   /note="Missing (in isoform 2 and isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15368895,
FT                   ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:16141072"
FT                   /id="VSP_031634"
FT   CONFLICT        169
FT                   /note="A -> E (in Ref. 3; AAH31718)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        439
FT                   /note="K -> Q (in Ref. 2; BAC25433)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        561
FT                   /note="V -> L (in Ref. 3; AAH43304)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   924 AA;  102735 MW;  5C70FD19FF2B4711 CRC64;
     MATPSAAFEA LMNGVTSWDI PEDSVPCELL LIGEASFPIM VNDVGQVLVA ASSYGRGRMV
     VASHEDFLLE SQLFVFLVNA VGWLRSSPNS AIGVHSSLAP LVKILESCGI ESKIEPEVND
     SLGVYCIDAY NETMTDKLVQ FVKRGGGLLI GGEAWDWDTQ GDDDRVLFAF PGNLVTSVAG
     VYFTDNKADT SFFKVSKKMP KIPILVRCDD DLSDDRDELL RGIIDLDITN SDCFPSQLLV
     HGSLAFPLGL DTYHGCVIAA ARYGRGRVVV TGHKVLFTVG KLGPFLLNAV RWLDGGRKGK
     IVVQTELRTL SGLLAVGGID TSIEPHLTSD ASVYCFEPTS DVGVKELQEF VAEGGGLFVG
     TQAWWWAFKN PGVSPLARFP GNLLLNAFGI SITSQSLNPG PFRTPKIGTR TYHFRSTLAE
     FQVIMGRKRG NVEKGWLAKL GPDGATFLQI PAEEIPAYMS VHRLLRKLLS RYRLPVATRE
     NPVINDCCRG AMLSLATGLA HSGSDLSLLI PEIEDVYSSR YLRPSASPIT VNVNCTNPGT
     RYCWMSTGLY IPGRQVIDVS VPESAASADL KIQIGCHTDD LTRASKLFRG PLVINRCCLD
     KPTKSITCLW GGLLYIIVPQ NSKLGSVPLT VKGAVRAPFY KLGETSKEEW KRRLLEYPGP
     WGELATDNII LTVPTANLRT LENPEPLLRL WDEMMQAVAK LGGETFPLRL PQRIVADVQI
     SVGWMHAGYP IMCHLESVQE LINEKLIRTK GLWGPVHELG RNQQRQEWEF PPHTTEATCN
     LWCVYVHETV LGIPRSRANI ALWPPVREKR VRIYLSKGPS VKHWNAWTAL ETYLQLQEAF
     GWEPFIRLFT EYRNQTTSSS PPSDNVDKMN LWVKMFSQQV QRNLAPFFEA WGWPIQKEVA
     TSLAYLPEWK ENIMKLYLLT QMPH
 
 
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