TCAF2_HUMAN
ID TCAF2_HUMAN Reviewed; 919 AA.
AC A6NFQ2; B4DK02; Q14D25; Q17RQ4; Q8IWQ0; Q8NF84;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-JAN-2008, sequence version 2.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=TRPM8 channel-associated factor 2 {ECO:0000303|PubMed:25559186};
DE AltName: Full=TRP channel-associated factor 2 {ECO:0000303|PubMed:25559186};
GN Name=TCAF2 {ECO:0000312|HGNC:HGNC:26878};
GN Synonyms=FAM115C {ECO:0000312|HGNC:HGNC:26878},
GN FAM139A {ECO:0000312|HGNC:HGNC:26878};
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RA Guo J.H., Yu L.;
RL Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Thalamus;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12690205; DOI=10.1126/science.1083423;
RA Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K.,
RA Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R.,
RA Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A.,
RA Kanematsu E., Gentles S., Christopoulos C.C., Choufani S., Kwasnicka D.,
RA Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S.,
RA Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R.,
RA Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N.,
RA Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E.,
RA Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R.,
RA Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T.,
RA Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W.,
RA Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A.,
RA Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X.,
RA Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E.,
RA Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H.,
RA Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J.,
RA Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 289-919 (ISOFORM 1).
RC TISSUE=Spleen;
RX PubMed=12693554; DOI=10.1093/dnares/10.1.49;
RA Jikuya H., Takano J., Kikuno R., Hirosawa M., Nagase T., Nomura N.,
RA Ohara O.;
RT "Characterization of long cDNA clones from human adult spleen. II. The
RT complete sequences of 81 cDNA clones.";
RL DNA Res. 10:49-57(2003).
RN [7]
RP FUNCTION (ISOFORM 2), INTERACTION WITH TRPM8 AND TRPV6, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=25559186; DOI=10.1083/jcb.201402076;
RA Gkika D., Lemonnier L., Shapovalov G., Gordienko D., Poux C.,
RA Bernardini M., Bokhobza A., Bidaux G., Degerny C., Verreman K., Guarmit B.,
RA Benahmed M., de Launoit Y., Bindels R.J., Fiorio Pla A., Prevarskaya N.;
RT "TRP channel-associated factors are a novel protein family that regulates
RT TRPM8 trafficking and activity.";
RL J. Cell Biol. 208:89-107(2015).
CC -!- FUNCTION: [Isoform 2]: Negatively regulates the plasma membrane cation
CC channel TRPM8 activity. Involved in the recruitment of TRPM8 to the
CC cell surface. Promotes prostate cancer cell migration stimulation in a
CC TRPM8-dependent manner. {ECO:0000269|PubMed:25559186}.
CC -!- SUBUNIT: Isoform 2 interacts with TRPM8 (via N-terminus and C-terminus
CC domains); the interaction inhibits TRPM8 channel activity. Interacts
CC with TRPV6. {ECO:0000269|PubMed:25559186}.
CC -!- SUBCELLULAR LOCATION: [Isoform 2]: Cell membrane
CC {ECO:0000269|PubMed:25559186}. Note=Colocalizes with TRPM8 on the
CC plasma membrane. {ECO:0000269|PubMed:25559186}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A6NFQ2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A6NFQ2-2; Sequence=VSP_031635;
CC Name=3;
CC IsoId=A6NFQ2-3; Sequence=VSP_042050, VSP_042051;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in the prostate and in
CC cancerous prostate samples. {ECO:0000269|PubMed:25559186}.
CC -!- SIMILARITY: Belongs to the TCAF family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC03376.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AY167570; AAN87343.1; -; mRNA.
DR EMBL; AK296318; BAG59014.1; -; mRNA.
DR EMBL; AC073264; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC106862; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236959; EAL23793.1; -; Genomic_DNA.
DR EMBL; BC113530; AAI13531.1; -; mRNA.
DR EMBL; BC117233; AAI17234.1; -; mRNA.
DR EMBL; AK090395; BAC03376.1; ALT_INIT; mRNA.
DR CCDS; CCDS34769.1; -. [A6NFQ2-2]
DR CCDS; CCDS47735.2; -. [A6NFQ2-3]
DR CCDS; CCDS87559.1; -. [A6NFQ2-1]
DR RefSeq; NP_001123497.1; NM_001130025.1.
DR RefSeq; NP_001123498.2; NM_001130026.2. [A6NFQ2-3]
DR RefSeq; NP_775949.2; NM_173678.2. [A6NFQ2-2]
DR RefSeq; XP_006715990.1; XM_006715927.3.
DR RefSeq; XP_006715991.1; XM_006715928.3. [A6NFQ2-2]
DR AlphaFoldDB; A6NFQ2; -.
DR SMR; A6NFQ2; -.
DR BioGRID; 130260; 44.
DR IntAct; A6NFQ2; 20.
DR STRING; 9606.ENSP00000412724; -.
DR MEROPS; M98.A03; -.
DR GlyGen; A6NFQ2; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; A6NFQ2; -.
DR PhosphoSitePlus; A6NFQ2; -.
DR BioMuta; TCAF2; -.
DR EPD; A6NFQ2; -.
DR jPOST; A6NFQ2; -.
DR MassIVE; A6NFQ2; -.
DR MaxQB; A6NFQ2; -.
DR PaxDb; A6NFQ2; -.
DR PeptideAtlas; A6NFQ2; -.
DR PRIDE; A6NFQ2; -.
DR ProteomicsDB; 1064; -. [A6NFQ2-1]
DR ProteomicsDB; 1065; -. [A6NFQ2-2]
DR ProteomicsDB; 1066; -. [A6NFQ2-3]
DR Antibodypedia; 51007; 42 antibodies from 13 providers.
DR DNASU; 285966; -.
DR Ensembl; ENST00000357344.9; ENSP00000349902.4; ENSG00000170379.21. [A6NFQ2-2]
DR Ensembl; ENST00000411935.5; ENSP00000389100.1; ENSG00000170379.21. [A6NFQ2-3]
DR Ensembl; ENST00000425618.3; ENSP00000441099.2; ENSG00000170379.21. [A6NFQ2-3]
DR Ensembl; ENST00000441159.7; ENSP00000404265.2; ENSG00000170379.21. [A6NFQ2-1]
DR Ensembl; ENST00000444908.7; ENSP00000412724.2; ENSG00000170379.21. [A6NFQ2-2]
DR Ensembl; ENST00000643242.1; ENSP00000495809.1; ENSG00000170379.21. [A6NFQ2-2]
DR Ensembl; ENST00000684770.1; ENSP00000506869.1; ENSG00000170379.21. [A6NFQ2-1]
DR GeneID; 285966; -.
DR KEGG; hsa:285966; -.
DR MANE-Select; ENST00000684770.1; ENSP00000506869.1; NM_001363538.2; NP_001350467.1.
DR UCSC; uc003wdf.4; human. [A6NFQ2-1]
DR CTD; 285966; -.
DR GeneCards; TCAF2; -.
DR HGNC; HGNC:26878; TCAF2.
DR HPA; ENSG00000170379; Low tissue specificity.
DR MIM; 616252; gene.
DR neXtProt; NX_A6NFQ2; -.
DR OpenTargets; ENSG00000170379; -.
DR PharmGKB; PA162385772; -.
DR VEuPathDB; HostDB:ENSG00000170379; -.
DR eggNOG; ENOG502QQUS; Eukaryota.
DR GeneTree; ENSGT00390000017365; -.
DR HOGENOM; CLU_011215_0_0_1; -.
DR InParanoid; A6NFQ2; -.
DR OMA; WASQHGR; -.
DR OrthoDB; 1049811at2759; -.
DR PhylomeDB; A6NFQ2; -.
DR TreeFam; TF331520; -.
DR PathwayCommons; A6NFQ2; -.
DR SignaLink; A6NFQ2; -.
DR BioGRID-ORCS; 285966; 5 hits in 1035 CRISPR screens.
DR GenomeRNAi; 285966; -.
DR Pharos; A6NFQ2; Tbio.
DR PRO; PR:A6NFQ2; -.
DR Proteomes; UP000005640; Chromosome 7.
DR RNAct; A6NFQ2; protein.
DR Bgee; ENSG00000170379; Expressed in islet of Langerhans and 103 other tissues.
DR ExpressionAtlas; A6NFQ2; baseline and differential.
DR Genevisible; A6NFQ2; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR GO; GO:0044325; F:transmembrane transporter binding; IDA:MGI.
DR GO; GO:0010360; P:negative regulation of anion channel activity; IDA:UniProtKB.
DR GO; GO:0030335; P:positive regulation of cell migration; IDA:UniProtKB.
DR GO; GO:0090314; P:positive regulation of protein targeting to membrane; IMP:UniProtKB.
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 Alternative splicing; Cell membrane; Membrane; Reference proteome;
KW Transport.
FT CHAIN 1..919
FT /note="TRPM8 channel-associated factor 2"
FT /id="PRO_0000320187"
FT DOMAIN 542..841
FT /note="Peptidase M60"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01060"
FT VAR_SEQ 1..207
FT /note="MATIAAAAFEALMDGVTCWDVPRGPIPSELLLIGEAAFPVMVNDKGQVLIAA
FT SSYGRGRLVVVSHEGYLSHTGLAPFLLNAVSWLCPCPGAPVGVHPSLAPLVNILQDAGL
FT EAQVKPEPGEPLGVYCINAYNDTLTATLIQFVKHGGGLLIGGQAWYWASQHGPDKVLSR
FT FPGNKVTSVAGVYFTDTYGDRDRFKVSKKVPKIPLHV -> MKIFQKEFKFILKKCTPI
FT QKYREENGNSSSSPHHQLQSHASGP (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042050"
FT VAR_SEQ 538
FT /note="P -> PESHSVIQVGMQWRDLSSCNLHLLGLSNSSLSASCVAGTTGTRHHAW
FT LIFVFLVEREFHRK (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_042051"
FT VAR_SEQ 836..919
FT /note="LQEAFGWEPFTQLFAEYQTLSHLPKDNTGRMNLWVKKFSEKVKKNLVPFFEA
FT WGWPIQKEVADSLASLPEWQENPMQVYLRARK -> VLSRNSGRRG (in isoform
FT 2)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_031635"
FT CONFLICT 72
FT /note="T -> A (in Ref. 1; AAN87343 and 5; AAI17234)"
FT /evidence="ECO:0000305"
FT CONFLICT 592
FT /note="V -> M (in Ref. 5; AAI17234 and 6; BAC03376)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 919 AA; 100906 MW; C39AFA211CD43BF8 CRC64;
MATIAAAAFE ALMDGVTCWD VPRGPIPSEL LLIGEAAFPV MVNDKGQVLI AASSYGRGRL
VVVSHEGYLS HTGLAPFLLN AVSWLCPCPG APVGVHPSLA PLVNILQDAG LEAQVKPEPG
EPLGVYCINA YNDTLTATLI QFVKHGGGLL IGGQAWYWAS QHGPDKVLSR FPGNKVTSVA
GVYFTDTYGD RDRFKVSKKV PKIPLHVRYG EDVRQDQQQL LEGISELDIR TGGVPSQLLV
HGALAFPLGL DASLNCFLAA AHYGRGRVVL AAHECLLCAP KMGPFLLNAV RWLARGQTGK
VGVNTNLKDL CPLLSEHGLQ CSLEPHLNSD LCVYCCKAYS DKEAKQLQEF VAEGGGLLIG
GQAWWWASQN PGHCPLAGFP GNIILNCFGL SILPQTLKAG CFPVPTPEMR SYHFRKALSQ
FQAILNHENG NLEKSCLAKL RVDGAAFLQI PAEGVPAYIS LHRLLRKMLR GSGLPAVSRE
NPVASDSYEA AVLSLATGLA HSGTDCSQLA QGLGTWTCSS SLYPSKHPIT VEINGINPGN
NDCWVSTGLY LLEGQNAEVS LSEAAASAGL RVQIGCHTDD LTKARKLSRA PVVTHQCWMD
RTERSVSCLW GGLLYVIVPK GSQLGPVPVT IRGAVPAPYY KLGKTSLEEW KRQMQENLAP
WGELATDNII LTVPTTNLQA LKDPEPVLRL WDEMMQAVAR LAAEPFPFRR PERIVADVQI
SAGWMHSGYP IMCHLESVKE IINEMDMRSR GVWGPIHELG HNQQRHGWEF PPHTTEATCN
LWSVYVHETV LGIPRAQAHE ALSPPERERR IKAHLGKGAP LCDWNVWTAL ETYLQLQEAF
GWEPFTQLFA EYQTLSHLPK DNTGRMNLWV KKFSEKVKKN LVPFFEAWGW PIQKEVADSL
ASLPEWQENP MQVYLRARK
