Full text data of TECPR1
TECPR1
(KIAA1358)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Tectonin beta-propeller repeat-containing protein 1
Tectonin beta-propeller repeat-containing protein 1
UniProt
Q7Z6L1
ID TCPR1_HUMAN Reviewed; 1165 AA.
AC Q7Z6L1; A8KAD1; B3KPZ1; C9J024; F5GX57; Q96EB0; Q9P2I9; Q9UFR6;
read moreDT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=Tectonin beta-propeller repeat-containing protein 1;
GN Name=TECPR1; Synonyms=KIAA1358;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
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.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA 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.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-1165 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI.
RT The complete sequences of 150 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 418-1165 (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-938 AND SER-949, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE ATG5-ATG12
RP CONJUGATE, AND INTERACTION WITH ATG5 AND WIPI2.
RX PubMed=21575909; DOI=10.1016/j.chom.2011.04.010;
RA Ogawa M., Yoshikawa Y., Kobayashi T., Mimuro H., Fukumatsu M.,
RA Kiga K., Piao Z., Ashida H., Yoshida M., Kakuta S., Koyama T.,
RA Goto Y., Nagatake T., Nagai S., Kiyono H., Kawalec M., Reichhart J.M.,
RA Sasakawa C.;
RT "A Tecpr1-dependent selective autophagy pathway targets bacterial
RT pathogens.";
RL Cell Host Microbe 9:376-389(2011).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE ATG5-ATG12
RP CONJUGATE, INTERACTION WITH ATG5, AND PTDINS(3)P-BINDING.
RX PubMed=22342342; DOI=10.1016/j.molcel.2011.12.036;
RA Chen D., Fan W., Lu Y., Ding X., Chen S., Zhong Q.;
RT "A mammalian autophagosome maturation mechanism mediated by TECPR1 and
RT the Atg12-Atg5 conjugate.";
RL Mol. Cell 45:629-641(2012).
CC -!- FUNCTION: Tethering factor involved in autophagy. Involved in
CC autophagosome maturation by promoting the autophagosome fusion
CC with lysosomes: acts by associating with both the ATG5-ATG12
CC conjugate and phosphatidylinositol-3-phosphate (PtdIns(3)P)
CC present at the surface of autophagosomes. Also involved in
CC selective autophagy against bacterial pathogens, by being required
CC for phagophore/preautophagosomal structure biogenesis and
CC maturation.
CC -!- SUBUNIT: Interacts with ATG5; the interaction is direct. Interacts
CC with WIPI2. Interacts with the ATG5-ATG12 conjugate, the
CC interaction is however mutually exclusive with ATG16, since it
CC does not interact with ATG12-ATG5-ATG16 complex.
CC -!- INTERACTION:
CC Q9NT62:ATG3; NbExp=3; IntAct=EBI-2946676, EBI-988094;
CC Q9H1Y0:ATG5; NbExp=6; IntAct=EBI-2946676, EBI-1047414;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane.
CC Lysosome membrane. Note=Localizes to Lysosome membranes, and binds
CC PtdIns(3)P at the surface of autophagosome. Localizes to
CC autolysosomes, a vesicle formed by the fusion between
CC autophagosomes and lysosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7Z6L1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z6L1-2; Sequence=VSP_033861;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q7Z6L1-3; Sequence=VSP_042969, VSP_042970, VSP_042973;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q7Z6L1-4; Sequence=VSP_042971, VSP_042972;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The PH domain mediates the binding to
CC phosphatidylinositol-3-phosphate (PtdIns(3)P). While full-length
CC protein is unable to bind PtdIns(3)P in vitro, it is assumed that
CC the binding to the ATG5-ATG12 conjugate exposes the PH domain,
CC allowing the association with PtdIns(3)P (PubMed:22342342).
CC -!- SIMILARITY: Belongs to the TECPR1 family.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 9 TECPR repeats.
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DR EMBL; AK057048; BAG51853.1; -; mRNA.
DR EMBL; AK292996; BAF85685.1; -; mRNA.
DR EMBL; AC091654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236956; EAL23891.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76717.1; -; Genomic_DNA.
DR EMBL; BC012529; AAH12529.2; -; mRNA.
DR EMBL; BC053591; AAH53591.1; -; mRNA.
DR EMBL; AB037779; BAA92596.1; -; mRNA.
DR EMBL; AL117495; CAB55961.2; -; mRNA.
DR PIR; T17271; T17271.
DR RefSeq; NP_056210.1; NM_015395.2.
DR RefSeq; XP_005250310.1; XM_005250253.1.
DR RefSeq; XP_005250311.1; XM_005250254.1.
DR UniGene; Hs.592281; -.
DR ProteinModelPortal; Q7Z6L1; -.
DR SMR; Q7Z6L1; 64-173, 820-923.
DR IntAct; Q7Z6L1; 11.
DR STRING; 9606.ENSP00000404923; -.
DR PhosphoSite; Q7Z6L1; -.
DR DMDM; 74738829; -.
DR PaxDb; Q7Z6L1; -.
DR PRIDE; Q7Z6L1; -.
DR Ensembl; ENST00000379795; ENSP00000369121; ENSG00000205356.
DR Ensembl; ENST00000447648; ENSP00000404923; ENSG00000205356.
DR Ensembl; ENST00000542604; ENSP00000441121; ENSG00000205356.
DR GeneID; 25851; -.
DR KEGG; hsa:25851; -.
DR UCSC; uc003upg.4; human.
DR CTD; 25851; -.
DR GeneCards; GC07M097843; -.
DR H-InvDB; HIX0006878; -.
DR HGNC; HGNC:22214; TECPR1.
DR HPA; HPA021061; -.
DR MIM; 614781; gene.
DR neXtProt; NX_Q7Z6L1; -.
DR PharmGKB; PA164726436; -.
DR eggNOG; NOG328700; -.
DR HOGENOM; HOG000007892; -.
DR InParanoid; Q7Z6L1; -.
DR OMA; QYASDFP; -.
DR OrthoDB; EOG7HXCQ5; -.
DR GenomeRNAi; 25851; -.
DR NextBio; 47193; -.
DR PRO; PR:Q7Z6L1; -.
DR ArrayExpress; Q7Z6L1; -.
DR Bgee; Q7Z6L1; -.
DR Genevestigator; Q7Z6L1; -.
DR GO; GO:0000421; C:autophagic vacuole membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0000046; P:autophagic vacuole fusion; IMP:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR006624; Beta-propeller_rpt_TECPR.
DR InterPro; IPR010482; Peroxin/Dysferlin.
DR InterPro; IPR006614; Peroxin/Ferlin.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR Pfam; PF06462; Hyd_WA; 8.
DR Pfam; PF06398; Pex24p; 2.
DR SMART; SM00694; DysFC; 2.
DR SMART; SM00693; DysFN; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00706; TECPR; 11.
DR PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Complete proteome;
KW Cytoplasmic vesicle; Lipid-binding; Lysosome; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 1165 Tectonin beta-propeller repeat-containing
FT protein 1.
FT /FTId=PRO_0000337060.
FT REPEAT 209 240 TECPR 1.
FT REPEAT 254 285 TECPR 2.
FT REPEAT 301 332 TECPR 3.
FT REPEAT 344 376 TECPR 4.
FT DOMAIN 611 717 PH.
FT REPEAT 729 756 TECPR 5.
FT REPEAT 953 984 TECPR 6.
FT REPEAT 998 1029 TECPR 7.
FT REPEAT 1044 1075 TECPR 8.
FT REPEAT 1087 1127 TECPR 9.
FT COMPBIAS 384 391 Poly-Ser.
FT MOD_RES 938 938 Phosphoserine.
FT MOD_RES 949 949 Phosphoserine.
FT VAR_SEQ 1 79 Missing (in isoform 3).
FT /FTId=VSP_042969.
FT VAR_SEQ 219 219 K -> KVLCPCLASQ (in isoform 3).
FT /FTId=VSP_042970.
FT VAR_SEQ 556 556 Q -> QA (in isoform 4).
FT /FTId=VSP_042971.
FT VAR_SEQ 557 557 A -> AG (in isoform 2).
FT /FTId=VSP_033861.
FT VAR_SEQ 836 836 T -> TS (in isoform 4).
FT /FTId=VSP_042972.
FT VAR_SEQ 838 1165 RGLPTDRYMWSDASGLQECTKAGTKPPSLQWAWVSDWFVDF
FT SVPGGTDQEGWQYASDFPASYHGSKTMKDFVRRRCWARKCK
FT LVTSGPWLEVPPIALRDVSIIPESPGAEGSGHSIALWAVSD
FT KGDVLCRLGVSELNPAGSSWLHVGTDQPFASISIGACYQVW
FT AVARDGSAFYRGSVYPSQPAGDCWYHIPSPPRQRLKQVSAG
FT QTSVYALDENGNLWYRQGITPSYPQGSSWEHVSNNVCRVSV
FT GPLDQVWVIANKVQGSHSLSRGTVCHRTGVQPHEPKGHGWD
FT YGIGGGWDHISVRANATRAPRSSSQEQEPSAPPEAHGPVCC
FT -> SRDRISPCW (in isoform 3).
FT /FTId=VSP_042973.
FT VARIANT 733 733 S -> Y (in dbSNP:rs35623371).
FT /FTId=VAR_060190.
FT VARIANT 944 944 P -> L (in dbSNP:rs11762014).
FT /FTId=VAR_062238.
FT CONFLICT 116 116 W -> R (in Ref. 1; BAF85685).
FT CONFLICT 151 151 D -> Y (in Ref. 1; BAG51853).
FT CONFLICT 464 464 A -> T (in Ref. 1; BAF85685).
FT CONFLICT 746 746 S -> T (in Ref. 7; CAB55961).
FT CONFLICT 953 953 I -> T (in Ref. 1; BAF85685).
FT CONFLICT 988 988 P -> L (in Ref. 7; CAB55961).
SQ SEQUENCE 1165 AA; 129696 MW; D396F4128710062D CRC64;
MPNSVLWAVD LFGRVYTLST AGQYWEMCKD SQLEFKRVSA TTQCCWGIAC DNQVYVYVCA
SDVPIRRREE AYENQRWNPM GGFCEKLLLS DRWGWSDVSG LQHRPLDRVA LPSPHWEWES
DWYVDENFGG EPTEKGGWTY AIDFPATYTK DKKWNSCVRR RKWIRYRRYK SRDIWAKIPS
KDDPKELPDP FNDLSVGGWE ITEEPVGRLS VWAVSLQGKV WYREDVSHSN PEGSSWSLLD
TPGEVVQISC GPHDLLWATL WEGQALVREG INRSNPKGSS WSIVEPPGSE NGVMHISVGV
SVVWAVTKDW KVWFRRGVNS HNPCGTSWIE MVGEMTMVNV GMNDQVWGIG CEDRAVYFRQ
GVTPSELSGK TWKAIIAARE CDRSHSGSSS SLLSAGCFFG DEVRGSGESA PSDTDASSEV
ERPGPGQILP AEPLDDSKNA TGNSASGLGA GRTAEDTVED ACPAEGSREA RPNTHPGPAP
TPAELPWTNI DLKEAKKVPS HSAAGFPETT SLSSLGLLPL GLEEPYGVDD HPLWAWVSGG
GCVVEACAMP RWFTVQAGLS SSVHMLSLSI TPAQTAAWRK QIFQQLTERT KRELENFRHY
EQAVEQSVWV KTGALQWWCD WKPHKWVDVR LALEQFTGHD GVRDSILFIY YVVHEEKKYI
HIFLNEVVAL VPVLNETKHS FALYTPERTR QRWPVRLAAA TEQDMNDWLA LLSLSCCESR
KVQGRPSPQA IWSITCKGDI FVSEPSPDLE AHEHPLPCDQ MFWRQMGGHL RMVEANSRGV
VWGIGYDHTA WVYTGGYGGG CFQGLASSTS NIYTQSDVKC VHIYENQRWN PVTGYTSRGL
PTDRYMWSDA SGLQECTKAG TKPPSLQWAW VSDWFVDFSV PGGTDQEGWQ YASDFPASYH
GSKTMKDFVR RRCWARKCKL VTSGPWLEVP PIALRDVSII PESPGAEGSG HSIALWAVSD
KGDVLCRLGV SELNPAGSSW LHVGTDQPFA SISIGACYQV WAVARDGSAF YRGSVYPSQP
AGDCWYHIPS PPRQRLKQVS AGQTSVYALD ENGNLWYRQG ITPSYPQGSS WEHVSNNVCR
VSVGPLDQVW VIANKVQGSH SLSRGTVCHR TGVQPHEPKG HGWDYGIGGG WDHISVRANA
TRAPRSSSQE QEPSAPPEAH GPVCC
//
ID TCPR1_HUMAN Reviewed; 1165 AA.
AC Q7Z6L1; A8KAD1; B3KPZ1; C9J024; F5GX57; Q96EB0; Q9P2I9; Q9UFR6;
read moreDT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 22-JAN-2014, entry version 87.
DE RecName: Full=Tectonin beta-propeller repeat-containing protein 1;
GN Name=TECPR1; Synonyms=KIAA1358;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Trachea;
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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 [2]
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.,
RA Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z.,
RA Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C.,
RA Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J.,
RA Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F.,
RA Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F.,
RA Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H.,
RA Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G.,
RA Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P.,
RA Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J.,
RA Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F.,
RA Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B.,
RA 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.,
RA Mural R.J., Adams M.D., Tsui L.-C.;
RT "Human chromosome 7: DNA sequence and biology.";
RL Science 300:767-772(2003).
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.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA 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.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., 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].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye, and Placenta;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-1165 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10718198; DOI=10.1093/dnares/7.1.65;
RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XVI.
RT The complete sequences of 150 new cDNA clones from brain which code
RT for large proteins in vitro.";
RL DNA Res. 7:65-73(2000).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 418-1165 (ISOFORM 2).
RC TISSUE=Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-938 AND SER-949, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE ATG5-ATG12
RP CONJUGATE, AND INTERACTION WITH ATG5 AND WIPI2.
RX PubMed=21575909; DOI=10.1016/j.chom.2011.04.010;
RA Ogawa M., Yoshikawa Y., Kobayashi T., Mimuro H., Fukumatsu M.,
RA Kiga K., Piao Z., Ashida H., Yoshida M., Kakuta S., Koyama T.,
RA Goto Y., Nagatake T., Nagai S., Kiyono H., Kawalec M., Reichhart J.M.,
RA Sasakawa C.;
RT "A Tecpr1-dependent selective autophagy pathway targets bacterial
RT pathogens.";
RL Cell Host Microbe 9:376-389(2011).
RN [10]
RP FUNCTION, SUBCELLULAR LOCATION, ASSOCIATION WITH THE ATG5-ATG12
RP CONJUGATE, INTERACTION WITH ATG5, AND PTDINS(3)P-BINDING.
RX PubMed=22342342; DOI=10.1016/j.molcel.2011.12.036;
RA Chen D., Fan W., Lu Y., Ding X., Chen S., Zhong Q.;
RT "A mammalian autophagosome maturation mechanism mediated by TECPR1 and
RT the Atg12-Atg5 conjugate.";
RL Mol. Cell 45:629-641(2012).
CC -!- FUNCTION: Tethering factor involved in autophagy. Involved in
CC autophagosome maturation by promoting the autophagosome fusion
CC with lysosomes: acts by associating with both the ATG5-ATG12
CC conjugate and phosphatidylinositol-3-phosphate (PtdIns(3)P)
CC present at the surface of autophagosomes. Also involved in
CC selective autophagy against bacterial pathogens, by being required
CC for phagophore/preautophagosomal structure biogenesis and
CC maturation.
CC -!- SUBUNIT: Interacts with ATG5; the interaction is direct. Interacts
CC with WIPI2. Interacts with the ATG5-ATG12 conjugate, the
CC interaction is however mutually exclusive with ATG16, since it
CC does not interact with ATG12-ATG5-ATG16 complex.
CC -!- INTERACTION:
CC Q9NT62:ATG3; NbExp=3; IntAct=EBI-2946676, EBI-988094;
CC Q9H1Y0:ATG5; NbExp=6; IntAct=EBI-2946676, EBI-1047414;
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane.
CC Lysosome membrane. Note=Localizes to Lysosome membranes, and binds
CC PtdIns(3)P at the surface of autophagosome. Localizes to
CC autolysosomes, a vesicle formed by the fusion between
CC autophagosomes and lysosomes.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q7Z6L1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q7Z6L1-2; Sequence=VSP_033861;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q7Z6L1-3; Sequence=VSP_042969, VSP_042970, VSP_042973;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q7Z6L1-4; Sequence=VSP_042971, VSP_042972;
CC Note=No experimental confirmation available;
CC -!- DOMAIN: The PH domain mediates the binding to
CC phosphatidylinositol-3-phosphate (PtdIns(3)P). While full-length
CC protein is unable to bind PtdIns(3)P in vitro, it is assumed that
CC the binding to the ATG5-ATG12 conjugate exposes the PH domain,
CC allowing the association with PtdIns(3)P (PubMed:22342342).
CC -!- SIMILARITY: Belongs to the TECPR1 family.
CC -!- SIMILARITY: Contains 1 PH domain.
CC -!- SIMILARITY: Contains 9 TECPR repeats.
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DR EMBL; AK057048; BAG51853.1; -; mRNA.
DR EMBL; AK292996; BAF85685.1; -; mRNA.
DR EMBL; AC091654; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH236956; EAL23891.1; -; Genomic_DNA.
DR EMBL; CH471091; EAW76717.1; -; Genomic_DNA.
DR EMBL; BC012529; AAH12529.2; -; mRNA.
DR EMBL; BC053591; AAH53591.1; -; mRNA.
DR EMBL; AB037779; BAA92596.1; -; mRNA.
DR EMBL; AL117495; CAB55961.2; -; mRNA.
DR PIR; T17271; T17271.
DR RefSeq; NP_056210.1; NM_015395.2.
DR RefSeq; XP_005250310.1; XM_005250253.1.
DR RefSeq; XP_005250311.1; XM_005250254.1.
DR UniGene; Hs.592281; -.
DR ProteinModelPortal; Q7Z6L1; -.
DR SMR; Q7Z6L1; 64-173, 820-923.
DR IntAct; Q7Z6L1; 11.
DR STRING; 9606.ENSP00000404923; -.
DR PhosphoSite; Q7Z6L1; -.
DR DMDM; 74738829; -.
DR PaxDb; Q7Z6L1; -.
DR PRIDE; Q7Z6L1; -.
DR Ensembl; ENST00000379795; ENSP00000369121; ENSG00000205356.
DR Ensembl; ENST00000447648; ENSP00000404923; ENSG00000205356.
DR Ensembl; ENST00000542604; ENSP00000441121; ENSG00000205356.
DR GeneID; 25851; -.
DR KEGG; hsa:25851; -.
DR UCSC; uc003upg.4; human.
DR CTD; 25851; -.
DR GeneCards; GC07M097843; -.
DR H-InvDB; HIX0006878; -.
DR HGNC; HGNC:22214; TECPR1.
DR HPA; HPA021061; -.
DR MIM; 614781; gene.
DR neXtProt; NX_Q7Z6L1; -.
DR PharmGKB; PA164726436; -.
DR eggNOG; NOG328700; -.
DR HOGENOM; HOG000007892; -.
DR InParanoid; Q7Z6L1; -.
DR OMA; QYASDFP; -.
DR OrthoDB; EOG7HXCQ5; -.
DR GenomeRNAi; 25851; -.
DR NextBio; 47193; -.
DR PRO; PR:Q7Z6L1; -.
DR ArrayExpress; Q7Z6L1; -.
DR Bgee; Q7Z6L1; -.
DR Genevestigator; Q7Z6L1; -.
DR GO; GO:0000421; C:autophagic vacuole membrane; IDA:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral to membrane; IEA:InterPro.
DR GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IDA:UniProtKB.
DR GO; GO:0000046; P:autophagic vacuole fusion; IMP:UniProtKB.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR006624; Beta-propeller_rpt_TECPR.
DR InterPro; IPR010482; Peroxin/Dysferlin.
DR InterPro; IPR006614; Peroxin/Ferlin.
DR InterPro; IPR011993; PH_like_dom.
DR InterPro; IPR001849; Pleckstrin_homology.
DR Pfam; PF06462; Hyd_WA; 8.
DR Pfam; PF06398; Pex24p; 2.
DR SMART; SM00694; DysFC; 2.
DR SMART; SM00693; DysFN; 2.
DR SMART; SM00233; PH; 1.
DR SMART; SM00706; TECPR; 11.
DR PROSITE; PS50003; PH_DOMAIN; FALSE_NEG.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Complete proteome;
KW Cytoplasmic vesicle; Lipid-binding; Lysosome; Membrane;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat.
FT CHAIN 1 1165 Tectonin beta-propeller repeat-containing
FT protein 1.
FT /FTId=PRO_0000337060.
FT REPEAT 209 240 TECPR 1.
FT REPEAT 254 285 TECPR 2.
FT REPEAT 301 332 TECPR 3.
FT REPEAT 344 376 TECPR 4.
FT DOMAIN 611 717 PH.
FT REPEAT 729 756 TECPR 5.
FT REPEAT 953 984 TECPR 6.
FT REPEAT 998 1029 TECPR 7.
FT REPEAT 1044 1075 TECPR 8.
FT REPEAT 1087 1127 TECPR 9.
FT COMPBIAS 384 391 Poly-Ser.
FT MOD_RES 938 938 Phosphoserine.
FT MOD_RES 949 949 Phosphoserine.
FT VAR_SEQ 1 79 Missing (in isoform 3).
FT /FTId=VSP_042969.
FT VAR_SEQ 219 219 K -> KVLCPCLASQ (in isoform 3).
FT /FTId=VSP_042970.
FT VAR_SEQ 556 556 Q -> QA (in isoform 4).
FT /FTId=VSP_042971.
FT VAR_SEQ 557 557 A -> AG (in isoform 2).
FT /FTId=VSP_033861.
FT VAR_SEQ 836 836 T -> TS (in isoform 4).
FT /FTId=VSP_042972.
FT VAR_SEQ 838 1165 RGLPTDRYMWSDASGLQECTKAGTKPPSLQWAWVSDWFVDF
FT SVPGGTDQEGWQYASDFPASYHGSKTMKDFVRRRCWARKCK
FT LVTSGPWLEVPPIALRDVSIIPESPGAEGSGHSIALWAVSD
FT KGDVLCRLGVSELNPAGSSWLHVGTDQPFASISIGACYQVW
FT AVARDGSAFYRGSVYPSQPAGDCWYHIPSPPRQRLKQVSAG
FT QTSVYALDENGNLWYRQGITPSYPQGSSWEHVSNNVCRVSV
FT GPLDQVWVIANKVQGSHSLSRGTVCHRTGVQPHEPKGHGWD
FT YGIGGGWDHISVRANATRAPRSSSQEQEPSAPPEAHGPVCC
FT -> SRDRISPCW (in isoform 3).
FT /FTId=VSP_042973.
FT VARIANT 733 733 S -> Y (in dbSNP:rs35623371).
FT /FTId=VAR_060190.
FT VARIANT 944 944 P -> L (in dbSNP:rs11762014).
FT /FTId=VAR_062238.
FT CONFLICT 116 116 W -> R (in Ref. 1; BAF85685).
FT CONFLICT 151 151 D -> Y (in Ref. 1; BAG51853).
FT CONFLICT 464 464 A -> T (in Ref. 1; BAF85685).
FT CONFLICT 746 746 S -> T (in Ref. 7; CAB55961).
FT CONFLICT 953 953 I -> T (in Ref. 1; BAF85685).
FT CONFLICT 988 988 P -> L (in Ref. 7; CAB55961).
SQ SEQUENCE 1165 AA; 129696 MW; D396F4128710062D CRC64;
MPNSVLWAVD LFGRVYTLST AGQYWEMCKD SQLEFKRVSA TTQCCWGIAC DNQVYVYVCA
SDVPIRRREE AYENQRWNPM GGFCEKLLLS DRWGWSDVSG LQHRPLDRVA LPSPHWEWES
DWYVDENFGG EPTEKGGWTY AIDFPATYTK DKKWNSCVRR RKWIRYRRYK SRDIWAKIPS
KDDPKELPDP FNDLSVGGWE ITEEPVGRLS VWAVSLQGKV WYREDVSHSN PEGSSWSLLD
TPGEVVQISC GPHDLLWATL WEGQALVREG INRSNPKGSS WSIVEPPGSE NGVMHISVGV
SVVWAVTKDW KVWFRRGVNS HNPCGTSWIE MVGEMTMVNV GMNDQVWGIG CEDRAVYFRQ
GVTPSELSGK TWKAIIAARE CDRSHSGSSS SLLSAGCFFG DEVRGSGESA PSDTDASSEV
ERPGPGQILP AEPLDDSKNA TGNSASGLGA GRTAEDTVED ACPAEGSREA RPNTHPGPAP
TPAELPWTNI DLKEAKKVPS HSAAGFPETT SLSSLGLLPL GLEEPYGVDD HPLWAWVSGG
GCVVEACAMP RWFTVQAGLS SSVHMLSLSI TPAQTAAWRK QIFQQLTERT KRELENFRHY
EQAVEQSVWV KTGALQWWCD WKPHKWVDVR LALEQFTGHD GVRDSILFIY YVVHEEKKYI
HIFLNEVVAL VPVLNETKHS FALYTPERTR QRWPVRLAAA TEQDMNDWLA LLSLSCCESR
KVQGRPSPQA IWSITCKGDI FVSEPSPDLE AHEHPLPCDQ MFWRQMGGHL RMVEANSRGV
VWGIGYDHTA WVYTGGYGGG CFQGLASSTS NIYTQSDVKC VHIYENQRWN PVTGYTSRGL
PTDRYMWSDA SGLQECTKAG TKPPSLQWAW VSDWFVDFSV PGGTDQEGWQ YASDFPASYH
GSKTMKDFVR RRCWARKCKL VTSGPWLEVP PIALRDVSII PESPGAEGSG HSIALWAVSD
KGDVLCRLGV SELNPAGSSW LHVGTDQPFA SISIGACYQV WAVARDGSAF YRGSVYPSQP
AGDCWYHIPS PPRQRLKQVS AGQTSVYALD ENGNLWYRQG ITPSYPQGSS WEHVSNNVCR
VSVGPLDQVW VIANKVQGSH SLSRGTVCHR TGVQPHEPKG HGWDYGIGGG WDHISVRANA
TRAPRSSSQE QEPSAPPEAH GPVCC
//
MIM
614781
*RECORD*
*FIELD* NO
614781
*FIELD* TI
*614781 TECTONIN BETA-PROPELLER REPEAT-CONTAINING 1; TECPR1
;;KIAA1358
*FIELD* TX
read moreDESCRIPTION
TECPR1 has a central role in autophagy and mediates the fusion of
autophagosomes with lysosomes for degradation of autophagosome contents
(Chen et al., 2012).
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Nagase et al. (2000) cloned TECPR1, which they designated
KIAA1358. The transcript contains a repetitive element in its 3-prime
end and the deduced protein contains 1,123 amino acids. RT-PCR analysis
revealed variable TECPR1 expression in all tissues examined. Highest
expression was detected in lung, whole adult brain, and in most specific
adult brain regions examined, and lowest expression was detected in
adult heart, skeletal muscle, pancreas, spleen, and in fetal liver.
Chen et al. (2012) reported that the full-length TECPR1 protein contains
1,165 amino acids. It has a dysferlin (603009) domain near the N
terminus, followed by 4 TECPR beta-propeller repeats, an ATG5
(604261)-ATG12 (609608) interacting region (AIR), a pleckstrin homology
(PH) domain, another beta-propeller repeat, a second dysferlin domain,
and 4 additional beta-propeller repeats near the C terminus.
Epitope-tagged TECPR1 localized to cellular puncta that proved to be
mature autophagic structures, with a subset of TECPR1 colocalizing with
the lysosome marker LAMP2 (309060).
GENE FUNCTION
Behrends et al. (2010) reported a proteomic analysis of the autophagy
interaction network in human cells under conditions of ongoing (basal)
autophagy, revealing 751 interactions among 409 candidate-interacting
proteins with extensive connectivity among subnetworks. TECPR1 was
identified by its interaction with ATG12, ATG3 (609606), and ATG5 and
appeared to be part of a ubiquitin-like transfer cascade subnetwork.
TECPR1 also associated with components of the TRAPP vesicle-tethering
complex, including FLJ12716 (TRAPPC11; 614138), TTC15 (TRAPPC12;
614139), KIAA1012 (TRAPPC8; 614136), TRAPPC2L (610970), TRAPPC3
(610955), TRAPPC4 (610971), and TRAPPC5.
Using coimmunoprecipitation experiments with HEK293 cells, Chen et al.
(2012) found that full-length TECPR1 precipitated with the ATG12-ATG5
conjugate, free ATG5, and free ATG12, but did not precipitate with
ATG12-ATG5 complexes that also included ATG16 (ATG16L1; 610767).
Mutation analysis helped define the central AIR domain required for the
interaction of TECPR1 with ATG12-ATG5 and showed that an N-terminal
dysferlin domain bound free ATG5. Protein-lipid overlay assays revealed
that the isolated PH domain of TECPR1, but not full-length TECPR1,
specifically interacted with phosphatidylinositol-3-phosphate
(PtdIns(3)P). Binding of the AIR domain by ATG12-ATG5 permitted
full-length TECPR1 to interact with PtdIns(3)P. Treatment of human cells
with an agent that elevated lysosomal pH resulted in formation of large
TECPR1- and ATG5-positive autolysosomes. Depletion of TECPR1 in HeLa
cells via short hairpin RNA did not alter autophagophore formation or
lysosomal activity, but inhibited degradation of autophagosome content
and resulted in accumulation of autophagic vacuoles. Both the AIR domain
and PH domain of TECPR1 were required for the autophagic function of
TECPR1. Chen et al. (2012) concluded that TECPR1 is required for
autophagosome maturation. They hypothesized that TECPR1 may function as
a tethering factor to join autophagosomes with lysosomes through its
association with ATG12-ATG5 and PtdIns(3)P.
MAPPING
By radiation hybrid analysis, Nagase et al. (2000) mapped the TECPR1
gene to chromosome 7. Hartz (2012) mapped the TECPR1 gene to chromosome
7q21.3 based on an alignment of the TECPR1 sequence (GenBank GENBANK
AB037779) with the genomic sequence (GRCh37).
*FIELD* RF
1. Behrends, C.; Sowa, M. E.; Gygi, S. P.; Harper, J. W.: Network
organization of the human autophagy system. Nature 466: 68-76, 2010.
2. Chen, D.; Fan, W.; Lu, Y.; Ding, X.; Chen, S.; Zhong, Q.: A mammalian
autophagosome maturation mechanism mediated by TECPR1 and the Atg12-Atg5
conjugate. Molec. Cell 45: 629-641, 2012.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/20/2012.
4. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 65-73, 2000.
*FIELD* CD
Patricia A. Hartz: 8/21/2012
*FIELD* ED
terry: 12/05/2012
carol: 8/21/2012
*RECORD*
*FIELD* NO
614781
*FIELD* TI
*614781 TECTONIN BETA-PROPELLER REPEAT-CONTAINING 1; TECPR1
;;KIAA1358
*FIELD* TX
read moreDESCRIPTION
TECPR1 has a central role in autophagy and mediates the fusion of
autophagosomes with lysosomes for degradation of autophagosome contents
(Chen et al., 2012).
CLONING
By sequencing clones obtained from a size-fractionated fetal brain cDNA
library, Nagase et al. (2000) cloned TECPR1, which they designated
KIAA1358. The transcript contains a repetitive element in its 3-prime
end and the deduced protein contains 1,123 amino acids. RT-PCR analysis
revealed variable TECPR1 expression in all tissues examined. Highest
expression was detected in lung, whole adult brain, and in most specific
adult brain regions examined, and lowest expression was detected in
adult heart, skeletal muscle, pancreas, spleen, and in fetal liver.
Chen et al. (2012) reported that the full-length TECPR1 protein contains
1,165 amino acids. It has a dysferlin (603009) domain near the N
terminus, followed by 4 TECPR beta-propeller repeats, an ATG5
(604261)-ATG12 (609608) interacting region (AIR), a pleckstrin homology
(PH) domain, another beta-propeller repeat, a second dysferlin domain,
and 4 additional beta-propeller repeats near the C terminus.
Epitope-tagged TECPR1 localized to cellular puncta that proved to be
mature autophagic structures, with a subset of TECPR1 colocalizing with
the lysosome marker LAMP2 (309060).
GENE FUNCTION
Behrends et al. (2010) reported a proteomic analysis of the autophagy
interaction network in human cells under conditions of ongoing (basal)
autophagy, revealing 751 interactions among 409 candidate-interacting
proteins with extensive connectivity among subnetworks. TECPR1 was
identified by its interaction with ATG12, ATG3 (609606), and ATG5 and
appeared to be part of a ubiquitin-like transfer cascade subnetwork.
TECPR1 also associated with components of the TRAPP vesicle-tethering
complex, including FLJ12716 (TRAPPC11; 614138), TTC15 (TRAPPC12;
614139), KIAA1012 (TRAPPC8; 614136), TRAPPC2L (610970), TRAPPC3
(610955), TRAPPC4 (610971), and TRAPPC5.
Using coimmunoprecipitation experiments with HEK293 cells, Chen et al.
(2012) found that full-length TECPR1 precipitated with the ATG12-ATG5
conjugate, free ATG5, and free ATG12, but did not precipitate with
ATG12-ATG5 complexes that also included ATG16 (ATG16L1; 610767).
Mutation analysis helped define the central AIR domain required for the
interaction of TECPR1 with ATG12-ATG5 and showed that an N-terminal
dysferlin domain bound free ATG5. Protein-lipid overlay assays revealed
that the isolated PH domain of TECPR1, but not full-length TECPR1,
specifically interacted with phosphatidylinositol-3-phosphate
(PtdIns(3)P). Binding of the AIR domain by ATG12-ATG5 permitted
full-length TECPR1 to interact with PtdIns(3)P. Treatment of human cells
with an agent that elevated lysosomal pH resulted in formation of large
TECPR1- and ATG5-positive autolysosomes. Depletion of TECPR1 in HeLa
cells via short hairpin RNA did not alter autophagophore formation or
lysosomal activity, but inhibited degradation of autophagosome content
and resulted in accumulation of autophagic vacuoles. Both the AIR domain
and PH domain of TECPR1 were required for the autophagic function of
TECPR1. Chen et al. (2012) concluded that TECPR1 is required for
autophagosome maturation. They hypothesized that TECPR1 may function as
a tethering factor to join autophagosomes with lysosomes through its
association with ATG12-ATG5 and PtdIns(3)P.
MAPPING
By radiation hybrid analysis, Nagase et al. (2000) mapped the TECPR1
gene to chromosome 7. Hartz (2012) mapped the TECPR1 gene to chromosome
7q21.3 based on an alignment of the TECPR1 sequence (GenBank GENBANK
AB037779) with the genomic sequence (GRCh37).
*FIELD* RF
1. Behrends, C.; Sowa, M. E.; Gygi, S. P.; Harper, J. W.: Network
organization of the human autophagy system. Nature 466: 68-76, 2010.
2. Chen, D.; Fan, W.; Lu, Y.; Ding, X.; Chen, S.; Zhong, Q.: A mammalian
autophagosome maturation mechanism mediated by TECPR1 and the Atg12-Atg5
conjugate. Molec. Cell 45: 629-641, 2012.
3. Hartz, P. A.: Personal Communication. Baltimore, Md. 8/20/2012.
4. Nagase, T.; Kikuno, R.; Ishikawa, K.; Hirosawa, M.; Ohara, O.:
Prediction of the coding sequences of unidentified human genes. XVI.
The complete sequences of 150 new cDNA clones from brain which code
for large proteins in vitro. DNA Res. 7: 65-73, 2000.
*FIELD* CD
Patricia A. Hartz: 8/21/2012
*FIELD* ED
terry: 12/05/2012
carol: 8/21/2012