TCPR1_MOUSE
ID TCPR1_MOUSE Reviewed; 1166 AA.
AC Q80VP0; Q8CHA3; Q8R3E0; Q99KQ5; Q9CVC6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 149.
DE RecName: Full=Tectonin beta-propeller repeat-containing protein 1;
GN Name=Tecpr1; Synonyms=Kiaa1358;
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).
RC TISSUE=Brain;
RX PubMed=12465718; DOI=10.1093/dnares/9.5.179;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Hara Y., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: I.
RT The complete nucleotide sequences of 100 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 9:179-188(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Stomach;
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 1).
RC STRAIN=Czech II, and FVB/N; TISSUE=Mammary tumor, and Olfactory epithelium;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-386; SER-388; SER-391;
RP SER-413 AND SER-418, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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: Tethering factor involved in autophagy. Involved in
CC autophagosome maturation by promoting the autophagosome fusion with
CC lysosomes: acts by associating with both the ATG5-ATG12 conjugate and
CC phosphatidylinositol-3-phosphate (PtdIns(3)P) present at the surface of
CC autophagosomes. Also involved in selective autophagy against bacterial
CC pathogens, by being required for phagophore/preautophagosomal structure
CC biogenesis and maturation (By similarity). {ECO:0000250}.
CC -!- SUBUNIT: Interacts with ATG5; the interaction is direct. Interacts with
CC WIPI2. Interacts with the ATG5-ATG12 conjugate, the interaction is
CC however mutually exclusive with ATG16, since it does not interact with
CC ATG12-ATG5-ATG16 complex.
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, autophagosome membrane
CC {ECO:0000250}. Lysosome membrane {ECO:0000250}. Note=Localizes to
CC Lysosome membranes, and binds PtdIns(3)P at the surface of
CC autophagosome. Localizes to autolysosomes, a vesicle formed by the
CC fusion between autophagosomes and lysosomes (By similarity).
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q80VP0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80VP0-2; Sequence=VSP_033862;
CC -!- DOMAIN: The PH domain mediates the binding to phosphatidylinositol-3-
CC phosphate (PtdIns(3)P). {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TECPR1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH25567.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC41478.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AB093295; BAC41478.1; ALT_INIT; mRNA.
DR EMBL; AK008701; BAB25841.1; -; mRNA.
DR EMBL; AK169888; BAE41437.1; -; mRNA.
DR EMBL; AK170108; BAE41568.1; -; mRNA.
DR EMBL; BC004058; AAH04058.1; -; mRNA.
DR EMBL; BC025567; AAH25567.1; ALT_INIT; mRNA.
DR EMBL; BC046968; AAH46968.1; -; mRNA.
DR CCDS; CCDS39377.1; -. [Q80VP0-1]
DR RefSeq; NP_081686.1; NM_027410.1. [Q80VP0-1]
DR AlphaFoldDB; Q80VP0; -.
DR SMR; Q80VP0; -.
DR BioGRID; 214015; 17.
DR ComplexPortal; CPX-360; ATG5-ATG12-TECPR1 complex.
DR STRING; 10090.ENSMUSP00000082844; -.
DR iPTMnet; Q80VP0; -.
DR PhosphoSitePlus; Q80VP0; -.
DR SwissPalm; Q80VP0; -.
DR EPD; Q80VP0; -.
DR jPOST; Q80VP0; -.
DR MaxQB; Q80VP0; -.
DR PaxDb; Q80VP0; -.
DR PeptideAtlas; Q80VP0; -.
DR PRIDE; Q80VP0; -.
DR ProteomicsDB; 259365; -. [Q80VP0-1]
DR ProteomicsDB; 259366; -. [Q80VP0-2]
DR Antibodypedia; 8742; 126 antibodies from 22 providers.
DR Ensembl; ENSMUST00000085701; ENSMUSP00000082844; ENSMUSG00000066621. [Q80VP0-1]
DR GeneID; 70381; -.
DR KEGG; mmu:70381; -.
DR UCSC; uc009alj.2; mouse. [Q80VP0-1]
DR CTD; 25851; -.
DR MGI; MGI:1917631; Tecpr1.
DR VEuPathDB; HostDB:ENSMUSG00000066621; -.
DR eggNOG; KOG3669; Eukaryota.
DR GeneTree; ENSGT00510000047886; -.
DR HOGENOM; CLU_008303_0_0_1; -.
DR InParanoid; Q80VP0; -.
DR OMA; CPMQISR; -.
DR OrthoDB; 119234at2759; -.
DR PhylomeDB; Q80VP0; -.
DR TreeFam; TF323648; -.
DR BioGRID-ORCS; 70381; 3 hits in 74 CRISPR screens.
DR ChiTaRS; Tecpr1; mouse.
DR PRO; PR:Q80VP0; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; Q80VP0; protein.
DR Bgee; ENSMUSG00000066621; Expressed in lacrimal gland and 249 other tissues.
DR Genevisible; Q80VP0; MM.
DR GO; GO:0000421; C:autophagosome membrane; ISS:UniProtKB.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0032991; C:protein-containing complex; IC:ComplexPortal.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; ISS:UniProtKB.
DR GO; GO:0097352; P:autophagosome maturation; ISS:UniProtKB.
DR GO; GO:0006914; P:autophagy; ISS:UniProtKB.
DR GO; GO:0016236; P:macroautophagy; ISO:MGI.
DR GO; GO:1901096; P:regulation of autophagosome maturation; ISO:MGI.
DR Gene3D; 2.30.29.30; -; 1.
DR InterPro; IPR006624; Beta-propeller_rpt_TECPR.
DR InterPro; IPR010482; Peroxin.
DR InterPro; IPR006614; Peroxin/Ferlin.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR000772; Ricin_B_lectin.
DR Pfam; PF06398; Pex24p; 2.
DR Pfam; PF19193; Tectonin; 3.
DR SMART; SM00694; DysFC; 2.
DR SMART; SM00693; DysFN; 2.
DR SMART; SM00706; TECPR; 11.
PE 1: Evidence at protein level;
KW Alternative splicing; Autophagy; Cytoplasmic vesicle; Lipid-binding;
KW Lysosome; Membrane; Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1166
FT /note="Tectonin beta-propeller repeat-containing protein 1"
FT /id="PRO_0000337061"
FT REPEAT 209..240
FT /note="TECPR 1"
FT REPEAT 254..285
FT /note="TECPR 2"
FT REPEAT 301..332
FT /note="TECPR 3"
FT REPEAT 344..376
FT /note="TECPR 4"
FT DOMAIN 616..722
FT /note="PH"
FT REPEAT 734..761
FT /note="TECPR 5"
FT REPEAT 958..989
FT /note="TECPR 6"
FT REPEAT 1003..1034
FT /note="TECPR 7"
FT REPEAT 1049..1080
FT /note="TECPR 8"
FT REPEAT 1092..1132
FT /note="TECPR 9"
FT REGION 404..496
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 433..461
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 462..477
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6L1"
FT VAR_SEQ 1..141
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12465718"
FT /id="VSP_033862"
FT CONFLICT 725
FT /note="R -> W (in Ref. 1; BAC41478)"
FT /evidence="ECO:0000305"
FT CONFLICT 1014
FT /note="A -> T (in Ref. 3; AAH04058)"
FT /evidence="ECO:0000305"
FT CONFLICT 1159
FT /note="R -> C (in Ref. 3; AAH04058)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1166 AA; 130266 MW; 5DA166A7ACA30908 CRC64;
MPTSVLWAVD LFGRVYTLST AGQYWELCKD VQLEFKRVSA ATQCCWGIAG DNQVYLYVCS
SDVPIRHREE AYENQRWNPM GGFCEKLLPS DRWPWSDVSG LQHRPLDGVA LPSPHWEWES
DWYVDENFGG EPTEKGGWTY AMDFPATYTR DKKWNSCVRR RKWIRYRRYK SRDSWAKIPS
KDDPKELPDP FNDLSVGGWE ITEEPVGRLS VWAVSLQGKV WYREDVSHPN PEGSSWSLVE
TPGEVVQISC GPHDLIWATL WEGQALVREG VCRNNPKGSY WSMVEPPGSE NGIMHVSAGV
SVVWAITKDR KVWFRRGVNS HNPCGTSWIE MVGEMTMVNV GLNDQVWGIS CEDRAVYFRQ
GVTPSELSGK TWKAIVVGRE SDRSHSGSSS SLLSAGCFFG DEVRGSGTES APSDTDASLE
VERQGPEQPL PKEALDNSTN LKGSLSKGHE TSGNTDHSTE NACLTEGKEK APETSRSDEC
RGPASTPAEL PWTNIDLKEP KKVSNQPAAG FPETAGLSSL GLFPMGMEEP YGADDHPLWA
WVSGGACAVE AGSTLKWFTI QSGLSPSVQT LSLSITPAQT AAWRKQIFQQ LTERTKRELE
SFRHYEQAVE QSVWVKTGAL QWWCDWKPHK WVDVRVALEQ FTGHDGARDS ILFIYYVVHE
EKKYLHVFLN EVTVLVPVLN EAKHSFALYT PERTRQRWPV RLAAATEQDM NDWLALLSLS
CCESRKVHGR PSPQAIWSVT CKGDIFVSEP SPDLEARERL LPCDQMFWRQ MGGHLRIIEA
NSRGVVWGIG YDHTAWVYTG GYGGGCFQGL ASSTSNIYTQ SDVKSVYIYE NQRWNPVTGY
TSRGLPTDRF MWSDVTGLQE CTKAGTKPPS LQWTWVSDWY VDFSVPGGTD QEGWQYASDF
PASYHGYKTM KDFVRRRCWA RKCKLVTSGP WLEVAPITLS DVSIIPESAH ADGRGHNVAL
WAVSDKGDVL CRLGVSELNP AGSSWLHVGT DQPFASVSIG ACYQVWAVAR DGSAFYRGSV
SPSQPAGDCW YHIPSPPKQK LTQVSVGQTS VYALDENGNL WYRAGITPSY PQGSSWEHVS
NNVRKVSVGP LDQVWVIANK VQGSHGLSRG TVCRRMGVQP REPKGQGWDY GIGGGWDHIS
VRANATRVPR NMSRDREARG PGPVCC
