TCPR1_RAT
ID TCPR1_RAT Reviewed; 1166 AA.
AC Q3ZBA0;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Tectonin beta-propeller repeat-containing protein 1;
GN Name=Tecpr1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Prostate;
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: 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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BC103478; AAI03479.1; -; mRNA.
DR RefSeq; NP_001032268.1; NM_001037191.1.
DR RefSeq; XP_017453805.1; XM_017598316.1.
DR AlphaFoldDB; Q3ZBA0; -.
DR SMR; Q3ZBA0; -.
DR STRING; 10116.ENSRNOP00000001347; -.
DR iPTMnet; Q3ZBA0; -.
DR PhosphoSitePlus; Q3ZBA0; -.
DR PaxDb; Q3ZBA0; -.
DR Ensembl; ENSRNOT00000001347; ENSRNOP00000001347; ENSRNOG00000001010.
DR GeneID; 304285; -.
DR KEGG; rno:304285; -.
DR CTD; 25851; -.
DR RGD; 1306873; Tecpr1.
DR eggNOG; KOG3669; Eukaryota.
DR GeneTree; ENSGT00510000047886; -.
DR HOGENOM; CLU_008303_0_0_1; -.
DR InParanoid; Q3ZBA0; -.
DR OMA; CPMQISR; -.
DR OrthoDB; 119234at2759; -.
DR PhylomeDB; Q3ZBA0; -.
DR TreeFam; TF323648; -.
DR PRO; PR:Q3ZBA0; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000001010; Expressed in frontal cortex and 20 other tissues.
DR Genevisible; Q3ZBA0; RN.
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:0005765; C:lysosomal membrane; ISS:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
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:RGD.
DR GO; GO:1901096; P:regulation of autophagosome maturation; ISO:RGD.
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 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 2: Evidence at transcript level;
KW Autophagy; Cytoplasmic vesicle; Lipid-binding; Lysosome; Membrane;
KW Phosphoprotein; Reference proteome; Repeat.
FT CHAIN 1..1166
FT /note="Tectonin beta-propeller repeat-containing protein 1"
FT /id="PRO_0000337063"
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 403..492
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1147..1166
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 420..435
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 386
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80VP0"
FT MOD_RES 388
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80VP0"
FT MOD_RES 391
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80VP0"
FT MOD_RES 413
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80VP0"
FT MOD_RES 418
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q80VP0"
FT MOD_RES 943
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z6L1"
SQ SEQUENCE 1166 AA; 130187 MW; F7CB6872B2F93BBD CRC64;
MPTSMLWAVD LFGRVYTLST AGQYWELCKD VQLEFKRVSA ATQCCWGIAC DNQVYLYVCS
SDVPIRHREE AYENQRWNPM GGFCEKLLPS DRWSWSDVSG LQHRPLDGVA LPSPYWEWES
DWYVDENFGG EPTEKGGWTY AMDFPATYTR DKKWNSCVRR RKWIRYRRYK SRDTWAKIPS
KDDPKELPDP FNDLSVGGWE ITEEPVGRLS VWAVSLQGKV WYRENVSHPN PEGSSWSLVD
TPGEVVQISC GPHDLIWATL WEGQALVREG ICRNNPKGNS WSIVEPPGSE NGIMHVSAGV
SVVWAITKDR KVWFRRGVNS HNPCGTSWIE MVGEMTMVNV GLNDQVWGIS CEDRAVYFRQ
GVTPSELSGK TWKAIVVGRE SDRSHSGSSS SLLSAGCFFG EEVRGSGTES APSDTDASSE
VERQGPERSL PKESLDNSRN LKGSSSKGHE STRNTEDPME NACLAEGQAK APKTSGPDEC
HGPAPTPAEL PWTNIDLKEP KKASNQPAAG FPETSGLSSL GLFPMGMEEP YGADDHPLWA
WVSGGGCAVE AGSALKWFTV QSGLSPSVQT LSLSITPAQT AAWRKQIFQQ LTERTKRELE
SFRHYEQAVE QSVWVKTGAL QWWCDWKPHK WVDVRVALEQ FTGHDGARDS ILFIYYVVHE
EKKYLHVFLN EVTVLVPVLN EAKHSFALYT PERTRQRWPV RLAATTEQDM NDWLTLLSLS
CCESRKVHGR PSLQAIWSVT CKGDIFVSEP SPDLEAHEHL LPCDQMFWRQ MGGHLRIIEA
NSRGVVWGIG YDHTAWVYTG GYGGGCFQGL ASSTSNIYTQ SDVKSVYIYE NQRWNPVTGY
TSRGLPTDRY MWSDVTGLQE CTKAGTKPPS LQWTWVSDWY VDFSVLGGTD QEGWQYASDF
PASYHGYKTM KDFVRRRCWA RKCKLVTSGP WLEVAPIALS DVSIIPESAD ANGRGHNIAL
WAVSDKGDVL CRLGVSELNP AGSSWLHVGT DQPFASVSIG ACYQVWAVAR DGSAFYRGSV
SPSQPAGDCW YHIPSPPKQK LTQVSVGQTS VYALDENGNL WYRAGITPSY PQGSSWEHVS
NNVRKVSVGP LDQVWVIANK VQGSHGLSRG TVCRRMGVQP REPKGQGWDY GIGGGWDHIS
VRANATRAPR NMSRDQEAHG PGPVCC
