TGFA1_BOVIN
ID TGFA1_BOVIN Reviewed; 859 AA.
AC A7MB11;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 25-MAY-2022, entry version 65.
DE RecName: Full=Transforming growth factor-beta receptor-associated protein 1;
DE Short=TGF-beta receptor-associated protein 1;
DE Short=TRAP-1;
DE Short=TRAP1;
GN Name=TGFBRAP1;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Thymus;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Plays a role in the TGF-beta/activin signaling pathway. It
CC associates with inactive heteromeric TGF-beta and activin receptor
CC complexes, mainly through the type II receptor, and is released upon
CC activation of signaling. May recruit SMAD4 to the vicinity of the
CC receptor complex and facilitate its interaction with receptor-regulated
CC Smads, such as SMAD2 (By similarity). {ECO:0000250|UniProtKB:Q8WUH2}.
CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking of the
CC endocytic membrane transport pathway. Believed to act as a component of
CC the putative CORVET endosomal tethering complexes which is proposed to
CC be involved in the Rab5-to-Rab7 endosome conversion probably
CC implicating MON1A/B, and via binding SNAREs and SNARE complexes to
CC mediate tethering and docking events during SNARE-mediated membrane
CC fusion. The CORVET complex is proposed to function as a Rab5 effector
CC to mediate early endosome fusion probably in specific endosome
CC subpopulations. Functions predominantly in APPL1-containing endosomes
CC and in degradative but not recycling trafficking of endocytosed cargo
CC (By similarity). {ECO:0000250|UniProtKB:Q8WUH2}.
CC -!- SUBUNIT: Interacts with TGFBR2 and ACVR2B; in the absence of ligand
CC stimulation. Interacts with TGFBR1, ACVRL1, BMPR1A and ACVR1B; in the
CC absence of ligand stimulation and to a less extent. Interacts with
CC SMAD4; the interaction seems to be mutually exclusive with the
CC interaction of SMAD4 and phosphorylated SMAD2. May interact with ALOX5.
CC Interacts with RAB5C. Interacts with VPS8, VPS11 and VPS16. Component
CC of the putative class C core vacuole/endosome tethering (CORVET)
CC complex; the core of which composed of the class C Vps proteins VPS11,
CC VPS16, VPS18 and VPS33A, is associated with VPS8 and TGFBRAP1 (By
CC similarity). {ECO:0000250|UniProtKB:Q3UR70,
CC ECO:0000250|UniProtKB:Q8WUH2}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Early endosome
CC {ECO:0000250|UniProtKB:Q8WUH2}. Note=Colocalizes with TGF-beta
CC receptors in the absence of signaling. {ECO:0000250|UniProtKB:Q8WUH2}.
CC -!- SIMILARITY: Belongs to the TRAP1 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; BC151278; AAI51279.1; -; mRNA.
DR RefSeq; NP_001095478.1; NM_001102008.1.
DR AlphaFoldDB; A7MB11; -.
DR STRING; 9913.ENSBTAP00000028967; -.
DR PaxDb; A7MB11; -.
DR PRIDE; A7MB11; -.
DR GeneID; 514660; -.
DR KEGG; bta:514660; -.
DR CTD; 9392; -.
DR eggNOG; KOG2063; Eukaryota.
DR InParanoid; A7MB11; -.
DR OrthoDB; 682722at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005769; C:early endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; IBA:GO_Central.
DR GO; GO:0034058; P:endosomal vesicle fusion; IBA:GO_Central.
DR GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR001180; CNH_dom.
DR InterPro; IPR032914; Vam6/VPS39/TRAP1.
DR InterPro; IPR019452; VPS39/TGF_beta_rcpt-assoc_1.
DR InterPro; IPR019453; VPS39/TGF_beta_rcpt-assoc_2.
DR PANTHER; PTHR12894; PTHR12894; 1.
DR Pfam; PF00637; Clathrin; 1.
DR Pfam; PF00780; CNH; 1.
DR Pfam; PF10366; Vps39_1; 1.
DR Pfam; PF10367; Vps39_2; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50219; CNH; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Endosome; Protein transport; Reference proteome; Transport.
FT CHAIN 1..859
FT /note="Transforming growth factor-beta receptor-associated
FT protein 1"
FT /id="PRO_0000345404"
FT DOMAIN 24..297
FT /note="CNH"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00795"
FT REPEAT 563..727
FT /note="CHCR"
SQ SEQUENCE 859 AA; 97006 MW; F056154B83D653E9 CRC64;
MMSTKAFTLV PAIEREQLLS DRDRGLLECV ECCGRNLYVG TSDCFVYHFL LEEKTLPGGS
ATFTATRQLH RHLGFKKAVS ELRAASALSR LLVLCDGCIS LVHMLSLEPV PSGARIKGAT
AFALNENPVS GDPFCVEVCI ISVKRRTIQV FLVYEDRVQI VREVSTPEQP LAVAVDGHFL
CLALTTQYII LNYSTGAAQD LFPFCSEERR PIVKRIGRQE FLLAGPGGLG MFATVAGISQ
RAPVRWSENV IGAAVCFPYV VALDDEFITV HSMLDQQQKQ TLPFKEGHIL QDFEGRVIVA
TSKGVYILVP LPLEKRIQDL LASHRVEEAL VLAKGARRNI PKEKFQVMYR RILLQAGFIQ
FAQLQFLKAK ELFRSGQLDV RELISLYPLL LPTSSSFTRS HPPLHEFADL NQLTQGDQDK
VAKCKRFLMS YLNEVRSTEV ANGYKEDIDT ALLKLYAEAD HDSLLDLLVT ENFCLLPDSA
AWLEKHKKYF ALGLLYHYNH QDAAAVQLWV SIVNGDIQDS TRSDLYEYIV DFLTYSTDPD
LVWRHADWVL QRSQEVGVQV FTKRPLDEQQ SGFNPDDIIS CLKKYPQALV KYLEHLVTER
RLQKEEYHTH LAVLYLDEVL QQRPCTPDKD AEVTETQAKL RRLLQESDLY RVHFLMDRTR
GAGLPLESAI LHGKLEQHEE ALHILVHELA DFPAAEDYCL WRSEGRDPPY RQRLFHLLLA
VYLGPGPAAP ARTVAAVDLL NRHAVEFDAA QVLQLLPGTW SVQLLRPFLM GAMRDSIHAR
RTTQVAVGLA RSENLIYKYD KMKLKGSSVR LSDEKLCQMC QNPFLEPVFV RYPNGGLVHT
HCAASRHTEP SSPSAGART
