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Database: UniProt
Entry: A0A1S3G4B1_DIPOR
LinkDB: A0A1S3G4B1_DIPOR
Original site: A0A1S3G4B1_DIPOR 
ID   A0A1S3G4B1_DIPOR        Unreviewed;       443 AA.
AC   A0A1S3G4B1;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE            EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
GN   Name=Acvr1c {ECO:0000313|RefSeq:XP_012883648.1};
OS   Dipodomys ordii (Ord's kangaroo rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Castorimorpha; Heteromyidae;
OC   Dipodomyinae; Dipodomys.
OX   NCBI_TaxID=10020 {ECO:0000313|Proteomes:UP000081671, ECO:0000313|RefSeq:XP_012883648.1};
RN   [1] {ECO:0000313|RefSeq:XP_012883648.1}
RP   IDENTIFICATION.
RC   TISSUE=Kidney {ECO:0000313|RefSeq:XP_012883648.1};
RG   RefSeq;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|ARBA:ARBA00001936};
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004479}; Single-
CC       pass type I membrane protein {ECO:0000256|ARBA:ARBA00004479}.
CC   -!- SIMILARITY: Belongs to the protein kinase superfamily. TKL Ser/Thr
CC       protein kinase family. TGFB receptor subfamily.
CC       {ECO:0000256|ARBA:ARBA00009605}.
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DR   RefSeq; XP_012883648.1; XM_013028194.1.
DR   AlphaFoldDB; A0A1S3G4B1; -.
DR   GeneID; 105994593; -.
DR   KEGG; dord:105994593; -.
DR   CTD; 130399; -.
DR   InParanoid; A0A1S3G4B1; -.
DR   OrthoDB; 3900892at2759; -.
DR   Proteomes; UP000081671; Unplaced.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0004675; F:transmembrane receptor protein serine/threonine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009719; P:response to endogenous stimulus; IEA:UniProt.
DR   CDD; cd14143; STKc_TGFbR1_ACVR1b_ACVR1c; 1.
DR   Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 1.
DR   InterPro; IPR000472; Activin_recp.
DR   InterPro; IPR003605; GS_dom.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   InterPro; IPR000719; Prot_kinase_dom.
DR   InterPro; IPR017441; Protein_kinase_ATP_BS.
DR   InterPro; IPR001245; Ser-Thr/Tyr_kinase_cat_dom.
DR   InterPro; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF58; ACTIVIN RECEPTOR TYPE-1C; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF07714; PK_Tyr_Ser-Thr; 1.
DR   Pfam; PF08515; TGF_beta_GS; 1.
DR   SMART; SM00467; GS; 1.
DR   SMART; SM00220; S_TKc; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   SUPFAM; SSF57302; Snake toxin-like; 1.
DR   PROSITE; PS51256; GS; 1.
DR   PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR   PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR   PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Kinase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Manganese {ECO:0000256|ARBA:ARBA00023211};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU10141};
KW   Receptor {ECO:0000256|ARBA:ARBA00023170,
KW   ECO:0000313|RefSeq:XP_012883648.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000081671};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527,
KW   ECO:0000256|RuleBase:RU000304}; Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527, ECO:0000256|RuleBase:RU000304};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        64..86
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          115..144
FT                   /note="GS"
FT                   /evidence="ECO:0000259|PROSITE:PS51256"
FT   DOMAIN          145..435
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         172
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   443 AA;  49765 MW;  F6027BFDCD12E3A4 CRC64;
     MLTNGKEQVI KSCVSLPELN AQVFCHSSNN VTKTECCFTD FCNNITLHLP TASPRAPKLG
     PTELTIVITV PICLLFIAAM LTIWVCQDRQ CTHRKKKRSN VEEALSECNL GNAGKTLKDL
     IYDVTASGSG SGLPLLVQRT IARTIVLQEI VGKGRFGEVW HGKWCGEDVA VKIFSSRDER
     SWFREAEIYQ TVMLRHENIL GFIAADNKDN GTWTQLWLVS EYHEQGSLYD YLNRNIVTEA
     GMVRLALSIA SGLAHLHMEI VGTQGKPAIA HRDIKSKNIL VKKCETCAIA DLGLAVKHDS
     VLNTIDIPQN PRVGTKRYMA PEMLDDTMNL NIFESFKRAD IYSVGLVYWE IARRCSVGGI
     VEEYQLPYYD MVPSDPSIEE MRKVVCDQKL RPSIPNQWQS CEALRVMGRI MRECWYASGA
     ARLTALRIKK TISQLCVKDD CKA
//
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