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Database: UniProt
Entry: A0A096NRY2_PAPAN
LinkDB: A0A096NRY2_PAPAN
Original site: A0A096NRY2_PAPAN 
ID   A0A096NRY2_PAPAN        Unreviewed;       505 AA.
AC   A0A096NRY2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 56.
DE   RecName: Full=receptor protein serine/threonine kinase {ECO:0000256|ARBA:ARBA00012401};
DE            EC=2.7.11.30 {ECO:0000256|ARBA:ARBA00012401};
GN   Name=ACVR1B {ECO:0000313|Ensembl:ENSPANP00000015802.1};
OS   Papio anubis (Olive baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000015802.1, ECO:0000313|Proteomes:UP000028761};
RN   [1] {ECO:0000313|Ensembl:ENSPANP00000015802.1, ECO:0000313|Proteomes:UP000028761}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA   Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA   Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA   Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA   Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA   Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA   Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA   Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA   Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA   Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA   Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA   Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA   Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA   Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA   Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA   Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA   Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA   Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA   Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA   Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA   Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA   Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA   Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT   "Whole Genome Assembly of Papio anubis.";
RL   Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Ensembl:ENSPANP00000015802.1}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-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_003906444.1; XM_003906395.1.
DR   AlphaFoldDB; A0A096NRY2; -.
DR   SMR; A0A096NRY2; -.
DR   STRING; 9555.ENSPANP00000015802; -.
DR   Ensembl; ENSPANT00000009285.3; ENSPANP00000015802.1; ENSPANG00000013988.3.
DR   GeneID; 101020254; -.
DR   KEGG; panu:101020254; -.
DR   CTD; 91; -.
DR   eggNOG; KOG2052; Eukaryota.
DR   GeneTree; ENSGT00940000157032; -.
DR   HOGENOM; CLU_000288_8_1_1; -.
DR   OMA; VRNTHCC; -.
DR   OrthoDB; 3900892at2759; -.
DR   Proteomes; UP000028761; Chromosome 9.
DR   Bgee; ENSPANG00000013988; Expressed in adult mammalian kidney and 66 other cell types or tissues.
DR   GO; GO:0048179; C:activin receptor complex; IEA:Ensembl.
DR   GO; GO:0009986; C:cell surface; IEA:Ensembl.
DR   GO; GO:0005829; C:cytosol; IEA:Ensembl.
DR   GO; GO:0048185; F:activin binding; IEA:Ensembl.
DR   GO; GO:0016361; F:activin receptor activity, type I; IEA:Ensembl.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019838; F:growth factor binding; IEA:Ensembl.
DR   GO; GO:0070411; F:I-SMAD binding; IEA:Ensembl.
DR   GO; GO:0034711; F:inhibin binding; IEA:Ensembl.
DR   GO; GO:0031625; F:ubiquitin protein ligase binding; IEA:Ensembl.
DR   GO; GO:0097191; P:extrinsic apoptotic signaling pathway; IEA:Ensembl.
DR   GO; GO:0000082; P:G1/S transition of mitotic cell cycle; IEA:Ensembl.
DR   GO; GO:0001942; P:hair follicle development; IEA:Ensembl.
DR   GO; GO:0001701; P:in utero embryonic development; IEA:Ensembl.
DR   GO; GO:0030308; P:negative regulation of cell growth; IEA:Ensembl.
DR   GO; GO:0010629; P:negative regulation of gene expression; IEA:Ensembl.
DR   GO; GO:0038092; P:nodal signaling pathway; IEA:Ensembl.
DR   GO; GO:0032927; P:positive regulation of activin receptor signaling pathway; IEA:Ensembl.
DR   GO; GO:0045648; P:positive regulation of erythrocyte differentiation; IEA:Ensembl.
DR   GO; GO:0010628; P:positive regulation of gene expression; IEA:Ensembl.
DR   GO; GO:1901165; P:positive regulation of trophoblast cell migration; IEA:Ensembl.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:Ensembl.
DR   CDD; cd14143; STKc_TGFbR1_ACVR1b_ACVR1c; 1.
DR   Gene3D; 2.10.60.10; CD59; 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; IPR008271; Ser/Thr_kinase_AS.
DR   InterPro; IPR045860; Snake_toxin-like_sf.
DR   InterPro; IPR000333; TGFB_receptor.
DR   PANTHER; PTHR23255:SF22; ACTIVIN RECEPTOR TYPE-1B; 1.
DR   PANTHER; PTHR23255; TRANSFORMING GROWTH FACTOR-BETA RECEPTOR TYPE I AND II; 1.
DR   Pfam; PF01064; Activin_recp; 1.
DR   Pfam; PF00069; Pkinase; 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}; Kinase {ECO:0000256|ARBA:ARBA00022527};
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}; Receptor {ECO:0000256|ARBA:ARBA00023170};
KW   Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW   Serine/threonine-protein kinase {ECO:0000256|ARBA:ARBA00022527};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   Transferase {ECO:0000256|ARBA:ARBA00022527};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..505
FT                   /note="receptor protein serine/threonine kinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001922670"
FT   TRANSMEM        127..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          177..206
FT                   /note="GS"
FT                   /evidence="ECO:0000259|PROSITE:PS51256"
FT   DOMAIN          207..497
FT                   /note="Protein kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50011"
FT   BINDING         234
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ   SEQUENCE   505 AA;  56920 MW;  454F326DECFA0BFA CRC64;
     MAESARASSF FPLVVLLLAG SGGSGPRGIQ ALLCACTSCL QANYTCETDG ACMVSIFNLD
     GMEHHVRTCI PKVELVPAGK PFYCLSSEDL RNTHCCYTDY CNRIDLRVPS GHLKEPEHPS
     MWGPVELVGI IAGPVFLLFL IIIIVFLVIN YHQRVYHNRQ RLDMEDPSCE MCLSKDKTLQ
     DLVYDLSTSG SGSGLPLFVQ RTVARTIVLQ EIIGKGRFGE VWRGRWRGGD VAVKIFSSRE
     ERSWFREAEI YQTVMLRHEN ILGFIAADNK DNGTWTQLWL VSDYHEHGSL FDYLNRYTVT
     IEGMIKLALS AASGLAHLHM EIVGTQGKPG IAHRDLKSKN ILVKKNGMCA IADLGLAVRH
     DAVTDTIDIA PNQRVGTKRY MAPEVLDETI NMKHFDSFKC ADIYALGLVY WEIARRCNSG
     GVHEEYQLPY YDLVPSDPSI EEMRKVVCDQ KLRPNIPNWW QSYEALRVMG KMMRECWYAN
     GAARLTALRI KKTLSQLSVQ EDVKI
//
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