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Database: UniProt
Entry: H0VNG9_CAVPO
LinkDB: H0VNG9_CAVPO
Original site: H0VNG9_CAVPO 
ID   H0VNG9_CAVPO            Unreviewed;       860 AA.
AC   H0VNG9;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 2.
DT   27-MAR-2024, entry version 68.
DE   SubName: Full=A-kinase anchoring protein 1 {ECO:0000313|Ensembl:ENSCPOP00000011998.3};
GN   Name=AKAP1 {ECO:0000313|Ensembl:ENSCPOP00000011998.3};
OS   Cavia porcellus (Guinea pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Caviidae;
OC   Cavia.
OX   NCBI_TaxID=10141 {ECO:0000313|Ensembl:ENSCPOP00000011998.3, ECO:0000313|Proteomes:UP000005447};
RN   [1] {ECO:0000313|Proteomes:UP000005447}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2N {ECO:0000313|Proteomes:UP000005447};
RX   PubMed=21993624; DOI=10.1038/nature10530;
RA   Lindblad-Toh K., Garber M., Zuk O., Lin M.F., Parker B.J., Washietl S.,
RA   Kheradpour P., Ernst J., Jordan G., Mauceli E., Ward L.D., Lowe C.B.,
RA   Holloway A.K., Clamp M., Gnerre S., Alfoldi J., Beal K., Chang J.,
RA   Clawson H., Cuff J., Di Palma F., Fitzgerald S., Flicek P., Guttman M.,
RA   Hubisz M.J., Jaffe D.B., Jungreis I., Kent W.J., Kostka D., Lara M.,
RA   Martins A.L., Massingham T., Moltke I., Raney B.J., Rasmussen M.D.,
RA   Robinson J., Stark A., Vilella A.J., Wen J., Xie X., Zody M.C., Baldwin J.,
RA   Bloom T., Chin C.W., Heiman D., Nicol R., Nusbaum C., Young S.,
RA   Wilkinson J., Worley K.C., Kovar C.L., Muzny D.M., Gibbs R.A., Cree A.,
RA   Dihn H.H., Fowler G., Jhangiani S., Joshi V., Lee S., Lewis L.R.,
RA   Nazareth L.V., Okwuonu G., Santibanez J., Warren W.C., Mardis E.R.,
RA   Weinstock G.M., Wilson R.K., Delehaunty K., Dooling D., Fronik C.,
RA   Fulton L., Fulton B., Graves T., Minx P., Sodergren E., Birney E.,
RA   Margulies E.H., Herrero J., Green E.D., Haussler D., Siepel A., Goldman N.,
RA   Pollard K.S., Pedersen J.S., Lander E.S., Kellis M.;
RT   "A high-resolution map of human evolutionary constraint using 29 mammals.";
RL   Nature 478:476-482(2011).
RN   [2] {ECO:0000313|Ensembl:ENSCPOP00000011998.3}
RP   IDENTIFICATION.
RC   STRAIN=2N {ECO:0000313|Ensembl:ENSCPOP00000011998.3};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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DR   EMBL; AAKN02042255; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_003466871.1; XM_003466823.3.
DR   AlphaFoldDB; H0VNG9; -.
DR   STRING; 10141.ENSCPOP00000011998; -.
DR   Ensembl; ENSCPOT00000013457.3; ENSCPOP00000011998.3; ENSCPOG00000013327.4.
DR   GeneID; 100723081; -.
DR   KEGG; cpoc:100723081; -.
DR   CTD; 8165; -.
DR   VEuPathDB; HostDB:ENSCPOG00000013327; -.
DR   eggNOG; KOG2279; Eukaryota.
DR   GeneTree; ENSGT00390000001360; -.
DR   HOGENOM; CLU_016731_0_0_1; -.
DR   InParanoid; H0VNG9; -.
DR   OMA; CLTNIYT; -.
DR   OrthoDB; 4118571at2759; -.
DR   TreeFam; TF105401; -.
DR   Proteomes; UP000005447; Unassembled WGS sequence.
DR   Bgee; ENSCPOG00000013327; Expressed in testis and 13 other cell types or tissues.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005739; C:mitochondrion; IEA:Ensembl.
DR   GO; GO:0034237; F:protein kinase A regulatory subunit binding; IEA:Ensembl.
DR   GO; GO:0003723; F:RNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0140374; P:antiviral innate immune response; IEA:Ensembl.
DR   GO; GO:0006915; P:apoptotic process; IEA:Ensembl.
DR   CDD; cd22395; KH-I_AKAP1; 1.
DR   CDD; cd20407; Tudor_AKAP1; 1.
DR   Gene3D; 2.30.30.140; -; 1.
DR   Gene3D; 2.40.50.90; -; 1.
DR   Gene3D; 3.30.1370.10; K Homology domain, type 1; 1.
DR   InterPro; IPR047368; KH-I_AKAP1.
DR   InterPro; IPR004087; KH_dom.
DR   InterPro; IPR004088; KH_dom_type_1.
DR   InterPro; IPR036612; KH_dom_type_1_sf.
DR   InterPro; IPR018459; RII-bd_1.
DR   InterPro; IPR035437; SNase_OB-fold_sf.
DR   InterPro; IPR002999; Tudor.
DR   InterPro; IPR047367; Tudor_AKAP1.
DR   PANTHER; PTHR22948:SF65; A-KINASE ANCHOR PROTEIN 1, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR22948; TUDOR DOMAIN CONTAINING PROTEIN; 1.
DR   Pfam; PF00013; KH_1; 1.
DR   Pfam; PF10522; RII_binding_1; 1.
DR   Pfam; PF00567; TUDOR; 1.
DR   SMART; SM00322; KH; 1.
DR   SMART; SM00333; TUDOR; 1.
DR   SUPFAM; SSF54791; Eukaryotic type KH-domain (KH-domain type I); 1.
DR   SUPFAM; SSF63748; Tudor/PWWP/MBT; 1.
DR   PROSITE; PS50084; KH_TYPE_1; 1.
DR   PROSITE; PS50304; TUDOR; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005447};
KW   RNA-binding {ECO:0000256|PROSITE-ProRule:PRU00117};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        7..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          715..774
FT                   /note="Tudor"
FT                   /evidence="ECO:0000259|PROSITE:PS50304"
FT   REGION          74..128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          170..199
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          275..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          366..435
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          456..555
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        104..126
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        179..193
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        456..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   860 AA;  92349 MW;  E873FC5A947D5A56 CRC64;
     MAVQFRSLFP LALPGMLALL GWWWFFSRKK QQVSSNKEQA ESGAVALSAG PTTKEPLPTE
     EACSTVVSVP LSVTQLPRNK ESAPSKPSTE PPAPLWMHLP HHRSESSGSL QNTTDVRSQP
     GTRKDNTTKV ELAVMGDKAK PVPLGCPLTF PKDLLFSQEA AEVCKQEPTL SGMPTTEKRG
     AGEKAREREM GGTEGNGDAV LGETVLAKGL LPQERALDPE NGKAFGLAPS GGKIAKGSGS
     LPLVVGPVRA LPKEEYPLGK LPGVLVQSAK EEATQTPWVT SGNARDKDPV GELGKEEALD
     ENEKLEQAAF QIISQVILEA TEEVLATTDQ AAANQPQGRK EEENCAPVSQ ETLMGRDIIE
     PTLATAGAAA SSQDTALPSP GPLAADLPPP KTYVSCLSSP LSSPTKDRKP KNSAHPISLA
     PCPAPDTPLR ESLDQASSLA GDATCVTCML DKSQSVSPVT TSGQCSDSVS MSGLGDSCTE
     TNSSPKDNNR TPPLPASTQP FSNGVLKGEL SDVGTEDGWS VDAEADHSGG SDANSMDSEN
     CWERRKTDDL QNAQAGSNPK KVDLIIWEIE VPKHLVGRLI GKQGRYVSFL KQTSGAKIYI
     STLPYTQNIQ ICHIEGSQHH VDKALNLIGK KFKELNLTNI YAPPLPSLAL PSLPMTSWLM
     LPDGITVEVI VVNQVNAGHL FVQQHTHPTF HALRSLDQQM YLCYSQPGIP TLPTPVKIMV
     ICAAPGVDGA WWRAQVVASY EETNEVEIRY VDYGGYKRVK VDVLRQIRSD FVTLPFQGAE
     VLLDSVMPLS DDDHFSPEAD AAMSEMTGNT ALLAQVTSYS PTGLPLIQLW SVVGDEVVLI
     NRSLVERGLA QWVDSYYLSL
//
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