RP1_BOVIN
ID RP1_BOVIN Reviewed; 2105 AA.
AC Q8MJ05;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 25-MAY-2022, entry version 83.
DE RecName: Full=Oxygen-regulated protein 1;
DE AltName: Full=Retinitis pigmentosa RP1 protein homolog;
GN Name=RP1;
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 [MRNA].
RA Malone K.A.;
RT "Comparative sequencing of RP1: a closer look at a highly divergent retina-
RT specific protein.";
RL Submitted (MAY-2001) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Microtubule-associated protein regulating the stability and
CC length of the microtubule-based axoneme of photoreceptors. Required for
CC the differentiation of photoreceptor cells, it plays a role in the
CC organization of the outer segment of rod and cone photoreceptors
CC ensuring the correct orientation and higher-order stacking of outer
CC segment disks along the photoreceptor axoneme (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts (via the doublecortin domains) with microtubules.
CC Interacts with RP1L1 (By similarity). Interacts with MAK (By
CC similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250}. Cell projection, cilium, photoreceptor outer segment
CC {ECO:0000250}. Note=Specifically localized in the connecting cilia of
CC rod and cone photoreceptors. {ECO:0000250}.
CC -!- DOMAIN: The doublecortin domains, which mediate interaction with
CC microtubules, are required for regulation of microtubule polymerization
CC and function in photoreceptor differentiation. {ECO:0000250}.
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DR EMBL; AY034785; AAK58442.1; -; mRNA.
DR RefSeq; NP_776383.1; NM_173958.1.
DR AlphaFoldDB; Q8MJ05; -.
DR SMR; Q8MJ05; -.
DR BioGRID; 158304; 1.
DR STRING; 9913.ENSBTAP00000014879; -.
DR PaxDb; Q8MJ05; -.
DR PRIDE; Q8MJ05; -.
DR GeneID; 280916; -.
DR KEGG; bta:280916; -.
DR CTD; 6101; -.
DR eggNOG; KOG1181; Eukaryota.
DR eggNOG; KOG3757; Eukaryota.
DR InParanoid; Q8MJ05; -.
DR OrthoDB; 894392at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005875; C:microtubule associated complex; ISS:UniProtKB.
DR GO; GO:0001750; C:photoreceptor outer segment; ISS:UniProtKB.
DR GO; GO:0008017; F:microtubule binding; ISS:UniProtKB.
DR GO; GO:0035082; P:axoneme assembly; ISS:UniProtKB.
DR GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR GO; GO:0042461; P:photoreceptor cell development; ISS:UniProtKB.
DR GO; GO:0045494; P:photoreceptor cell maintenance; ISS:UniProtKB.
DR GO; GO:0035845; P:photoreceptor cell outer segment organization; ISS:UniProtKB.
DR GO; GO:0046549; P:retinal cone cell development; ISS:UniProtKB.
DR GO; GO:0046548; P:retinal rod cell development; ISS:UniProtKB.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 3.10.20.230; -; 2.
DR InterPro; IPR003533; Doublecortin_dom.
DR InterPro; IPR036572; Doublecortin_dom_sf.
DR InterPro; IPR040163; RP1/RP1L1/DCX.
DR PANTHER; PTHR23005; PTHR23005; 1.
DR Pfam; PF03607; DCX; 2.
DR SMART; SM00537; DCX; 2.
DR SUPFAM; SSF89837; SSF89837; 2.
DR PROSITE; PS50309; DC; 2.
PE 2: Evidence at transcript level;
KW Cell projection; Cilium; Cilium biogenesis/degradation; Cytoplasm;
KW Cytoskeleton; Reference proteome; Repeat; Sensory transduction; Vision.
FT CHAIN 1..2105
FT /note="Oxygen-regulated protein 1"
FT /id="PRO_0000097408"
FT DOMAIN 36..118
FT /note="Doublecortin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT DOMAIN 153..232
FT /note="Doublecortin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 252..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..460
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 862..886
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..987
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1406..1440
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1537..1593
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..289
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 403..436
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 947..981
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1417..1440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1541..1584
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 2105 AA; 233979 MW; 73D0C3785842DDF5 CRC64;
MSETPSTSFS MVRRISSEGQ LPSPRQLGIT QPVVAKRISF YKSGDPQFGG VRVVLNPRSF
KTFDALLDNL SGKVPLPFGV RNISTPRGRH SITRLEELED GQSYLCSHGR KVQPVDLDKA
RRRPRPWLSS RALSTHVQRG PAPAAPGMLR APRRLVVFRN GDPKTRRAIV LNRRVTQSFE
VFLQYLTQVM QRPVTKLYAT DGRKVPSLQA VILSSGAVVA AGREPFKPGN YDIQKYLLPA
RLPGISRRVY PKGNARSESR KMSTHVSSSP TSQIYSLSSE KMQNNDSYSD HSFASENYLA
LEKNDSQNLL IYPSEDDVEK SIIFNQDGTM TVEMKIRFKI KEEETIKWTT TLCRADLSNN
GEKSEINSLP GRTDDRSSGV KITACSLSAD VSPLEKGGSQ VDSLAEEANT QVKDQDVETG
SSTSWENPAL DTDATQGTQD RVKHRFYRPP TPGPRRVRQK KSVIGSVTLV SETEVQEKMI
GQFSYNEERK DWENKSEYHM VTHSCSKMSS VSNRPILVQV DNDEQVASSL ERKKESRLLK
SSAVSAGVVE ITSQKTLEMS HNGGLPQTTS EKSIVEEGIV DNVIADNKAR VRNLRTYGNT
DDRSSPFLGD AAHFSSNNPG TDKTISKTPA SVGNSTVTTR IDQLIHEFSH CGLTKLPENE
KQISSSVASK KKMKSQQHVI NSQHQAGEMA TKRIPRKNKR MNTRGRIAQE TILRDSHSSL
KGAILCEKDL HASDTVIESN YFSSKGNNPV NSRNFPRNKL NTIHKPKIQG LLARRKSRPL
NKVNLGGPTK REIGQGEKVF SHNEIGCCKN TFENQNLFHL FNFLEQKPNA FCGPESQAET
ASWYLRGTSK RSLVSKVNNS HITLRSQKKQ KRDKLKSDTT VSKEHVTTRA NSLASLEKAV
FPENVTHHSV QSYVQRWLQN LSPQAALQLG KSAPVYKKER GVASYNNGFL PGNSSHTSSG
KRNDSILQSN RHTTKSASLT GDNLGKRVGM SFDKNSSEEL IQDHCESQTD SLNDTYLLSV
HEFCTLSQSA TDDPNAKSQV SAAKSGQEMS LVYKDINLAA KGPSVETAVQ VDLEGDTPQH
LSPVQLLHQL QALVPSSPKA QNGVVQMPGP LSEVPFPSLI RNSSTNVLLA WLLVLTLKGG
VSSFCPGDAL KATSGSSEAL ALLEVLKHIA VTEEADDLKA AVASLVESTT NHSGLTEKEQ
DVGPIGLSAN CSTPNIQIIP QCAENEKTQK ISLDGSHTAG EEVSEVCVTA VTRSPRKMGT
VVKTYPPEET CHLSEDSFPS DDCTMDQTSM NKACFLGDIS SLTEAVSSHE GCAYEQNHIY
ERADNLELTK ELERVDEVQK DRNILADPGC KHGSNMLVSH QSASSLSPCG SFQNTTESEL
DGEHSFLDKS ESCSLKKFQD KSVYTSFDKE DSKTSEEPGS TTNSMTSSER NVSEMESFEE
LENQNTDIFN IKVNSGEQVT EELIREELEA GKSLELIEVS SRNDAEEGKD GVICETISRK
LVTPPSLVFC YDSKQNMEKE PSEGETETKV RKMVESLEAG SSAESPLNFK SGLRRSGTSD
WSDYRQNSEN EPSYKASSNG PSDSDEEMTP EKECNKGFVK RTIEKLYGKA EMMRPFFFRW
IYTHISGLSC DSVEFQGTGK VGLYDPEGQS LGSLERVSSN STVLQKFPEQ KRDKCDVNNV
RASYPREDIA EHGTKQNDHK TILRDREEGV LIDKGKWLLK ENHLLRLSSP ECSGPCGHAD
TTSVDTLLDN SSTEVPYSHF GNLAPGPNMA ELSSSELEEL TQPPELRCNY FNVPHCSDSE
PFHDDELDTQ DEACAQEREP NHPAEEKGNL RSERVCTSAT HVFASAGNKV HPVSDGAVRN
QPLAGSNVIH GALQEGDSLD KLYNICGQHC PILTVINQPV NEEHRGFAYC KDSDVENSLS
LQLWMKIHPC LRHSSKTMFR DKNNKTISRR ALTDNAVGNT HVWPHFNNTF DLMDRRRKLK
QSNCLGLEEE NNFNKFQSYL KNFLHTLLLV VGQVNSNPQD PSSQTKEFFE VVDENNNLLN
SRFQNSGTNL NQVVREHSYH LSFEMLGQAR LFCQVETFLG ISNRNILEMF YIFEDENLFI
WEEEN
