ID   RP1_PAPHA               Reviewed;        2152 AA.
AC   Q8MJ06;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 63.
DE   RecName: Full=Oxygen-regulated protein 1;
DE   AltName: Full=Retinitis pigmentosa RP1 protein homolog;
GN   Name=RP1;
OS   Papio hamadryas (Hamadryas baboon).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC   Cercopithecidae; Cercopithecinae; Papio.
OX   NCBI_TaxID=9557;
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}.
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; AY034784; AAK58441.1; -; mRNA.
DR   AlphaFoldDB; Q8MJ06; -.
DR   SMR; Q8MJ06; -.
DR   PRIDE; Q8MJ06; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005875; C:microtubule associated complex; ISS:UniProtKB.
DR   GO; GO:0001917; C:photoreceptor inner segment; 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; Repeat; Sensory transduction; Vision.
FT   CHAIN           1..2152
FT                   /note="Oxygen-regulated protein 1"
FT                   /id="PRO_0000097412"
FT   DOMAIN          36..118
FT                   /note="Doublecortin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT   DOMAIN          154..233
FT                   /note="Doublecortin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          353..375
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1435..1455
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1587..1616
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2152 AA;  241002 MW;  574BD771E8B14C4C CRC64;
     MSDTPSTGFS IIHPTSSEDQ VPPPRHLSLT HPVVAKRISF YKSGDPQFGG VRVVVNPRSF
     KSFDALLDNL SRKVPLPFGV RNISTPRGRH SITRLEELED GESYLCSHGR KVQPVDLDKA
     RRRPRPWLSS RAISAQAPPH PVAVAAPGKP RAPRSLVVFR NGDPKTRRTV LLSRRVTQSF
     EAFLQHLTEV MQRPVVKLYA TDGRRVPSLQ AVILSSGAVV AAGREPFKPG NYDIQKYLLP
     ARLPGISQRV YPKGNAKSES RKISTHMSSS SRSQIYSVSS EKTHNNDCYL DYSFVPENYL
     ALEKSDSQNL PIYPSEDDIE KSIIFNQDGT MTVEMKVRFR IKEEETIKWT TTVSKTGPSN
     NDEKSEMSFP GRTESRSSGL KLAACSFSAD VSPMERSSDQ EGSLPEEINI QTTDEEAETC
     SSASWENATV DTDITQGTQD QAKHRFYRPP TPGLRRVRQK KSVIGSVTLV SETEVQEKMI
     GQFSYSEERE SGENKSEYHM FAHSCSKMSA VSNKPVLVQI NNNDQMEESL LERKKENRLL
     KSSAISAGVI EITSQKMLEM SHNNGLPSTI SNNSIVEEGV VDSMVSDNKT GIKNFRAYDN
     TNDRFSPISA DATHFSSTNS GTDKNISEAT ASETSSTVTA RIDRLINEFA QCGLTKLPKN
     EKKILSSVAS KKKKKSLQQA INSRYQDGQL ATKGILNKNE RINTRGRIRK EMILQDSDSR
     LKGGILCEED LQTSDTVIES NTFCSKSNLN SMISKNFHRN KLNTTQNSKV QGLLTKRKSK
     SLKKVSLGAP KKREICQGDK VFPHNESKYC KSTFENKSLF HVFNILEQKP KYFYAPQSQA
     EVASGYLRGM AKKSLVTDSH ITLRSQKKQK GDKLKASAVV SKQHATTRAN SLASLKKPDF
     PEDIAHHSVQ NYIQSWLQNI NPYPTLKPIK SAPVCRNEMS VVNCNNNSFP GNDPHKSSGK
     INNFVMESNK HITKIASLTG DNLCKEGDKS FIASDTGEED LHETQVGSLN DAYLVSLHEH
     CTLSQSAIND RNTKRHIAAE KSGPEKKLVY QEINLARKRQ SVEAAIQVDP IEEETPKDLL
     PVLMLHQLQA SVPGISKTQN GVVQMPGSLA NVPFHSAICN SSTNLLLAWL LVLNLKGSMN
     SFCQVDAHKT INKSSETLAL LEILKHIAIT EEADDLKAAV ANLVESTTSH FGLSEKEQDV
     VPLDLSANCS TVSIQSVPKC SENERTQRIS SLDGDCSASE ACAPEVCVLE VTCSPCETWT
     VNKTYPPKET CNPSDTHFPS DGYGVDQTSM NKACFLGEVC SLTDTVFSNK ACAQKENHIY
     EGACPTVETY VPVSVCNTID FFNSKENTYT DNLESTEELE RGDDIQKDLN ILTDPEYKNG
     FNTLVSHQNV SNLSSCRLCL SEKEAELDKK HSSLDDFKNC SLKKFQDENA YTSFDMEEPR
     TSEEPGSITN SMTSSERNIS ELESFEELEN PDTDIFNTVV NGGEQATEEL IQEELEASKT
     LELIDISGKN VMEEKRRNGI IYEIISKRLA TPPSLVFCYD SKQNREKETN EGETKMVKMM
     VKSMEAGSYS ESSPDLKKCI KSPVTSDWSD YRPDSDSEQP YKTSSDDPND SGELAQEKEY
     NIGFVKRAIE KLYGKADIIK PSFFPGSTRK SQVCPYNSVE FQCSRKASLY DSEGQSFGSS
     EQVSTSSPML QEFQEERQDK CDVNGVRNDY YGGDIVEPGT KQNDHSRILT DIEEGVLIDK
     GKWLLKENHL LRMSSENPGM CGNADTTSVD TLLDNNSSEV PYSHFGNLAP VPVMDELSSS
     ELEELTQPLE LKCNYFNMPH GSDSEPFHED VHNETCAKER IANHHTEERG NNHQSERVCT
     SVTHSFTSAS NKVYPVSDDA IKNQPLPGSN MIHGTLQEAD SLDKLYALCG QHCPILTVII
     QPVNEEDRGF AYRKESDIEN FLGFYLWMKI HPYLLQTDKK VFREENNKAS MRQNHIDNAI
     GDIFDQFYFN NTFDLMGKRR KQKRINFLEL EEEGNLKKFQ PDLKERLCMN FLHTSLLVVS
     NMNSDTQDLS SQTNEMFKAV DENNNLLNTG FQGSRTNLNQ IVRENTNCHY FFEMLGQACL
     LDICQVETSL NISNRNTLEE LCMFEGENLF IWEEEDILNL TDLESSREQE DL