ID   RP1_SAIBB               Reviewed;        2149 AA.
AC   Q8MJ03;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 65.
DE   RecName: Full=Oxygen-regulated protein 1;
DE   AltName: Full=Retinitis pigmentosa RP1 protein homolog;
GN   Name=RP1;
OS   Saimiri boliviensis boliviensis (Bolivian squirrel monkey).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Saimiriinae; Saimiri.
OX   NCBI_TaxID=39432;
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; AY034787; AAK58444.1; -; mRNA.
DR   RefSeq; NP_001266942.1; NM_001280013.1.
DR   AlphaFoldDB; Q8MJ03; -.
DR   SMR; Q8MJ03; -.
DR   STRING; 39432.ENSSBOP00000016672; -.
DR   GeneID; 101034977; -.
DR   CTD; 6101; -.
DR   Proteomes; UP000233220; Whole Genome Shotgun Assembly.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR   GO; GO:0005874; C:microtubule; 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; Microtubule; Reference proteome; Repeat;
KW   Sensory transduction; Vision.
FT   CHAIN           1..2149
FT                   /note="Oxygen-regulated protein 1"
FT                   /id="PRO_0000097413"
FT   DOMAIN          36..118
FT                   /note="Doublecortin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT   DOMAIN          152..231
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          127..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          351..373
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1435..1456
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1583..1613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..24
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1442..1456
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1590..1613
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2149 AA;  239837 MW;  02CDCA902C3A9823 CRC64;
     MSDTPSTGFS MIHPTSSEGQ VPSPRHLSLT HPVVAKRISF YKSGDPQFGG VRVVVNPRSF
     KSFDALLDNL SRKVPLPFGV RNISTPRGRH SITRLEELED GESYLCSHGR KVQPVDLDKA
     RRRPRPWLSS RAVSTHAPPH SVAAPGMPRA PRSLVVFRNG DPKTRRAVLL SRKVTQSFEA
     FLQHLTEVMQ RPVVKLYATD GRRVPSLQAV ILSSGAVVAA GREPFKPGNY DIQKYLLPAR
     LPGISQRVYP KGNGKSESRK ISTHMASSSR SQIYSVSSEK THNNDCYLDY SFVPENYLAL
     EKNDSQNLPI YPSEDDVEKS IIFNQDGTMT VEMKVRFRIK EEETIKWTTT VSKTGPSNND
     EKSEMSFPGR TESRSSGLKL AACSFSADVS PTERSSNQEG SLAEEINIQM TDQEAETCSS
     ASWENATVDT DIIQGTQDQA KHRFYRPPTP GLRRVRQKKS VIGSVTLVSE TEVQEKMIGQ
     FSYSEERESG ENKSEYHMFT HSCSKMSSVS NKPVLVQINN SDQMEESSLE RKKENRLLKS
     SAISAGVIEI TSQKMLELSH NNGLPSTISN NSIVEEDVVD SVVSDNKTGI KNLRTYGNTS
     DRFSPVSADA THFSSNKSRA DKNISEAPAS VASSTVTARI DRLINEFAQC GLTKLPKTEK
     KILSSVASKK KKKKSQQQAI NSRYQDGQLA TTGILNKNER INAGGRITKE MILQDSDSPL
     KGGVLCEEDL RTSETVIESN TFCSKSNLNP MISKNFHRNK LNTTQNSKVQ GLLTKRKSRP
     LRKISLGTPK KREIGQGDKV FPHNESKYSK STCENKSLFH VFNLLEQKPK HFSGPRSQAE
     VASGYLRGMA KKSLVSKVTD SHITLKSQKK QKGDKLKASA ILSKQHAATR ANSLASLKKP
     DFPEDIAHPS VQTYIQNWLH NINPYPTLKP IKSAPVCKNE ISVVNCNNSF SGNDPHTSSG
     KINNFVMESN KHITKIASLT GDNLCKEGDK SFIANDTGED LCETQVGSLN DAYLVSLHEH
     CTSPQSAIND RNTKSRISPE KSGPEINLVY QEINLAKKRQ SVEAAIQVDP IEEDTPKDLL
     PVLMLHQLQA SVPSTPKTQN GVVRMPGSLA DVSFPSAICN SSTNLLLAWL LVLNLKGSMN
     SFCQGDAHKT TNKSSETLAL LEILKHIAIT EEADDLKAAV ANLVESTTNH FGLSEKEQDT
     VPIDLSANCS IVNIQSVPKC NENEGTQGIF SFDGGCSAVE ACAPEVCVLE LTYPPREVCT
     VNKAYVPKET CNLSDTFFPS DGYTVDRTSM NKACFVGEVC SLTDTVFSDK ACAQKENHIY
     EGACATDETC VPVDVCNTTG FLNSKQNTYT DNLESTEELE RGDDVQKDLN ILTDPEYKNG
     FNTLVSHQNV SNLSPCGLCV SEEAEFDKKH SSADDFKNCS LNLFQDKNAY TSFDMEEPRT
     SEEPGSVTNS VTSSERNISE LESFEELENQ DTDIFNTEIN VGEKATEEFI QEEIEASKTL
     ELLDISSKNI MVEERKNGII YETISKRLAT PPSLVFCYDS KQNNEKETNE GETNMVKMMV
     KSMETGSYSE SSPDMKKCIK SPVTSDWSDY RPDSDSEQAY KTSSDDPNDS GELEKEYNIG
     FVKRAIEKLY GKADIIKPSF FPGSTRKSQV CPYNSVEFQC TRRASLYDSE GQSFGSSERV
     SSSSPVLQEF QEEGQDKCDI NHVRNNYCGG DIVEPGTKEN DHSRVLTDIE EGVLIDKGKW
     LLKENHLLRM SYENPGVCGN ADTTSVDTLL DNNSSEVPYS HFGNLAPGPT MDELSSSELE
     ELTQPLELKC NYFKMPHGSD SEPFHEDLLG VHNETCDKER IANHHTEEKC PHQSERICTS
     VTHSFMSAGN KVYPVSDDAI KNQPLPGSNM IHGTLQETDS LDKLYALCGQ HCPILTVTIQ
     PVNEEDRGFA YRKESDIENF LGFYLWMKIH PYLLQTDKNM FREENNKASM RKNLINNATG
     DIFDEFYFSN IFDLMDKRRK QKRINFLELQ EAGNLKKFQP DLKERFCMYF LHTSSLVVGN
     MNSNTQDLSS QTNEIFKAVD ENNNLLNNRF QGSRTNLNQV VRENISRYFF EMLGQACLLD
     ICQVETSLNI SNRNILEELC MFEDENIFIW EEEDILNLTD LESSREQDL