ID   RP1_CANLF               Reviewed;        2141 AA.
AC   Q8MJ04;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Oxygen-regulated protein 1;
DE   AltName: Full=Retinitis pigmentosa RP1 protein homolog;
GN   Name=RP1;
OS   Canis lupus familiaris (Dog) (Canis familiaris).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Carnivora; Caniformia; Canidae; Canis.
OX   NCBI_TaxID=9615;
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; AY034786; AAK58443.1; -; mRNA.
DR   AlphaFoldDB; Q8MJ04; -.
DR   SMR; Q8MJ04; -.
DR   STRING; 9615.ENSCAFP00000010380; -.
DR   PaxDb; Q8MJ04; -.
DR   PRIDE; Q8MJ04; -.
DR   eggNOG; KOG1181; Eukaryota.
DR   eggNOG; KOG3757; Eukaryota.
DR   InParanoid; Q8MJ04; -.
DR   Proteomes; UP000002254; Unplaced.
DR   GO; GO:0005930; C:axoneme; IBA:GO_Central.
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:0060041; P:retina development in camera-type eye; IBA:GO_Central.
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..2141
FT                   /note="Oxygen-regulated protein 1"
FT                   /id="PRO_0000097409"
FT   DOMAIN          34..116
FT                   /note="Doublecortin 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT   DOMAIN          156..235
FT                   /note="Doublecortin 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00072"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          126..149
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          259..278
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1432..1458
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1589..1612
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        263..278
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1590..1612
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2141 AA;  240096 MW;  C9EFC5BE189DB694 CRC64;
     MSETSSTSVS MIHRSFEGQG PPRHLSVMHP VVAKKISFYK SGDPQFGGVK VVVNPRSFKT
     FDALLDNLSR KVPLPFGVRN ISTPRGRHSI TRLEELEDGA SYLCSHRRKV QPVDLDKARR
     RPRPWLSSRA ISAHAQRSPP TSIGAAGAPG MLRAPRRLLV FRNGDPKIRR VVIVNRRVTQ
     SFQAFLQHLT EVMRFPVTKL YATDGRKVPS LQAVILSSGA VVAAGREPFK PGNYDIQKYL
     LSARLPGTSH HVYIKGNTRS ESRKMSTHVP SSPRSQIYSV SSGKMHNNDC YSDHSFASEN
     YLALEKNDSR NLLIYPSEDD IEKSIIFNQD GTMTVEMKVR FKIKEEETIK WTTVSRASLS
     HNNEKCEVGC FPGRTDDQSS HLKIAACSLS ADVSSLEKDN NQEVSLTEEI NTRITDQETE
     TCTSVSWENG AMDTNICTRV TQDQAKHHFY RPPTPGPKRV RQKSVRGSVT LVSETEVEEE
     MIRQFSYSEA REDGENKSEY HMFTHSCSKM SSVSNKPLLV QINNNEQMES SLERKKESRL
     LKSGAIRAGV EITNQKMLEM SHNNGSPQTI SENSIVGEVI VDSLTSDNKT NIKILRPYSR
     TRDRFSPILA DTTHSLSNDS GIDKTVSEIP ALVESSTVTT RIDRLINEFA QCDLTNSANE
     KQTSLSVASK KKMKSQQQVI NSRHQIRKIA TKGILSKNKR INTGRRIAQE IILEGSDGSL
     KGGVVCEEDL HVSDTVIESN YCSQSDLNPV NSKNFHVNKL NTLQNPKKFQ GLLAKRKSRP
     LTKVSLGGPT KREIGQGDKV FPHNDFRYCK NNFEDQNLFP MFNFLEQRPS DFCGPQGQAE
     IASWYLGGIT KKNLVSKVNN SHITLKTQKK QKGDKLKSST TVSKQQVTTR ANSLGSLKKA
     VFPEAISHHS VQNYIQRWLQ NTNPHSALQS RKSAPIYKKD RSVVSCNNNG FAGTKSHTSS
     GEGNNFARES NKYITKNASL TENLGKKVGK FFDKVNSEEL SKDLCENQVE SLNDACLLPL
     HENCALSQSA IDDHNTKIQV CAEKLGPEIS LVYQEINVAT KRHSVEAAIQ VDLTEEDTSK
     DPLPILLLRQ LQALVPSIHK TQNGITQMPG SLADIPFSSP ICKSYTNVLL AWLLVLTLKG
     SINSFCQGDA HKTTNRASEI LGLLEVLRHT AITEEADDLK AAVANLVEST TNHFGLTEKE
     QDMVPVGLSA NCSTPNLHRV PKCVENEKTQ KISSGGGHSA SEHCGPEACV SELTCSCQMC
     IVNKTCPPKE TCNLSDIFCP SDGCTVDQTP MNKACFQGEV CSLTDALSSH RACAHEENHS
     RKATCPIDEA YIPNKICNTS DFLIFKENTC TDNLELTEEL ERINKVQKDL NVLADPGCKH
     SFNILVSDQN ISNLSYSSFP INETEPEFDK ERSSVAELKN YSLKTFQGKN AYTSSDKEDS
     KTSEEPGSIT NSMTSSERNI SELESFEELE NQDTDTFHMK VNAREQAAEE LIQKELEASK
     NLQLIDGSRR NITEEEERNG IICEAIRRRL ATPPSLVFCY DSKQNTEKDL NEGETKMRVK
     MMVKSVEIGS YSESSLDFKN DFIGPVTSDW SEFRPSSENE QPYKTSSDGP NGSCEEIVQD
     KDYNKGFVKR TIEKLYSKGE IIKPSFFSGS IHRSQVCPYN SVEFQCARKV DLYDCEGQSF
     GSSEQLSSNS SMLQKFLEEG QDKCDFNDVR ANYHGGDILG HGTKQNDHNR IIRDIEEGVL
     IDKGKWLLKE NHLLRISSPE NSGLYGNADT ISVDTLLNND NEVPYSHFGN LAPDPTMAEL
     SSSELEELSQ PLELKCSYFN MPHCSDSEPF CEDLLDVQNK TCARERIPVH HAEEKANHKS
     ERVCTSVTHG FTSAGNKVHP VSDDTIKNQP LPVNNAIHGA LQEGDSLDKL YAICGQHCPI
     LTVIIQPINE EDRGFAYCKN SDIENFLGLH LWMKVHPYLL PSNKTIFRDA NNKANGRKAF
     IDNAFDDTFD LMDKRKLRNL KGISSLGLEE ENNLKKFQLY LKKKFCVNFL HTSLLIVDNR
     NSDTRDSINQ TNEIFEVVDE NNNFLNSRFQ NSRTNLNQVV RECSDFFFEM HGQTCLFYQV
     ETSLNISNRN TVEIFYVFED ENLFIWEEES QFDLESNDED L