RPGR1_BOVIN
ID RPGR1_BOVIN Reviewed; 1221 AA.
AC Q9GLM3; Q9GLJ5; Q9GLJ6; Q9GLJ7;
DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=X-linked retinitis pigmentosa GTPase regulator-interacting protein 1;
DE Short=RPGR-interacting protein 1;
GN Name=RPGRIP1;
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] (ISOFORMS 1; 2; 3 AND 4), INTERACTION WITH RPGR,
RP AND TISSUE SPECIFICITY.
RC TISSUE=Retina;
RX PubMed=10958648; DOI=10.1093/hmg/9.14.2095;
RA Roepman R., Bernoud-Hubac N., Schick D.E., Maugeri A., Berger W.,
RA Ropers H.-H., Cremers F.P.M., Ferreira P.A.;
RT "The retinitis pigmentosa GTPase regulator (RPGR) interacts with novel
RT transport-like proteins in the outer segments of rod photoreceptors.";
RL Hum. Mol. Genet. 9:2095-2105(2000).
RN [2]
RP TISSUE SPECIFICITY.
RX PubMed=12140192; DOI=10.1093/hmg/11.16.1899;
RA Mavlyutov T.A., Zhao H., Ferreira P.A.;
RT "Species-specific subcellular localization of RPGR and RPGRIP isoforms:
RT implications for the phenotypic variability of congenital retinopathies
RT among species.";
RL Hum. Mol. Genet. 11:1899-1907(2002).
RN [3]
RP INTERACTION WITH SPATA7.
RX PubMed=25398945; DOI=10.1093/hmg/ddu573;
RA Eblimit A., Nguyen T.M., Chen Y., Esteve-Rudd J., Zhong H., Letteboer S.,
RA van Reeuwijk J., Simons D.L., Ding Q., Wu K.M., Li Y., van Beersum S.,
RA Moayedi Y., Xu H., Pickard P., Wang K., Gan L., Wu S.M., Williams D.S.,
RA Mardon G., Roepman R., Chen R.;
RT "Spata7 is a retinal ciliopathy gene critical for correct RPGRIP1
RT localization and protein trafficking in the retina.";
RL Hum. Mol. Genet. 24:1584-1601(2015).
CC -!- FUNCTION: May function as scaffolding protein. Required for normal
CC location of RPGR at the connecting cilium of photoreceptor cells.
CC Required for normal disk morphogenesis and disk organization in the
CC outer segment of photoreceptor cells and for survival of photoreceptor
CC cells. {ECO:0000250|UniProtKB:Q9EPQ2}.
CC -!- SUBUNIT: Forms homodimers and elongated homopolymers (By similarity).
CC Interacts with NPHP4 (By similarity). Interacts with NEK4 (By
CC similarity). Interacts with RPGR (PubMed:10958648). Interacts with
CC SPATA7 (PubMed:25398945). Interacts with CEP290/NPHP6; mediating the
CC association between RPGR and CEP290/NPHP6 (By similarity).
CC {ECO:0000250|UniProtKB:Q96KN7, ECO:0000269|PubMed:10958648,
CC ECO:0000269|PubMed:25398945}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium
CC {ECO:0000250|UniProtKB:Q9EPQ2}. Note=Situated between the axonemal
CC microtubules and the plasma membrane (By similarity). In the retinal
CC photoreceptor cell layer, localizes at the connecting cilium, a thin
CC bridge linking the cell body and the light-sensing outer segment (By
CC similarity). Colocalizes with RGPR in the photoreceptor connecting
CC cilium,(at protein level) (By similarity).
CC {ECO:0000250|UniProtKB:Q9EPQ2}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q9GLM3-1; Sequence=Displayed;
CC Name=2; Synonyms=a;
CC IsoId=Q9GLM3-2; Sequence=VSP_009516;
CC Name=3; Synonyms=b;
CC IsoId=Q9GLM3-3; Sequence=VSP_009518;
CC Name=4; Synonyms=c;
CC IsoId=Q9GLM3-4; Sequence=VSP_009517;
CC -!- TISSUE SPECIFICITY: Retina, brain, skeletal muscle and kidney.
CC Colocalizes with RGPR in the outer segment of rod photoreceptors and
CC cone outer segments. {ECO:0000269|PubMed:10958648,
CC ECO:0000269|PubMed:12140192}.
CC -!- DOMAIN: The C2 domain does not bind calcium ions, and does not bind
CC phosphoinositides. {ECO:0000250|UniProtKB:Q96KN7}.
CC -!- SIMILARITY: Belongs to the RPGRIP1 family. {ECO:0000305}.
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DR EMBL; AF227258; AAG10247.1; -; mRNA.
DR EMBL; AF265668; AAG10002.1; -; mRNA.
DR EMBL; AF265669; AAG10003.1; -; mRNA.
DR EMBL; AF265670; AAG10004.1; -; mRNA.
DR RefSeq; NP_851377.1; NM_181034.2. [Q9GLM3-1]
DR AlphaFoldDB; Q9GLM3; -.
DR SMR; Q9GLM3; -.
DR IntAct; Q9GLM3; 4.
DR STRING; 9913.ENSBTAP00000050597; -.
DR PaxDb; Q9GLM3; -.
DR PRIDE; Q9GLM3; -.
DR GeneID; 282656; -.
DR KEGG; bta:282656; -.
DR CTD; 57096; -.
DR eggNOG; ENOG502R3GU; Eukaryota.
DR InParanoid; Q9GLM3; -.
DR OrthoDB; 152378at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0035869; C:ciliary transition zone; IBA:GO_Central.
DR GO; GO:0032391; C:photoreceptor connecting cilium; ISS:UniProtKB.
DR GO; GO:1905515; P:non-motile cilium assembly; IBA:GO_Central.
DR GO; GO:0050896; P:response to stimulus; IEA:UniProtKB-KW.
DR GO; GO:0046548; P:retinal rod cell development; IBA:GO_Central.
DR GO; GO:0007601; P:visual perception; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.150; -; 3.
DR InterPro; IPR021656; C2-C2_1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR031134; RPGRIP1.
DR InterPro; IPR041091; RPGRIP1_C.
DR InterPro; IPR031139; RPGRIP1_fam.
DR PANTHER; PTHR14240; PTHR14240; 1.
DR PANTHER; PTHR14240:SF3; PTHR14240:SF3; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF11618; C2-C2_1; 1.
DR Pfam; PF18111; RPGR1_C; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 2.
DR PROSITE; PS50004; C2; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell projection; Cilium; Coiled coil;
KW Reference proteome; Sensory transduction; Vision.
FT CHAIN 1..1221
FT /note="X-linked retinitis pigmentosa GTPase regulator-
FT interacting protein 1"
FT /id="PRO_0000097431"
FT DOMAIN 723..843
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 68..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..196
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 869..947
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1027..1216
FT /note="Interaction with RPGR"
FT /evidence="ECO:0000250|UniProtKB:Q96KN7"
FT COILED 267..533
FT /evidence="ECO:0000255"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 130..147
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 922..937
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT VAR_SEQ 1..903
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:10958648"
FT /id="VSP_009517"
FT VAR_SEQ 1..336
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10958648"
FT /id="VSP_009516"
FT VAR_SEQ 525..840
FT /note="EQLKDVAYGTRQLPLCLKPLPAHENEDKVDISPWHQSENLFELHIHQAFLTS
FT AALAQAGDTQPTTFCTYSFYDFETHCTPLVVGPQPLYDFTSQYVVEIDSLFLHYLQGAS
FT AQLDLHQAIASEHHTLAAGWICFDRVLETVERVHGSATLTGTGGEVFGVLEYWMRLRFP
FT IRSSLQAYNKRKKAQAYLAANVLGAWEAQKDEPRSGTWKNQNELRVEIIRCCGLRSRSL
FT GAQPSPYVMYRFFTFSDHDTTIIPASSNPYFRDLARFPVLVTSDLDQYLRREALSVYVF
FT DDEDSEPGSYLGRVQVPLLPLAQNKSIQ -> GILRSHGLPVS (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10958648"
FT /id="VSP_009518"
SQ SEQUENCE 1221 AA; 138434 MW; 8E4CE05E3CACB64A CRC64;
MIPTSKGKNT KTQPPLSRMT RDELEDSLFR LREEHMLVKE LFWKQQDEIK RMRTALLRLT
ASGRGLRAEA AADESSGSPL NGGGTESGGT APSSTSVPRC PGSSCSSSAW APLLPAAPSL
ASTRDTDSST PPGHRAEKPK RESRDRLSYT APPTFKEHVT NEKARGEVAS EPSELGHLMT
SDTMQVEEPP KSPEKMWSKD ENFAQRSSLE STQKATELRA SIKENIQLIR LKKLLHERNT
SLAVTKAQLT EVQAAYETLL HKNQGILGAA HNALLSQVNE LRAELKEESK KAVSLKSQME
DVSILQITLK EFQERVEDLE KERKLLNDNY DKLLESMLDS SNQPQWSHEL GEQLQQKVSQ
LQDQLDVEMK EKREILLQLS QEKAQNKDLE LEVTSLLQKH KQEVEDLQNI STFSQSPDRQ
SAPATHPALF QETIQIQPCE PKNQEEKKLS QMLSELQVSH AETTLELEKT RDMLILQRKI
NVCYQEELEA MMTKADNENK DHEAKLERLN QLLDLKNKRI NQLEEQLKDV AYGTRQLPLC
LKPLPAHENE DKVDISPWHQ SENLFELHIH QAFLTSAALA QAGDTQPTTF CTYSFYDFET
HCTPLVVGPQ PLYDFTSQYV VEIDSLFLHY LQGASAQLDL HQAIASEHHT LAAGWICFDR
VLETVERVHG SATLTGTGGE VFGVLEYWMR LRFPIRSSLQ AYNKRKKAQA YLAANVLGAW
EAQKDEPRSG TWKNQNELRV EIIRCCGLRS RSLGAQPSPY VMYRFFTFSD HDTTIIPASS
NPYFRDLARF PVLVTSDLDQ YLRREALSVY VFDDEDSEPG SYLGRVQVPL LPLAQNKSIQ
GDFNLTDPVG EPNGSVQVHL DWGSCYLPPE NFPKPEAQSE EDTRDGLETS IEEEEASFPP
QDQMVSIDTP TEAGQYQAKR KPPQVGERKE REHQVAGYSR RKHGRKTGLQ GKNRMEYLSH
NLLNGNTLQQ VKYIEWKFSG LKISADHVLK NQQKEEEMTS SYSAQILKET PHPVNDKEFC
EQASEGSEAQ TTDSDEIVTP VSQKCPKADS EKMCIEIVSL AFYPEAEVMC DENVEQVYVE
YRFYDLPLSE TETPVSLRKP RAGEEIYFHF SKVIDLDPVE QKERRQFLFT MLIGEDPEQG
HLKFTVVSDP IEEEKKECQE VGYAYLELWP MLVSGRDILE QDLDIVGPED QATPIGKLKV
SLQAAAALQA IYKEMTEDLC S
