RIMB3_MOUSE
ID RIMB3_MOUSE Reviewed; 1606 AA.
AC Q3V0F0; B9EJ89; E9PZY2; Q5DTW0;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2017, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=RIMS-binding protein 3;
DE Short=RIM-BP3;
GN Name=Rimbp3; Synonyms=Gm603, Kiaa1666;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 91-1606.
RC STRAIN=C57BL/6J; TISSUE=Testis;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 94-1606.
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 468-1606.
RC TISSUE=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP FUNCTION, INTERACTION WITH HOOK1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY,
RP DEVELOPMENTAL STAGE, AND DISRUPTION PHENOTYPE.
RX PubMed=19091768; DOI=10.1242/dev.030858;
RA Zhou J., Du Y.R., Qin W.H., Hu Y.G., Huang Y.N., Bao L., Han D.,
RA Mansouri A., Xu G.L.;
RT "RIM-BP3 is a manchette-associated protein essential for spermiogenesis.";
RL Development 136:373-382(2009).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-263 AND SER-274, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [7]
RP FUNCTION, INTERACTION WITH LRGUK, AND SUBCELLULAR LOCATION.
RX PubMed=28003339; DOI=10.1096/fj.201600909r;
RA Okuda H., DeBoer K., O'Connor A.E., Merriner D.J., Jamsai D., O'Bryan M.K.;
RT "LRGUK1 is part of a multiprotein complex required for manchette function
RT and male fertility.";
RL FASEB J. 31:1141-1152(2017).
CC -!- FUNCTION: Component of the manchette, a microtubule-based structure
CC which plays a key role in sperm head morphogenesis during late stages
CC of sperm development (PubMed:19091768, PubMed:28003339). Important for
CC male fertility (PubMed:19091768). {ECO:0000269|PubMed:19091768,
CC ECO:0000269|PubMed:28003339}.
CC -!- SUBUNIT: Interacts with FASLG (By similarity). Interacts with LRGUK
CC (via guanylate kinase-like domain) (PubMed:28003339). Interacts (via C-
CC terminus) with HOOK1 (via coiled-coil region) (PubMed:19091768).
CC {ECO:0000250|UniProtKB:A6NJZ7, ECO:0000269|PubMed:19091768,
CC ECO:0000269|PubMed:28003339}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:19091768, ECO:0000269|PubMed:28003339}. Note=In
CC elongating spermatids, localizes to the manchette.
CC {ECO:0000269|PubMed:19091768, ECO:0000269|PubMed:28003339}.
CC -!- TISSUE SPECIFICITY: Specifically expressed in testis, where it
CC localizes to postmeiotic germ cells (at protein level).
CC {ECO:0000269|PubMed:19091768}.
CC -!- DEVELOPMENTAL STAGE: Detected in testis from postnatal day 20 onwards
CC (at protein level). In developing spermatozoa, weakly expressed in
CC pachytene spermatocytes and round spermatids, and highly expressed in
CC elongating spermatids (at protein level). Detected in residual bodies
CC but not mature sperm (at protein level). {ECO:0000269|PubMed:19091768}.
CC -!- DISRUPTION PHENOTYPE: Males are almost completely infertile, but
CC otherwise have no visible phenotype. Sperm morphology is highly
CC abnormal with deformed nuclei, detached acrosomes and an expanded
CC perinuclear space. Defects are first apparent from the round spermatid
CC stage and are associated with abnormal development of the manchette.
CC {ECO:0000269|PubMed:19091768}.
CC -!- SIMILARITY: Belongs to the RIMBP family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI41387.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE21554.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC154667; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK133200; BAE21554.1; ALT_INIT; mRNA.
DR EMBL; BC141386; AAI41387.1; ALT_INIT; mRNA.
DR EMBL; AK220410; BAD90457.1; -; mRNA.
DR CCDS; CCDS27998.2; -.
DR RefSeq; NP_001028510.2; NM_001033338.3.
DR AlphaFoldDB; Q3V0F0; -.
DR SMR; Q3V0F0; -.
DR STRING; 10090.ENSMUSP00000127909; -.
DR iPTMnet; Q3V0F0; -.
DR PhosphoSitePlus; Q3V0F0; -.
DR PaxDb; Q3V0F0; -.
DR PRIDE; Q3V0F0; -.
DR ProteomicsDB; 253287; -.
DR Ensembl; ENSMUST00000169803; ENSMUSP00000127909; ENSMUSG00000071636.
DR GeneID; 239731; -.
DR KEGG; mmu:239731; -.
DR CTD; 85376; -.
DR MGI; MGI:2685449; Rimbp3.
DR VEuPathDB; HostDB:ENSMUSG00000071636; -.
DR eggNOG; KOG3632; Eukaryota.
DR GeneTree; ENSGT00950000183203; -.
DR InParanoid; Q3V0F0; -.
DR OMA; AQIPEDC; -.
DR OrthoDB; 102427at2759; -.
DR PhylomeDB; Q3V0F0; -.
DR TreeFam; TF316230; -.
DR BioGRID-ORCS; 239731; 0 hits in 74 CRISPR screens.
DR ChiTaRS; Rimbp3; mouse.
DR PRO; PR:Q3V0F0; -.
DR Proteomes; UP000000589; Chromosome 16.
DR RNAct; Q3V0F0; protein.
DR Bgee; ENSMUSG00000071636; Expressed in seminiferous tubule of testis and 39 other tissues.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0030156; F:benzodiazepine receptor binding; IBA:GO_Central.
DR GO; GO:0009566; P:fertilization; IMP:ParkinsonsUK-UCL.
DR GO; GO:0007286; P:spermatid development; IMP:ParkinsonsUK-UCL.
DR CDD; cd00063; FN3; 1.
DR Gene3D; 2.60.40.10; -; 2.
DR InterPro; IPR003961; FN3_dom.
DR InterPro; IPR036116; FN3_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR040325; RIMBP1/2/3.
DR InterPro; IPR035515; Rimbp3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR14234; PTHR14234; 1.
DR PANTHER; PTHR14234:SF21; PTHR14234:SF21; 1.
DR Pfam; PF07653; SH3_2; 3.
DR SMART; SM00060; FN3; 2.
DR SMART; SM00326; SH3; 3.
DR SUPFAM; SSF49265; SSF49265; 1.
DR SUPFAM; SSF50044; SSF50044; 3.
DR PROSITE; PS50853; FN3; 2.
DR PROSITE; PS50002; SH3; 3.
PE 1: Evidence at protein level;
KW Coiled coil; Cytoplasm; Cytoskeleton; Differentiation; Phosphoprotein;
KW Reference proteome; Repeat; SH3 domain; Spermatogenesis.
FT CHAIN 1..1606
FT /note="RIMS-binding protein 3"
FT /id="PRO_0000259598"
FT DOMAIN 822..889
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 982..1070
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1075..1171
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1420..1488
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1536..1603
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 41..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..352
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 677..731
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 744..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1234..1255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1364..1392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 24..146
FT /evidence="ECO:0000255"
FT COILED 352..431
FT /evidence="ECO:0000255"
FT COILED 461..649
FT /evidence="ECO:0000255"
FT COMPBIAS 230..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 295..311
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 677..704
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 705..719
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 748..781
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1238..1254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 263
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 274
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1606 AA; 177278 MW; DE272DBA3740F604 CRC64;
MTKDSPTPLG GGRASPKKPS SPGPAAAVLE EQRRELEKLR AELEGERARG RSERRRFATQ
TRQLRESAEQ ERQQLADHLR SKWEARRLRE LRQLQEEVQR EREAEIRQLL RWKEAEMRQL
QQLLHQERDV VLRQARELQR QLAQELVNRG YCSRSGASEA SAAQCRCRLQ EVLALLRWET
DGEQAARIRH LQAALDVERQ LFLKYILEHF RWQPALPGPA DPQATHSLEE PPLEAQSNTG
GTPKPARRLG SLESLNTGVR VHSPNDLLPT RAGSLESLAT AHSCSLDNTL NCSQASESEV
RAPATSASIP DTSSPQPPPQ LPSIHRKPND LQKESSENKP CEASTSSPPG LDYQELVRQN
SELAEALQVL VRRCCDLREE NLHLRRKGFS EEAGEKVKWL KVKHAELTDL AQRLEDRARK
LQETNLRAMS APVPGESLEG LDLSQVFTCQ RAQDLSEQAG ALQAKDLQIE ALRRECHLLQ
ARIAADLGSS SHPEEGATCA QWCNISDLDR LQRESQREVL RLQRQLTLHQ SKAGAWADAG
RPSTPSEITR HQVQALEREL GLQRRECEEL SVQAAAAERR YEETEAQLQA ALHKGARLSE
ENARLQALAN WMKKMADENS NVSRQQSHTR QRQELEATSL LAEQLLQQEG YAQDRRQQLQ
HYKNKALSDL RTSGKEMQGL QFQPGHPSET SETTQASESQ ARDSGRPTFK TKSEERVLPL
PTRDIQPPAC LSQQENPVIV EEPAAGPQVS DRNSTSQSLD SKPQAKKTSS QSNSSSEVES
MWATVPSCLS LDMDTASEVD DLEPDSMSTP LEMRSLEAPI IPKLKLFLAR SSYNPFEGPS
EHCQGKLPLT AGDYVYVFGD MDEDGFYEGE LVNGQRGLVP SNLVEPISGS PILNHLFLKS
PDIGPTALPA GHSKVLKKGS LLLGEVQERG LCQVGRVDSK TDMAAESLKT KTEACWLGLK
SSLEEQSFSR PLLEAKGAFC LAPMELQLQN VTATSATITW ASGSNRYPHV VYLDDEEHIL
TPSGVNHYTF QGLHPGTCYR VRVGVQLPRD LLQVLWETTS STLTFDTPLA GPPDPPLDVL
VEHHASPGVL VVSWLPVTID SAGSSNGVQV TGYAVYVDGF KVTEVADATA GNTLLEFSQL
QVPLSCQKVS VRTMSLYGES LDSVPAQIPE DFFSCCPFLG APPFNYTDGN PFPVCHQKLV
QASLGAKSSP RGPGNCGEPQ AKFLEAFPEE HPRKHLSLSS LSSDGTNSQA QGPTEAWKGY
EKDLSFQKSP QNHKPPLLFG QSGVEEGHAP HICISGSPAP GFVHLSSEIG HGKIRCWEKP
GLEKALLQNQ YAPMVPPHQQ GSSQCQPADF HHVFEEKEAL CLDSQGTEKP EQRKNKSQNG
QRQGTPGSKR ECSVLCPAPT NKVIKMTSGS PDQLETDANN PVRVFLALFD HSPLVISVNS
EAAEEELAFQ KGQLLRVWGS LDLHGFYHGE CNGHLGKIPG HLVVEVEVGT QQTDGRWHLP
AQGHLLSETQ REDLEGLTNS QGSYMPQGNS RTPTLWTPKT MVAALDYDPR DGRAGVQAKG
KLVLRAGDVV TVYGPVDDKG FYYGEYGGHR GLVPAHLLDD LPVHGE
