RIM3C_HUMAN
ID RIM3C_HUMAN Reviewed; 1639 AA.
AC A6NJZ7;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-MAR-2012, sequence version 3.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=RIMS-binding protein 3C;
DE Short=RIM-BP3.C;
DE AltName: Full=RIMS-binding protein 3.3;
DE Short=RIM-BP3.3;
GN Name=RIMBP3C;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=10591208; DOI=10.1038/990031;
RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M.,
RA Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C.,
RA Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E.,
RA Bridgeman A.M., Buck D., Burgess J., Burrill W.D., Burton J., Carder C.,
RA Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G.,
RA Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V.,
RA Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M.,
RA Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E.,
RA Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F.,
RA Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M.,
RA Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A.,
RA Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D.,
RA Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y.,
RA Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S.,
RA Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E.,
RA Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A.,
RA Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L.,
RA Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P.,
RA Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P.,
RA Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q.,
RA Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J.,
RA Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J.,
RA Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D.,
RA Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T.,
RA Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P.,
RA Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K.,
RA Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L.,
RA McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J.,
RA Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E.,
RA Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P.,
RA Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y.,
RA Wright H.;
RT "The DNA sequence of human chromosome 22.";
RL Nature 402:489-495(1999).
RN [2]
RP INTERACTION WITH FASLG.
RX PubMed=19807924; DOI=10.1186/1471-2172-10-53;
RA Voss M., Lettau M., Janssen O.;
RT "Identification of SH3 domain interaction partners of human FasL (CD178) by
RT phage display screening.";
RL BMC Immunol. 10:53-53(2009).
CC -!- FUNCTION: Probable component of the manchette, a microtubule-based
CC structure which plays a key role in sperm head morphogenesis during
CC late stages of sperm development. {ECO:0000250|UniProtKB:Q3V0F0}.
CC -!- SUBUNIT: Interacts with LRGUK (via guanylate kinase-like domain).
CC Interacts (via C-terminus) with HOOK1 (via coiled-coil region) (By
CC similarity). May interact with FASLG (PubMed:19807924).
CC {ECO:0000250|UniProtKB:Q3V0F0, ECO:0000269|PubMed:19807924}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC {ECO:0000250|UniProtKB:Q3V0F0}.
CC -!- SIMILARITY: Belongs to the RIMBP family. {ECO:0000305}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-95 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AP000557; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR CCDS; CCDS46669.1; -.
DR RefSeq; NP_001122105.1; NM_001128633.1.
DR AlphaFoldDB; A6NJZ7; -.
DR SMR; A6NJZ7; -.
DR BioGRID; 127271; 16.
DR IntAct; A6NJZ7; 2.
DR STRING; 9606.ENSP00000390630; -.
DR iPTMnet; A6NJZ7; -.
DR PhosphoSitePlus; A6NJZ7; -.
DR BioMuta; RIMBP3C; -.
DR EPD; A6NJZ7; -.
DR jPOST; A6NJZ7; -.
DR MassIVE; A6NJZ7; -.
DR MaxQB; A6NJZ7; -.
DR PaxDb; A6NJZ7; -.
DR PeptideAtlas; A6NJZ7; -.
DR PRIDE; A6NJZ7; -.
DR Antibodypedia; 21503; 1 antibodies from 1 providers.
DR DNASU; 150221; -.
DR Ensembl; ENST00000433039.2; ENSP00000390630.1; ENSG00000183246.8.
DR GeneID; 150221; -.
DR KEGG; hsa:150221; -.
DR MANE-Select; ENST00000433039.2; ENSP00000390630.1; NM_001128633.2; NP_001122105.1.
DR UCSC; uc002zuy.5; human.
DR CTD; 150221; -.
DR GeneCards; RIMBP3C; -.
DR HGNC; HGNC:33892; RIMBP3C.
DR HPA; ENSG00000183246; Tissue enriched (testis).
DR MIM; 612701; gene.
DR neXtProt; NX_A6NJZ7; -.
DR OpenTargets; ENSG00000183246; -.
DR VEuPathDB; HostDB:ENSG00000183246; -.
DR eggNOG; KOG3632; Eukaryota.
DR GeneTree; ENSGT00950000183203; -.
DR HOGENOM; CLU_001979_2_1_1; -.
DR InParanoid; A6NJZ7; -.
DR OMA; FREKENC; -.
DR OrthoDB; 102427at2759; -.
DR PhylomeDB; A6NJZ7; -.
DR TreeFam; TF316230; -.
DR PathwayCommons; A6NJZ7; -.
DR SignaLink; A6NJZ7; -.
DR SIGNOR; A6NJZ7; -.
DR BioGRID-ORCS; 150221; 18 hits in 280 CRISPR screens.
DR ChiTaRS; RIMBP3C; human.
DR GenomeRNAi; 150221; -.
DR Pharos; A6NJZ7; Tdark.
DR PRO; PR:A6NJZ7; -.
DR Proteomes; UP000005640; Chromosome 22.
DR RNAct; A6NJZ7; protein.
DR Bgee; ENSG00000183246; Expressed in right testis and 23 other tissues.
DR Genevisible; A6NJZ7; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0030156; F:benzodiazepine receptor binding; IBA:GO_Central.
DR GO; GO:0009566; P:fertilization; IBA:GO_Central.
DR GO; GO:0007286; P:spermatid development; IBA:GO_Central.
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; 1.
DR Pfam; PF14604; SH3_9; 1.
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; Reference proteome;
KW Repeat; SH3 domain; Spermatogenesis.
FT CHAIN 1..1639
FT /note="RIMS-binding protein 3C"
FT /id="PRO_0000332275"
FT DOMAIN 832..899
FT /note="SH3 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 995..1083
FT /note="Fibronectin type-III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1088..1184
FT /note="Fibronectin type-III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00316"
FT DOMAIN 1452..1520
FT /note="SH3 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 1569..1636
FT /note="SH3 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 215..240
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 295..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 697..811
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1251..1273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1292..1325
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1392..1413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 21..143
FT /evidence="ECO:0000255"
FT COILED 409..442
FT /evidence="ECO:0000255"
FT COILED 480..619
FT /evidence="ECO:0000255"
FT COMPBIAS 322..342
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 737..751
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 759..803
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1255..1273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1392..1406
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1639 AA; 180950 MW; A91AA22674EA0F26 CRC64;
MAKDSPSPLG ASPKKPGCSS PAAAVLENQR RELEKLRAEL EAERAGWRAE RRRFAARERQ
LREEAERERR QLADRLRSKW EAQRSRELRQ LQEEMQRERE AEIRQLLRWK EAEQRQLQQL
LHRERDGVVR QARELQRQLA EELVNRGHCS RPGASEVSAA QCRCRLQEVL AQLRWQTDGE
QAARIRYLQA ALEVERQLFL KYILAHFRGH PALSGSPDPQ AVHSLEEPLP QTSSGSCHAP
KPACQLGSLD SLSAEVGVRS RSLGLVSSAC SSSPDGLLST HASSLDCFAP ACSRSLDSTR
SLPKASKSEE RPSSPDTSTP GSRRLSPPPS PLPPPPPPSA HRKLSNPRGG EGSESQPCEV
LTPSPPGLGH HELIKLNWLL AKALWVLARR CYTLQEENKQ LRRAGCPYQA DEKVKRLKVK
RAELTGLARR LADRARELQE TNLRAVSAPI PGESCAGLEL CQVFARQRAR DLSEQASAPL
AKDKQIEELR QECHLLQARV ASGPCSDLHT GRGGPCTQWL NVRDLDRLQR ESQREVLRLQ
RQLMLQQGNG GAWPEAGGQS ATCEEVRRQM LALERELDQR RRECQELGTQ AAPARRRGEE
AETQLQAALL KNAWLAEENG RLQAKTDWVR KVEAENSEVR GHLGRACQER DASGLIAEQL
LQQAARGQDR QQQLQRDPQK ALCDLHPSWK EIQALQCRPG HPPEQPWETS QMPESQVKGS
RRPKFHARPE DYAVSQPNRD IQEKREASLE ESPVALGESA SVPQVSETVP ASQPLSKKTS
SQSNSSSEGS MWATVPSSPT LDRDTASEVD DLEPDSVSLA LEMGGSAAPA APKLKIFMAQ
YNYNPFEGPN DHPEGELPLT AGDYIYIFGD MDEDGFYEGE LDDGRRGLVP SNFVEQIPDS
YIPGCLPAKS PDLGPSQLPA GQDEALEEDS LLSGKAQGMV DRGLCQMVRV GSKTEVATEI
LDTKTEACQL GLLQSMGKQG LSRPLLGTKG VLRMAPMQLH LQNVTATSAN ITWVYSSHRH
PHVVYLDDRE HALTPAGVSC YTFQGLCPGT HYRVRVEVRL PWDLLQVYWG TMSSTVTFDT
LLAGPPYPPL DVLVERHASP GVLVVSWLPV TIDSAGSSNG VQVTGYAVYA DGLKVCEVAD
ATAGSTVLEF SQLQVPLTWQ KVSVRTMSLC GESLDSVPAQ IPEDFFMCHR WPETPPFSYT
CGDPSTYRVT FPVCPQKLSL APPSAKASPH NPGSCGEPQA KFLEAFFEEP PRRQSPVSNL
GSEGECPSSG AGSQAQELAE AWEGCRKDLL FQKSPQNHRP PSVSDQPGEK ENCYQHMGTS
KSPAPGFIHL RTECGPRKEP CQEKAALERV LRQKQDAQGF TPPQLGASQQ YASDFHNVLK
EEQEALCLDL RGTERREERR EPEPHSRQGQ ALGVKRGCQL HEPSSALCPA PSAKVIKMPR
GGPQQLGTGA NTPARVFVAL SDYNPLVMSA NLKAAEEELV FQKRQLLRVW GSQDTHDFYL
SECNRQVGNI PGRLVAEMEV GTEQTDRRWR SPAQGHLPSV AHLEDFQGLI IPQGSSLVLQ
GNSKRLPLWT PKIMIAALDY DPGDGQMGGQ GKGRLALRAG DVVMVYGPMD DQGFYYGELG
GHRGLVPAHL LDHMSLHGH
