ID A0A8I5N3R1_PAPAN Unreviewed; 1030 AA.
AC A0A8I5N3R1;
DT 25-MAY-2022, integrated into UniProtKB/TrEMBL.
DT 25-MAY-2022, sequence version 1.
DT 28-JAN-2026, entry version 18.
DE RecName: Full=BBSome complex member BBS5 {ECO:0000256|ARBA:ARBA00047191};
DE AltName: Full=Kelch repeat and BTB domain-containing protein 10 {ECO:0000256|ARBA:ARBA00076804};
DE AltName: Full=Kelch-like protein 41 {ECO:0000256|ARBA:ARBA00069965};
GN Name=KLHL41 {ECO:0000313|Ensembl:ENSPANP00000054715.1};
OS Papio anubis (Olive baboon).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini;
OC Cercopithecidae; Cercopithecinae; Papio.
OX NCBI_TaxID=9555 {ECO:0000313|Ensembl:ENSPANP00000054715.1, ECO:0000313|Proteomes:UP000028761};
RN [1] {ECO:0000313|Ensembl:ENSPANP00000054715.1, ECO:0000313|Proteomes:UP000028761}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu Y.L., Abraham K.A., Akbar H.A., Ali S.A., Anosike U.A., Aqrawi P.A.,
RA Arias F.A., Attaway T.A., Awwad R.A., Babu C.B., Bandaranaike D.B.,
RA Battles P.B., Bell A.B., Beltran B.B., Berhane-Mersha D.B., Bess C.B.,
RA Bickham C.B., Bolden T.B., Carter K.C., Chau D.C., Chavez A.C.,
RA Clerc-Blankenburg K.C., Coyle M.C., Dao M.D., Davila M.L.D.,
RA Davy-Carroll L.D., Denson S.D., Dinh H.D., Fernandez S.F., Fernando P.F.,
RA Forbes L.F., Francis C.F., Francisco L.F., Fu Q.F., Garcia-Iii R.G.,
RA Garrett T.G., Gross S.G., Gubbala S.G., Hirani K.H., Hogues M.H.,
RA Hollins B.H., Jackson L.J., Javaid M.J., Jhangiani S.J., Johnson A.J.,
RA Johnson B.J., Jones J.J., Joshi V.J., Kalu J.K., Khan N.K., Korchina V.K.,
RA Kovar C.K., Lago L.L., Lara F.L., Le T.-K.L., Lee S.L., Legall-Iii F.L.,
RA Lemon S.L., Liu J.L., Liu Y.-S.L., Liyanage D.L., Lopez J.L.,
RA Lorensuhewa L.L., Mata R.M., Mathew T.M., Mercado C.M., Mercado I.M.,
RA Morales K.M., Morgan M.M., Munidasa M.M., Ngo D.N., Nguyen L.N.,
RA Nguyen T.N., Nguyen N.N., Obregon M.O., Okwuonu G.O., Ongeri F.O.,
RA Onwere C.O., Osifeso I.O., Parra A.P., Patil S.P., Perez A.P., Perez Y.P.,
RA Pham C.P., Pu L.-L.P., Puazo M.P., Quiroz J.Q., Rouhana J.R., Ruiz M.R.,
RA Ruiz S.-J.R., Saada N.S., Santibanez J.S., Scheel M.S., Schneider B.S.,
RA Simmons D.S., Sisson I.S., Tang L.-Y.T., Thornton R.T., Tisius J.T.,
RA Toledanes G.T., Trejos Z.T., Usmani K.U., Varghese R.V., Vattathil S.V.,
RA Vee V.V., Walker D.W., Weissenberger G.W., White C.W., Williams A.W.,
RA Woodworth J.W., Wright R.W., Zhu Y.Z., Han Y.H., Newsham I.N.,
RA Nazareth L.N., Worley K.W., Muzny D.M., Rogers J.R., Gibbs R.G.;
RT "Whole Genome Assembly of Papio anubis.";
RL Submitted (MAR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Ensembl:ENSPANP00000054715.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (AUG-2025) to UniProtKB.
RN [3] {ECO:0000313|Ensembl:ENSPANP00000054715.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (SEP-2025) to UniProtKB.
CC -!- FUNCTION: Involved in skeletal muscle development and differentiation.
CC Regulates proliferation and differentiation of myoblasts and plays a
CC role in myofibril assembly by promoting lateral fusion of adjacent thin
CC fibrils into mature, wide myofibrils. Required for pseudopod elongation
CC in transformed cells. {ECO:0000256|ARBA:ARBA00053582}.
CC -!- FUNCTION: The BBSome complex is thought to function as a coat complex
CC required for sorting of specific membrane proteins to the primary
CC cilia. The BBSome complex is required for ciliogenesis but is
CC dispensable for centriolar satellite function. This ciliogenic function
CC is mediated in part by the Rab8 GDP/GTP exchange factor, which
CC localizes to the basal body and contacts the BBSome. Rab8(GTP) enters
CC the primary cilium and promotes extension of the ciliary membrane.
CC Firstly the BBSome associates with the ciliary membrane and binds to
CC RAB3IP/Rabin8, the guanosyl exchange factor (GEF) for Rab8 and then the
CC Rab8-GTP localizes to the cilium and promotes docking and fusion of
CC carrier vesicles to the base of the ciliary membrane. The BBSome
CC complex, together with the LTZL1, controls SMO ciliary trafficking and
CC contributes to the sonic hedgehog (SHH) pathway regulation. Required
CC for BBSome complex ciliary localization but not for the proper complex
CC assembly. {ECO:0000256|ARBA:ARBA00054242}.
CC -!- SUBUNIT: Part of BBSome complex, that contains BBS1, BBS2, BBS4, BBS5,
CC BBS7, BBS8/TTC8, BBS9 and BBIP10. Binds to phosphoinositides. Interacts
CC with CCDC28B. Interacts with SMO; the interaction is indicative for the
CC association of SMO with the BBsome complex to facilitate ciliary
CC localization of SMO. Interacts with PKD1. Interacts with DLEC1.
CC {ECO:0000256|ARBA:ARBA00066146}.
CC -!- SUBCELLULAR LOCATION: Cell projection, cilium membrane
CC {ECO:0000256|ARBA:ARBA00004309}. Cell projection, pseudopodium
CC {ECO:0000256|ARBA:ARBA00037818}. Cytoplasm, cytoskeleton, microtubule
CC organizing center, centrosome, centriolar satellite
CC {ECO:0000256|ARBA:ARBA00004607}. Sarcoplasmic reticulum membrane
CC {ECO:0000256|ARBA:ARBA00004449}.
CC -!- SIMILARITY: Belongs to the BBS5 family.
CC {ECO:0000256|ARBA:ARBA00005822}.
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 AlphaFoldDB; A0A8I5N3R1; -.
DR Ensembl; ENSPANT00000071635.1; ENSPANP00000054715.1; ENSPANG00000014471.3.
DR GeneTree; ENSGT00940000158859; -.
DR Proteomes; UP000028761; Chromosome 10.
DR GO; GO:0034464; C:BBSome; IEA:InterPro.
DR GO; GO:0034451; C:centriolar satellite; IEA:UniProtKB-SubCell.
DR GO; GO:0036064; C:ciliary basal body; IEA:TreeGrafter.
DR GO; GO:0060170; C:ciliary membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0031463; C:Cul3-RING ubiquitin ligase complex; IEA:UniProtKB-ARBA.
DR GO; GO:0031143; C:pseudopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0033017; C:sarcoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0032266; F:phosphatidylinositol-3-phosphate binding; IEA:TreeGrafter.
DR GO; GO:0060271; P:cilium assembly; IEA:TreeGrafter.
DR CDD; cd18517; BACK_KLHL41_KBTBD10; 1.
DR CDD; cd18341; BTB_POZ_KLHL41_KBTBD10; 1.
DR CDD; cd00900; PH-like; 1.
DR FunFam; 2.30.29.30:FF:000232; Bardet-Biedl syndrome 5 isoform 1; 1.
DR FunFam; 3.30.710.10:FF:000006; Kelch repeat and BTB domain-containing 6; 1.
DR FunFam; 1.25.40.420:FF:000001; Kelch-like family member 12; 1.
DR FunFam; 2.120.10.80:FF:000025; Kelch-like family member 41; 1.
DR Gene3D; 1.25.40.420; -; 1.
DR Gene3D; 2.120.10.80; Kelch-type beta propeller; 1.
DR Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR Gene3D; 3.30.710.10; Potassium Channel Kv1.1, Chain A; 1.
DR InterPro; IPR011705; BACK.
DR InterPro; IPR006606; BBL5.
DR InterPro; IPR014003; BBS5_PH.
DR InterPro; IPR000210; BTB/POZ_dom.
DR InterPro; IPR015915; Kelch-typ_b-propeller.
DR InterPro; IPR006652; Kelch_1.
DR InterPro; IPR030571; KLHL41_KL41B_BTB_POZ_dom.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR011333; SKP1/BTB/POZ_sf.
DR PANTHER; PTHR21351:SF0; BARDET-BIEDL SYNDROME 5 PROTEIN; 1.
DR PANTHER; PTHR21351; BARDET-BIEDL SYNDROME PROTEIN 5; 1.
DR Pfam; PF07707; BACK; 1.
DR Pfam; PF07289; BBL5; 1.
DR Pfam; PF00651; BTB; 1.
DR Pfam; PF24681; Kelch_KLHDC2_KLHL20_DRC7; 1.
DR SMART; SM00875; BACK; 1.
DR SMART; SM00225; BTB; 1.
DR SMART; SM00683; DM16; 2.
DR SMART; SM00612; Kelch; 4.
DR SUPFAM; SSF117281; Kelch motif; 1.
DR SUPFAM; SSF54695; POZ domain; 1.
DR PROSITE; PS50097; BTB; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW Cilium {ECO:0000256|ARBA:ARBA00023069};
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Cytoskeleton {ECO:0000256|ARBA:ARBA00023212};
KW Kelch repeat {ECO:0000256|ARBA:ARBA00022441};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Reference proteome {ECO:0000313|Proteomes:UP000028761};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 506..573
FT /note="BTB"
FT /evidence="ECO:0000259|PROSITE:PS50097"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1030 AA; 115862 MW; 63B3D706CEB420B8 CRC64;
MSVWRQGRSP RGQARAPRRT QLGFSETPKP CLVSQIGLSM RKSWATRAHS RGSLSLGARR
RRRDRGGPLP WSQRDAAGRP RLWRLPAAGL VHHVGAGCAL GGPGCPLRPV LAMALITPGP
TDLQVLEVLE DLISKYVNIW HSIIYAVSCF RQMKTRPGEV LIDCLDSIED TKGNNGDRGR
LLVTNLRILW HSLALSRVNV SVGYNCILNI TTRTANSKLR GQTEALYILT KCNSTRFEFI
FTNLVPGSPR LFTSVMAVHR AYETSKMYRD FKLRSALIQN KQLRLLPQEH VYDKINGVWN
LSSDQGNLGT FFITNVRIVW HANMNDSFNV SIPYLQIRSI KIRDSKFGLA LVIESSQQSG
GYVLGFKIDP VEKLQESVKE INSLHKVYSA SPIFGVDYEM EEKPQPLEAL TVEQIQDDVE
IDSDDHTDAF VAYFADGNKQ QDREPVFSEE LGLAIEKLKD GFTLQGLWEV THRMDSQREL
AEELRLYQST LLQDGLKDLL DEKKFIDCTL KAGDKSLPCH RLILSACSPY FREYFLSEID
EAKKKEVVLD NVDPAILDLI IKYLYSASID LNDGNVQDIF ALASRFQIPS VFTVCVSYLQ
KRLAPGNCLA ILRLGLLLDC PRLAISAREF VSDRFVQICK EEDFMQLSPQ ELISVISNDS
LNVEKEEAVF EAVMKWVRTD KENRVKNLSE VFDCIRFRLM TEKYFKDHVE KDDIIKSNPD
LQKKIKVLKD AFAGKLPEPS KNVQKTGAGE VNGDVGDEDL LPGYLNDIPR HGMFVKDLIL
LVNDTAAVAY DPTENECYLT ALAEQIPRNH SSIVTQQNQI YVVGGLYVDE ENKDQPLQSY
FFQLDSIASE WVGLPPLPSA RCLFGLGEVD DKIYVVAGKD LQTEASLDSV LCYDPVAAKW
NEVKKLPIKV YGHNVISHKG MIYCLGGKTD DKKCTNRVFI FNPKKGDWKD LAPMKTPRSM
FGVAVHKGKI VIAGGVTEDG LSASVEAFDL TTNKYEDDKK EWAGMLKEIR YASGASCLAT
RLNLFKLSKL
//
