ID G1LNV5_AILME Unreviewed; 854 AA.
AC G1LNV5;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=Vacuolar protein sorting-associated protein 41 homolog {ECO:0000256|ARBA:ARBA00029538, ECO:0000256|PIRNR:PIRNR028921};
GN Name=VPS41 {ECO:0000313|Ensembl:ENSAMEP00000008735.2};
OS Ailuropoda melanoleuca (Giant panda).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Carnivora; Caniformia; Ursidae; Ailuropoda.
OX NCBI_TaxID=9646 {ECO:0000313|Ensembl:ENSAMEP00000008735.2, ECO:0000313|Proteomes:UP000008912};
RN [1] {ECO:0000313|Ensembl:ENSAMEP00000008735.2, ECO:0000313|Proteomes:UP000008912}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=20010809; DOI=10.1038/nature08696;
RA Li R., Fan W., Tian G., Zhu H., He L., Cai J., Huang Q., Cai Q., Li B.,
RA Bai Y., Zhang Z., Zhang Y., Wang W., Li J., Wei F., Li H., Jian M., Li J.,
RA Zhang Z., Nielsen R., Li D., Gu W., Yang Z., Xuan Z., Ryder O.A.,
RA Leung F.C., Zhou Y., Cao J., Sun X., Fu Y., Fang X., Guo X., Wang B.,
RA Hou R., Shen F., Mu B., Ni P., Lin R., Qian W., Wang G., Yu C., Nie W.,
RA Wang J., Wu Z., Liang H., Min J., Wu Q., Cheng S., Ruan J., Wang M.,
RA Shi Z., Wen M., Liu B., Ren X., Zheng H., Dong D., Cook K., Shan G.,
RA Zhang H., Kosiol C., Xie X., Lu Z., Zheng H., Li Y., Steiner C.C.,
RA Lam T.T., Lin S., Zhang Q., Li G., Tian J., Gong T., Liu H., Zhang D.,
RA Fang L., Ye C., Zhang J., Hu W., Xu A., Ren Y., Zhang G., Bruford M.W.,
RA Li Q., Ma L., Guo Y., An N., Hu Y., Zheng Y., Shi Y., Li Z., Liu Q.,
RA Chen Y., Zhao J., Qu N., Zhao S., Tian F., Wang X., Wang H., Xu L., Liu X.,
RA Vinar T., Wang Y., Lam T.W., Yiu S.M., Liu S., Zhang H., Li D., Huang Y.,
RA Wang X., Yang G., Jiang Z., Wang J., Qin N., Li L., Li J., Bolund L.,
RA Kristiansen K., Wong G.K., Olson M., Zhang X., Li S., Yang H., Wang J.,
RA Wang J.;
RT "The sequence and de novo assembly of the giant panda genome.";
RL Nature 463:311-317(2010).
RN [2] {ECO:0000313|Ensembl:ENSAMEP00000008735.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
CC -!- FUNCTION: Plays a role in vesicle-mediated protein trafficking to
CC lysosomal compartments including the endocytic membrane transport
CC pathways. {ECO:0000256|PIRNR:PIRNR028921}.
CC -!- SUBCELLULAR LOCATION: Endosome membrane
CC {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR028921}. Late endosome membrane
CC {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR028921}. Early endosome membrane
CC {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR028921}. Lysosome membrane
CC {ECO:0000256|PIRNR:PIRNR028921}; Peripheral membrane protein
CC {ECO:0000256|PIRNR:PIRNR028921}. Golgi apparatus, trans-Golgi network
CC {ECO:0000256|PIRNR:PIRNR028921}. Cytoplasmic vesicle, clathrin-coated
CC vesicle {ECO:0000256|PIRNR:PIRNR028921}. Vesicle
CC {ECO:0000256|ARBA:ARBA00004373}.
CC -!- SIMILARITY: Belongs to the VPS41 family.
CC {ECO:0000256|ARBA:ARBA00009582, ECO:0000256|PIRNR:PIRNR028921}.
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DR AlphaFoldDB; G1LNV5; -.
DR STRING; 9646.ENSAMEP00000008735; -.
DR Ensembl; ENSAMET00000009108.2; ENSAMEP00000008735.2; ENSAMEG00000008248.2.
DR eggNOG; KOG2066; Eukaryota.
DR GeneTree; ENSGT00390000000481; -.
DR HOGENOM; CLU_001285_2_2_1; -.
DR OrthoDB; 8838at2759; -.
DR TreeFam; TF300451; -.
DR Proteomes; UP000008912; Unassembled WGS sequence.
DR GO; GO:0030136; C:clathrin-coated vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0031901; C:early endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005794; C:Golgi apparatus; IEA:UniProtKB-SubCell.
DR GO; GO:0030897; C:HOPS complex; IEA:UniProtKB-UniRule.
DR GO; GO:0031902; C:late endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005765; C:lysosomal membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0034058; P:endosomal vesicle fusion; IEA:UniProtKB-UniRule.
DR GO; GO:0006886; P:intracellular protein transport; IEA:UniProtKB-UniRule.
DR GO; GO:0006623; P:protein targeting to vacuole; IEA:InterPro.
DR GO; GO:0007034; P:vacuolar transport; IEA:UniProtKB-UniRule.
DR CDD; cd16690; RING-H2_Vps41; 1.
DR Gene3D; 1.25.40.10; Tetratricopeptide repeat domain; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 1.
DR InterPro; IPR000547; Clathrin_H-chain/VPS_repeat.
DR InterPro; IPR011990; TPR-like_helical_dom_sf.
DR InterPro; IPR016902; VPS41.
DR InterPro; IPR045111; Vps41/Vps8.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR InterPro; IPR001841; Znf_RING.
DR PANTHER; PTHR12616; VACUOLAR PROTEIN SORTING VPS41; 1.
DR PANTHER; PTHR12616:SF1; VACUOLAR PROTEIN SORTING-ASSOCIATED PROTEIN 41 HOMOLOG; 1.
DR Pfam; PF00637; Clathrin; 1.
DR PIRSF; PIRSF028921; VPS41; 1.
DR SMART; SM00299; CLH; 1.
DR SUPFAM; SSF57850; RING/U-box; 1.
DR SUPFAM; SSF50978; WD40 repeat-like; 1.
DR PROSITE; PS50236; CHCR; 1.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 3: Inferred from homology;
KW Cytoplasmic vesicle {ECO:0000256|PIRNR:PIRNR028921};
KW Endosome {ECO:0000256|PIRNR:PIRNR028921};
KW Golgi apparatus {ECO:0000256|ARBA:ARBA00023034,
KW ECO:0000256|PIRNR:PIRNR028921}; Lysosome {ECO:0000256|PIRNR:PIRNR028921};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Protein transport {ECO:0000256|PIRNR:PIRNR028921};
KW Reference proteome {ECO:0000313|Proteomes:UP000008912};
KW Transport {ECO:0000256|PIRNR:PIRNR028921};
KW Zinc {ECO:0000256|ARBA:ARBA00022833};
KW Zinc-finger {ECO:0000256|ARBA:ARBA00022771, ECO:0000256|PROSITE-
KW ProRule:PRU00175}.
FT DOMAIN 791..839
FT /note="RING-type"
FT /evidence="ECO:0000259|PROSITE:PS50089"
FT REGION 1..33
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..26
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 854 AA; 98560 MW; 9A29AFC808798948 CRC64;
MAEAEEQETE SLEESTDESE EEESEEEPKL KYERLSNGVT EILQKDAASC MTVHDKFLAL
GTHYGKVYLL DVQGNITQKF DVSPVKINQI SLDESGEHMG MCSEDGKVQV FGLYSGEEFH
ETFDCPIKII AVHPHFVRSS CKQFVTGGKK LLLFERSWMS RWKSSVLHEG EGNIRSVKWK
GHLIAWANNM GVKIFDITSK QRITNVPRDD ISLRPDMYPC SLCWKDNVTL IIGWGTSVKI
CSVKERHASE MRDLPSRYVE IVSQFETEFY ISGLAPLCDQ LVVLSYVKEV SEKTEREYCA
RPRLDIIQPL SETCEEISSD ALTVRGFQEN ECRDYHLEYS EGEPLFYIVS PRDVVVAKER
DQDDHIDWLL EKKKYEEALM AAEISQKNIK RHKILDIGLA YINHLVEKGE YDIAARKCQK
ILGKNAALWE YEVYKFKEIG QLKAISPYLP RGDPVLKPLI YEMILHEFLE SDYEGFATLI
REWPGDLYNN SVIVQAVRDH LKKDSQNRTL LKTLADLYTY DKNYGNALEI YLTLRHKDVF
QLIHKHNLFS SIKDKIVLLM DFDSEKAVDM LLDNEDKISI KKVVEELEDR PELQHVYLHK
LFKRDHHKGQ RYHEKQISLY AEYDRPNLLP FLRDSTHCPL EKALEICQQR NFVEETVYLL
SRMGNSRSAL KMIMEELHDV DKAIEFAKEQ DDGELWEDLI LYSIDKPPFI TGLLNNIGTH
VDPILLIHRI KEGMEIPNLR DSLVKILQDY NLQILLREGC KKILVADSLS LLKRMHRTQM
KGVLVDEENI CESCLSPVLP ADAAKPFSVV VFHCRHMFHK ECLPVPSMSS PAQFCGICSA
KHRGPGSAIL EMKK
//