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Database: UniProt
Entry: A0A0A0K1I7_CUCSA
LinkDB: A0A0A0K1I7_CUCSA
Original site: A0A0A0K1I7_CUCSA 
ID   A0A0A0K1I7_CUCSA        Unreviewed;       907 AA.
AC   A0A0A0K1I7;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Beta-adaptin-like protein {ECO:0000256|PIRNR:PIRNR002291};
GN   ORFNames=Csa_7G041890 {ECO:0000313|EMBL:KGN43495.1};
OS   Cucumis sativus (Cucumber).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Benincaseae; Cucumis.
OX   NCBI_TaxID=3659 {ECO:0000313|EMBL:KGN43495.1, ECO:0000313|Proteomes:UP000029981};
RN   [1] {ECO:0000313|EMBL:KGN43495.1, ECO:0000313|Proteomes:UP000029981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 9930 {ECO:0000313|Proteomes:UP000029981};
RX   PubMed=19881527; DOI=10.1038/ng.475;
RA   Huang S., Li R., Zhang Z., Li L., Gu X., Fan W., Lucas W.J., Wang X.,
RA   Xie B., Ni P., Ren Y., Zhu H., Li J., Lin K., Jin W., Fei Z., Li G.,
RA   Staub J., Kilian A., van der Vossen E.A., Wu Y., Guo J., He J., Jia Z.,
RA   Ren Y., Tian G., Lu Y., Ruan J., Qian W., Wang M., Huang Q., Li B.,
RA   Xuan Z., Cao J., Asan null, Wu Z., Zhang J., Cai Q., Bai Y., Zhao B.,
RA   Han Y., Li Y., Li X., Wang S., Shi Q., Liu S., Cho W.K., Kim J.Y., Xu Y.,
RA   Heller-Uszynska K., Miao H., Cheng Z., Zhang S., Wu J., Yang Y., Kang H.,
RA   Li M., Liang H., Ren X., Shi Z., Wen M., Jian M., Yang H., Zhang G.,
RA   Yang Z., Chen R., Liu S., Li J., Ma L., Liu H., Zhou Y., Zhao J., Fang X.,
RA   Li G., Fang L., Li Y., Liu D., Zheng H., Zhang Y., Qin N., Li Z., Yang G.,
RA   Yang S., Bolund L., Kristiansen K., Zheng H., Li S., Zhang X., Yang H.,
RA   Wang J., Sun R., Zhang B., Jiang S., Wang J., Du Y., Li S.;
RT   "The genome of the cucumber, Cucumis sativus L.";
RL   Nat. Genet. 41:1275-1281(2009).
CC   -!- FUNCTION: Subunit of clathrin-associated adaptor protein complex that
CC       plays a role in protein sorting in the late-Golgi/trans-Golgi network
CC       (TGN) and/or endosomes. The AP complexes mediate both the recruitment
CC       of clathrin to membranes and the recognition of sorting signals within
CC       the cytosolic tails of transmembrane cargo molecules.
CC       {ECO:0000256|PIRNR:PIRNR002291}.
CC   -!- SUBUNIT: Adaptor protein complexes are heterotetramers composed of two
CC       large adaptins (beta-type subunit and alpha-type or delta-type or
CC       epsilon-type or gamma-type subunit), a medium adaptin (mu-type subunit)
CC       and a small adaptin (sigma-type subunit).
CC       {ECO:0000256|PIRNR:PIRNR002291}.
CC   -!- SIMILARITY: Belongs to the adaptor complexes large subunit family.
CC       {ECO:0000256|ARBA:ARBA00006613, ECO:0000256|PIRNR:PIRNR002291}.
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DR   EMBL; CM002928; KGN43495.1; -; Genomic_DNA.
DR   RefSeq; XP_004144506.1; XM_004144458.2.
DR   AlphaFoldDB; A0A0A0K1I7; -.
DR   STRING; 3659.A0A0A0K1I7; -.
DR   EnsemblPlants; KGN43495; KGN43495; Csa_7G041890.
DR   GeneID; 101203329; -.
DR   Gramene; KGN43495; KGN43495; Csa_7G041890.
DR   KEGG; csv:101203329; -.
DR   eggNOG; KOG1061; Eukaryota.
DR   OMA; NPPEVQW; -.
DR   OrthoDB; 648032at2759; -.
DR   Proteomes; UP000029981; Chromosome 7.
DR   GO; GO:0030131; C:clathrin adaptor complex; IEA:InterPro.
DR   GO; GO:0030276; F:clathrin binding; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   GO; GO:0016192; P:vesicle-mediated transport; IBA:GO_Central.
DR   Gene3D; 2.60.40.1150; -; 1.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   Gene3D; 3.30.310.10; TATA-Binding Protein; 1.
DR   InterPro; IPR026739; AP_beta.
DR   InterPro; IPR016342; AP_complex_bsu_1_2_4.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR015151; B-adaptin_app_sub_C.
DR   InterPro; IPR002553; Clathrin/coatomer_adapt-like_N.
DR   InterPro; IPR008152; Clathrin_a/b/g-adaptin_app_Ig.
DR   InterPro; IPR013041; Clathrin_app_Ig-like_sf.
DR   InterPro; IPR013037; Clathrin_b-adaptin_app_Ig-like.
DR   InterPro; IPR009028; Coatomer/calthrin_app_sub_C.
DR   InterPro; IPR012295; TBP_dom_sf.
DR   PANTHER; PTHR11134; ADAPTOR COMPLEX SUBUNIT BETA FAMILY MEMBER; 1.
DR   PANTHER; PTHR11134:SF3; AP COMPLEX SUBUNIT BETA; 1.
DR   Pfam; PF01602; Adaptin_N; 1.
DR   Pfam; PF02883; Alpha_adaptinC2; 1.
DR   Pfam; PF09066; B2-adapt-app_C; 1.
DR   PIRSF; PIRSF002291; AP_complex_beta; 1.
DR   SMART; SM00809; Alpha_adaptinC2; 1.
DR   SMART; SM01020; B2-adapt-app_C; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   SUPFAM; SSF49348; Clathrin adaptor appendage domain; 1.
DR   SUPFAM; SSF55711; Subdomain of clathrin and coatomer appendage domain; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PIRNR:PIRNR002291};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927,
KW   ECO:0000256|PIRNR:PIRNR002291};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029981};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|PIRNR:PIRNR002291}.
FT   DOMAIN          672..786
FT                   /note="Clathrin adaptor alpha/beta/gamma-adaptin appendage
FT                   Ig-like subdomain"
FT                   /evidence="ECO:0000259|SMART:SM00809"
FT   DOMAIN          795..906
FT                   /note="Beta-adaptin appendage C-terminal subdomain"
FT                   /evidence="ECO:0000259|SMART:SM01020"
FT   REGION          593..654
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        605..630
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   907 AA;  100652 MW;  6D58EFF06F089B85 CRC64;
     MSGHDSKYFS TTKKGEIPEL KEELNSQYKD KRKDAVKKVI AAMTVGKDVS SLFTDVVNCM
     QTENLELKKL VYLYLINYAK SQPDLAILAV NTFVKDSQDP NPLIRALAVR TMGCIRVDKI
     TEYLCDPLQR CLKDDDPYVR KTAAICVAKL FDINAELVED RGFLDSLKDL ISDNNPMVVA
     NAVAALAEIQ EDSSKPIFEI TSHTLSKLLT ALNECTEWGQ VFILDALSRY KTEDAREAEN
     IVERVTPRLQ HANCAVVLSA VKMILLQMEL ITSTDIVRNL CKKMAPPLVT LLSSEPEIQY
     VALRNINLIV LKRPTILAHE IKVFFCKYND PIYVKVEKLE IMIKLASDRN IDQVLLEFKE
     YATEVDVDFV RKAVRAIGRC AIKLERAAER CISVLLELIK IKVNYVVQEA IIVIKDIFRR
     YPNTYESIIA TLCESLDTLD EPEAKASMIW IIGEYAERID NADELLESFL ESFPEEPAQV
     QLQLLTATVK LFLKKPTEGP QQMIQAVLNN ATVETDNPDL RDRAYIYWRL LSTDPEAAKD
     VVLAEKPVIG DDSNLLDSTL LDELLANIAT LSSVYHKPPE AFVTRVKTVS QRIDDDDYPE
     GSNSGHSEPP ANAASGGGAS PTTSDAPYSV TKRPVPTLAP APSSSPPPAS IPDLLGDLIG
     LDNSAIAPVD QSAAPAGSPL PILLTASAGQ GLQISAQLIR HDGQIFYSLT FDNSSQMILD
     GFMIQFNKNT FGLAAAGPLQ VPQLQPGSIA NTLLPMVVFQ NMSQGPPSSL LQVAVKNNQQ
     PVLYFSDKIL MHIFFTEDGR MERASFLETW RSLPDSNEVI RDLPTILINN VEAIVERLAA
     TNMFFIAKRK HANQDVFYFS TKIPRGIPFL IELTTVIGSP GLKCAVKTPN IDMAPLFFEA
     LEILLKE
//
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