ID   BICL1_HUMAN             Reviewed;         573 AA.
AC   Q6ZP65; A8MUC8; B4DWL0; B5MDJ0; O95000;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   30-NOV-2010, sequence version 2.
DT   02-SEP-2026, entry version 140.
DE   RecName: Full=BICD family-like cargo adapter 1;
DE   AltName: Full=Bicaudal D-related protein 1;
DE            Short=BICD-related protein 1;
DE            Short=BICDR-1;
DE   AltName: Full=Coiled-coil domain-containing protein 64A;
DE            Short=CCDC64A;
GN   Name=BICDL1; Synonyms=BICDR1, CCDC64;
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 MRNA] (ISOFORMS 1 AND 2).
RC   TISSUE=Kidney, and Mammary gland;
RX   PubMed=14702039; DOI=10.1038/ng1285;
RA   Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA   Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA   Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA   Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA   Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA   Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA   Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA   Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA   Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA   Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA   Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA   Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA   Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA   Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA   Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA   Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA   Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA   Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA   Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA   Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA   Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA   Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA   Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA   Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA   Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA   Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA   Isogai T., Sugano S.;
RT   "Complete sequencing and characterization of 21,243 full-length human
RT   cDNAs.";
RL   Nat. Genet. 36:40-45(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16541075; DOI=10.1038/nature04569;
RA   Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA   Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA   Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA   Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA   Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA   Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA   Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA   Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA   Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA   Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA   Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA   Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA   Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA   Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA   Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA   Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA   Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA   David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA   D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA   Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA   Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA   Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA   LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA   Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA   Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA   Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA   Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA   Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA   Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA   Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA   Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA   Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA   Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA   Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA   Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA   Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA   Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA   Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA   Gibbs R.A.;
RT   "The finished DNA sequence of human chromosome 12.";
RL   Nature 440:346-351(2006).
CC   -!- FUNCTION: Acts as an adapter protein linking the dynein motor complex
CC       to various cargos and converts dynein from a non-processive to a highly
CC       processive motor in the presence of dynactin. Facilitates the
CC       interaction between dynein and dynactin and activates dynein
CC       processivity (the ability to move along a microtubule for a long
CC       distance without falling off the track). Predominantly recruits 2
CC       dyneins, which increases both the force and speed of the microtubule
CC       motor. Component of secretory vesicle machinery in developing neurons
CC       that acts as a regulator of neurite outgrowth. Regulates the secretory
CC       vesicle transport by controlling the accumulation of Rab6-containing
CC       secretory vesicles in the pericentrosomal region restricting
CC       anterograde secretory transport during the early phase of neuronal
CC       differentiation, thereby inhibiting neuritogenesis.
CC       {ECO:0000250|UniProtKB:A0JNT9}.
CC   -!- SUBUNIT: Part of a tripartite complex with dynein and dynactin, acts an
CC       adapter linking the dynein motor complex and dynactin. Interacts with
CC       KIF1C. Interacts with RAB6A and RAB6B; interaction is specific to Rab6.
CC       {ECO:0000250|UniProtKB:A0JNT9}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton
CC       {ECO:0000250|UniProtKB:A0JNT9}. Cytoplasm, cytoskeleton, microtubule
CC       organizing center, centrosome {ECO:0000250|UniProtKB:A0JNT9}.
CC       Note=Localizes around the centrosome. {ECO:0000250|UniProtKB:A0JNT9}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q6ZP65-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6ZP65-2; Sequence=VSP_056941, VSP_056942;
CC   -!- SIMILARITY: Belongs to the BICDR family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC83181.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAC85259.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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   EMBL; AK129960; BAC85259.1; ALT_SEQ; mRNA.
DR   EMBL; AK301580; BAG63072.1; -; mRNA.
DR   EMBL; AC004812; AAC83181.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AC004815; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   CCDS; CCDS41845.1; -. [Q6ZP65-1]
DR   RefSeq; NP_997194.2; NM_207311.2. [Q6ZP65-1]
DR   AlphaFoldDB; Q6ZP65; -.
DR   SMR; Q6ZP65; -.
DR   BioGRID; 124955; 5.
DR   FunCoup; Q6ZP65; 102.
DR   IntAct; Q6ZP65; 4.
DR   STRING; 9606.ENSP00000380690; -.
DR   GlyGen; Q6ZP65; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q6ZP65; -.
DR   PhosphoSitePlus; Q6ZP65; -.
DR   BioMuta; BICDL1; -.
DR   DMDM; 313104078; -.
DR   jPOST; Q6ZP65; -.
DR   MassIVE; Q6ZP65; -.
DR   PaxDb; 9606-ENSP00000380690; -.
DR   PeptideAtlas; Q6ZP65; -.
DR   ProteomicsDB; 5351; -.
DR   ProteomicsDB; 68060; -. [Q6ZP65-1]
DR   Antibodypedia; 62366; 20 antibodies from 7 providers.
DR   DNASU; 92558; -.
DR   Ensembl; ENST00000397558.6; ENSP00000380690.2; ENSG00000135127.13. [Q6ZP65-1]
DR   GeneID; 92558; -.
DR   KEGG; hsa:92558; -.
DR   UCSC; uc001txl.2; human. [Q6ZP65-1]
DR   AGR; HGNC:28095; -.
DR   ClinPGx; PA143485416; -.
DR   CTD; 92558; -.
DR   DisGeNET; 92558; -.
DR   GeneCards; BICDL1; -.
DR   HGNC; HGNC:28095; BICDL1.
DR   HPA; ENSG00000135127; Tissue enhanced (kidney, pituitary gland).
DR   MIM; 617002; gene.
DR   OpenTargets; ENSG00000135127; -.
DR   VEuPathDB; HostDB:ENSG00000135127; -.
DR   eggNOG; ENOG502QUA9; Eukaryota.
DR   GeneTree; ENSGT00940000157442; -.
DR   HOGENOM; CLU_029068_0_0_1; -.
DR   InParanoid; Q6ZP65; -.
DR   OMA; PRQFGQY; -.
DR   OrthoDB; 9451547at2759; -.
DR   PAN-GO; Q6ZP65; 2 GO annotations based on evolutionary models.
DR   PhylomeDB; Q6ZP65; -.
DR   PathwayCommons; Q6ZP65; -.
DR   SignaLink; Q6ZP65; -.
DR   SIGNOR; Q6ZP65; -.
DR   Agora; ENSG00000135127; -.
DR   BioGRID-ORCS; 92558; 15 hits in 1143 CRISPR screens.
DR   ChiTaRS; BICDL1; human.
DR   GenomeRNAi; 92558; -.
DR   Pharos; Q6ZP65; Tdark.
DR   PRO; PR:Q6ZP65; -.
DR   Proteomes; UP000005640; Chromosome 12.
DR   RNAct; Q6ZP65; protein.
DR   Bgee; ENSG00000135127; Expressed in metanephros cortex and 160 other cell types or tissues.
DR   ExpressionAtlas; Q6ZP65; baseline and differential.
DR   GO; GO:0005813; C:centrosome; ISS:UniProtKB.
DR   GO; GO:0034452; F:dynactin binding; ISS:UniProtKB.
DR   GO; GO:0031267; F:small GTPase binding; ISS:UniProtKB.
DR   GO; GO:0055107; P:Golgi to secretory granule transport; ISS:UniProtKB.
DR   GO; GO:0031175; P:neuron projection development; ISS:UniProtKB.
DR   GO; GO:0047496; P:vesicle transport along microtubule; IBA:GO_Central.
DR   InterPro; IPR060493; BICDL1/2-like_C.
DR   InterPro; IPR051149; Spindly/BICDR_Dynein_Adapter.
DR   PANTHER; PTHR32123; BICD FAMILY-LIKE CARGO ADAPTER; 1.
DR   PANTHER; PTHR32123:SF12; BICD FAMILY-LIKE CARGO ADAPTER 1; 1.
DR   Pfam; PF27654; BICDL2_C; 1.
DR   Pfam; PF28219; Spindly; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Coiled coil; Cytoplasm; Cytoskeleton; Neurogenesis;
KW   Proteomics identification; Reference proteome; Transport.
FT   CHAIN           1..573
FT                   /note="BICD family-like cargo adapter 1"
FT                   /id="PRO_0000302858"
FT   REGION          67..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          386..412
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          118..376
FT                   /evidence="ECO:0000255"
FT   COILED          440..525
FT                   /evidence="ECO:0000255"
FT   MOTIF           113..117
FT                   /note="CC1 box"
FT                   /evidence="ECO:0000250|UniProtKB:A0JNT9"
FT   COMPBIAS        68..77
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        387..396
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   VAR_SEQ         1..351
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056941"
FT   VAR_SEQ         436
FT                   /note="T -> TGSRRLDDDSLEEQIRQTSEDSRALRELMEGERGKLRQSLEELQRLH
FT                   SQ (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_056942"
FT   CONFLICT        79..97
FT                   /note="Missing (in Ref. 1; BAC85259)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   573 AA;  64841 MW;  F514AF0264B13F09 CRC64;
     MSAFCLGLVG RASAPAEPDS ACCMELPAAA GDAVRSPAAA AALIFPGGSG ELELALEEEL
     ALLAAGERPS DPGEHPQAEP GSLAEGAGPQ PPPSQDPELL SVIRQKEKDL VLAARLGKAL
     LERNQDMSRQ YEQMHKELTD KLEHLEQEKH ELRRRFENRE GEWEGRVSEL ESDVKQLQDE
     LERQQIHLRE ADREKSRAVQ ELSEQNQRLL DQLSRASEVE RQLSMQVHAL REDFREKNSS
     TNQHIIRLES LQAEIKMLSD RKRELEHRLS ATLEENDLLQ GTVEELQDRV LILERQGHDK
     DLQLHQSQLE LQEVRLSCRQ LQVKVEELTE ERSLQSSAAT STSLLSEIEQ SMEAEELEQE
     REQLRLQLWE AYCQVRYLCS HLRGNDSADS AVSTDSSMDE SSETSSAKDV PAGSLRTALN
     ELKRLIQSIV DGMEPTVTLL SVEMTALKEE RDRLRVTSED KEPKEQLQKA IRDRDEAIAK
     KNAVELELAK CRMDMMSLNS QLLDAIQQKL NLSQQLEAWQ DDMHRVIDRQ LMDTHLKERS
     QPAAALCRGH SAGRGDEPSI AEGKRLFSFF RKI
//