KTN1_CHICK
ID KTN1_CHICK Reviewed; 1364 AA.
AC Q90631;
DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Kinectin;
GN Name=KTN1;
OS Gallus gallus (Chicken).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Galloanserae; Galliformes; Phasianidae;
OC Phasianinae; Gallus.
OX NCBI_TaxID=9031;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-12 AND 233-247.
RC STRAIN=Leghorn; TISSUE=Brain;
RX PubMed=7787244; DOI=10.1091/mbc.6.2.171;
RA Yu H., Nicchitta C.V., Kumar J., Becker M., Toyoshima I., Sheetz M.P.;
RT "Characterization of kinectin, a kinesin-binding protein: primary sequence
RT and N-terminal topogenic signal analysis.";
RL Mol. Biol. Cell 6:171-183(1995).
RN [2]
RP SUBUNIT, AND MYRISTOYLATION.
RX PubMed=9822636; DOI=10.1074/jbc.273.48.31738;
RA Kumar J., Erickson H.P., Sheetz M.P.;
RT "Ultrastructural and biochemical properties of the 120-kDa form of chick
RT kinectin.";
RL J. Biol. Chem. 273:31738-31743(1998).
CC -!- FUNCTION: Receptor for kinesin thus involved in kinesin-driven vesicle
CC motility.
CC -!- SUBUNIT: Parallel homodimers formed between the membrane-bound and the
CC cytosolic form, and also between 2 cytosolic forms.
CC {ECO:0000269|PubMed:9822636}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane; Single-pass type
CC II membrane protein. Note=Vesicle membrane protein anchored to the
CC endoplasmic reticulum.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced.;
CC Name=1;
CC IsoId=Q90631-1; Sequence=Displayed;
CC -!- PTM: Both the membrane and cytoplasmic forms seem to be myristoylated.
CC {ECO:0000269|PubMed:9822636}.
CC -!- MISCELLANEOUS: A cytoplasmic form lacking the first 232 amino acids has
CC been characterized.
CC -!- SIMILARITY: Belongs to the kinectin family. {ECO:0000305}.
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DR EMBL; U15617; AAA85818.1; -; mRNA.
DR RefSeq; NP_990707.1; NM_205376.1. [Q90631-1]
DR AlphaFoldDB; Q90631; -.
DR SMR; Q90631; -.
DR STRING; 9031.ENSGALP00000004048; -.
DR PaxDb; Q90631; -.
DR GeneID; 396335; -.
DR KEGG; gga:396335; -.
DR CTD; 3895; -.
DR VEuPathDB; HostDB:geneid_396335; -.
DR eggNOG; ENOG502QSIW; Eukaryota.
DR InParanoid; Q90631; -.
DR PhylomeDB; Q90631; -.
DR PRO; PR:Q90631; -.
DR Proteomes; UP000000539; Unplaced.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:InterPro.
DR GO; GO:0019894; F:kinesin binding; IEA:InterPro.
DR GO; GO:0007018; P:microtubule-based movement; IEA:InterPro.
DR GO; GO:0015031; P:protein transport; IEA:InterPro.
DR InterPro; IPR024854; Kinectin.
DR InterPro; IPR007794; Rib_rcpt_KP.
DR PANTHER; PTHR18864; PTHR18864; 1.
DR Pfam; PF05104; Rib_recp_KP_reg; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Coiled coil; Direct protein sequencing;
KW Endoplasmic reticulum; Glycoprotein; Lipoprotein; Membrane; Myristate;
KW Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..1364
FT /note="Kinectin"
FT /id="PRO_0000084336"
FT TOPO_DOM 1..6
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..29
FT /note="Helical; Signal-anchor for type II membrane protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..1364
FT /note="Lumenal"
FT /evidence="ECO:0000255"
FT REGION 46..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 315..1085
FT /evidence="ECO:0000255"
FT COILED 1116..1306
FT /evidence="ECO:0000255"
FT COMPBIAS 63..90
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CARBOHYD 202
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 267
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 623
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 638
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 704
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 775
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 976
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1061
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1088
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 1094
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 1364 AA; 155976 MW; 176BB11A19A80F00 CRC64;
MEFYESTYFI ILIPSVVITV IFLFFWLFMK ETLYDEVLAK QKRDLKFPPT KSDKKKTEKK
KNKKKEAQNG NIHESDSEST PRDFKLSDAL GTDEEQVAPV PLSATEASAG IRERKKKEKK
QKAAQDDHVT KESEGSKSSG KKVEPVPVTK QPTPPSEPAA AKKKPGQKKQ KNDDQDTKTD
SVASPAKKQE PVLLHQEVKQ ENVSGKKKVS AKKQKVLVDE PLIQPTTYIP LVDNSDAGAL
EKREVVEVAK QNMNEGIQKS GGKKMKNETD KENAEVKFKD FVMAMKNMIF TEDEARCVVE
VLKEKSGAIH DVLQKASKAE SAAAIHQLQD KEKLLAAVKE EAAVAKEQCK QLTQELVAEK
ERNGLLTAKM RERINALEKE HGTFQSKIHV SYQESQQMKI KFQQRCEQME AEISHLKQEN
TILRDAVSTS TNQMESKQAA ELNKLRQDCA RLVNELGEKN SKLQQEELQK KNAEQAVAQL
KVQQQEAERR WEEIQVYLRK RTAEHEAAQQ DVQNKLVAKD NEIQSLHSKL TDMVVSKQQL
EQRMLQLIES EQKRASKEDS MQLRVQELVE QNDALNAQLQ KLHSQMAAQT SASVLAEELH
KVIAEKDKQL KQMEDSLGNE HANLTSKEEE LKVLQNMNLS LKSEIQKLQA LTNEQAAAAH
ELERMQKSIH IKDDKIRTLE EQLREELAQT VNTKEEFKIL KDQNKTLQAE VQKLQALLSE
PVQPTFEANK DLLEEMERGM RERDDKIKTV EELLEAGLIQ MANKEEELKV LRTENSSLRK
ELQSLQIQLS EQVSFQSLVD ELQKVIHEKD GKIKSVEELL QAEILKVANK EKTVQALTQK
IEALKEEVGN SQLEMEKQVS ITSQVKELQT LLKGKENQVK TMEALLEEKE KEIVQKGERL
KGQQDTVAQL TSKVQELEQQ NLQQLQQVPA ASQVQDLESR LRGEEEQISK LKAVLEEKER
EIASQVKQLQ TMQSENESFK VQIQELKQEN CKQASLAVQS EELLQVVAGK EKEIASLQNE
LACQRNAFEQ QRKKNNDLRE KNWKAMEALA STEKLLQDKV NKTAKEKQQH VEAAEVETRE
LLQKLFPNVS LPANVSHSEW ICGFEKMAKE YLRGASGSED IKVMEQKLKE AEELHILLQL
ECEKYKSVLA ETEGILQRLQ RSVEEEESKW KIKVEESQKE LKQMRSSVAS LEHEVERLKE
EIKEVETLKK EREHLESELE KAEIERSTYV SEVRELKDLL TELQKKLDDS YSEAVRQNEE
LNLLKMKLSE TLSKLKVDQN ERQKVAGDLP KAQESLASLE REIGKVVGDA NVIENSDVRT
ESELTDKRLN VAVNLNQDVG HLKKLLVSVS QMLSKGREHY QLVE
