ID   SYTL2_BOVIN             Reviewed;         943 AA.
AC   A6QP06;
DT   01-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Synaptotagmin-like protein 2;
GN   Name=SYTL2;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC   Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Ascending colon;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: May act as a RAB27A effector protein and play a role in
CC       cytotoxic granule exocytosis in lymphocytes. {ECO:0000250}.
CC   -!- SUBUNIT: Monomer. Binds NRXN1. Binds RAB27A that has been activated by
CC       GTP-binding via its N-terminus. Interacts with RAB27B (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:Q9HCH5}.
CC       Note=In the pancreatic alpha cells distributed in both peripheral and
CC       anterior regions. Localizes on the glucagon granules in the cell
CC       periphery. {ECO:0000250|UniProtKB:Q9HCH5}.
CC   -!- DOMAIN: The RabBD domain mediates interaction with RAB27A.
CC       {ECO:0000250}.
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DR   EMBL; BC149087; AAI49088.1; -; mRNA.
DR   RefSeq; NP_001095748.1; NM_001102278.1.
DR   AlphaFoldDB; A6QP06; -.
DR   SMR; A6QP06; -.
DR   STRING; 9913.ENSBTAP00000030362; -.
DR   PaxDb; A6QP06; -.
DR   PRIDE; A6QP06; -.
DR   GeneID; 614406; -.
DR   KEGG; bta:614406; -.
DR   CTD; 54843; -.
DR   eggNOG; KOG1028; Eukaryota.
DR   InParanoid; A6QP06; -.
DR   OrthoDB; 916843at2759; -.
DR   Proteomes; UP000009136; Unplaced.
DR   GO; GO:0070382; C:exocytic vesicle; IBA:GO_Central.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR   GO; GO:0042043; F:neurexin family protein binding; IBA:GO_Central.
DR   GO; GO:0001786; F:phosphatidylserine binding; IEA:InterPro.
DR   GO; GO:0031267; F:small GTPase binding; IEA:InterPro.
DR   GO; GO:0006887; P:exocytosis; IBA:GO_Central.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
DR   CDD; cd04020; C2B_SLP_1-2-3-4; 1.
DR   Gene3D; 2.60.40.150; -; 2.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR010911; Rab_BD.
DR   InterPro; IPR043567; SYTL1-5_C2B.
DR   InterPro; IPR027006; SYTL2.
DR   PANTHER; PTHR45716:SF5; PTHR45716:SF5; 2.
DR   Pfam; PF00168; C2; 2.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; SSF49562; 2.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS50916; RABBD; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Exocytosis; Membrane; Reference proteome; Repeat.
FT   CHAIN           1..943
FT                   /note="Synaptotagmin-like protein 2"
FT                   /id="PRO_0000382653"
FT   DOMAIN          1..57
FT                   /note="RabBD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00234"
FT   DOMAIN          637..762
FT                   /note="C2 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   DOMAIN          777..906
FT                   /note="C2 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT   REGION          77..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          118..291
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          361..613
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        128..195
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        196..210
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        242..256
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        257..289
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        379..475
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        523..539
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        543..559
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        589..613
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   943 AA;  105851 MW;  AC331752B94D3BB7 CRC64;
     MIDLSFLTEE EQEAIMKVLQ RDAALKRAEE ERVRHLPEKV KDDQQLKNMS GQWFYEAKAK
     RHRDRIHGAD IIRVSMRKKR PQVADEQSKD RANRAKESWV NNVHKDAFLP PELTGVVEEP
     EEDVAPASPS SSVVNPVSTM IDASQENTRK SAISPAKPRK NPFNSSMLPE DHLSQQTKNE
     QSKNGKTGLF QTSKEGELSE SKEESSILDI SSQKLEKPKQ TLPGPESGFP IKAPVPKPRK
     MIYKSQDLKQ DDNQPFPRQR TDSLTTRGAP RGILKRNSSS SSTDSETVRF HQNFEPKSKI
     VSLGLTIHER ISEKEHSLED DSPSNSLEPL KHVRFSAVKD ELPQSSGLVH GREVGEFSVL
     ESDRLKNGTE DAGLTDEVWN DPQPSQYTNG LPFQSSASSP SPSKNETSQP TTSGSFPINE
     HPSSKEFLTT RAQSTENSHT INEHKTSSSE LSKNPADELS CTEPESSQVP DCSSRDHQQG
     SEEEPSPVLK ILERSAARKM PSKSLEDISS DSSNQAKVDN LPEELVRSAE DDQKADQEPD
     TNECIPGIST VSSQPDNQFS HPDKLKRMSK SVPAFLQDES DDRETDTASE GSYQLSRHKK
     SPSSLTNLSS NSGMTSLSSV SGSVMSVYSG DFGNLEVKGS IQFAIDYVDS LKELHVFVAQ
     CKDLAAADIK KQRSDPYVKT YLLPDKGKMG KKKTLVVKKT LNPVYNEILR YKINKQILKT
     QKLNLSVWHR DTFKRNSFLG EVELDLETWD WDNKQNKQLK WYPLKRKTAP VPLEAENRGE
     MKLALQYVPE PVPGKKLPTT GEVHIWVKEC LDLPLLRGSH LNSFVKCTIL PDTSRKSRQK
     TRAVGKTTNP VFNHTMVYDG FRPEDLTEAC VELTVWDHYK LTNQFLGGLR IGFGTGKSYG
     TEVDWMDSTS EEVALWEKMV KSPNTWIEAI LPLRMLLIAK ISK